In a study published in the Journal of Endocrinology, IL-15 doubled the rate of hypertrophy in skeletal mussle tissue. The same study showed that stacking IL-15 with IGF-1 increased muscular hypertrophy by 500%. I understand only a few BB have tried this stack and the results are amazing. Does any one have any other info reguarding this compound ? Has anyone used it? And where can it be VIEWED?
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Interleukin-15 (IL-15)
- Thread starter yardrock
- Start date
- Joined
- Aug 29, 2003
- Messages
- 5,165
Its the first time im hearin about this stuff, you better believe i want all the info i can find on it. Post up some more info or links where we can learn about it. Tell us as much as you can about it. Administration, storeage, time on/off it, etc...
- Joined
- Jul 31, 2003
- Messages
- 770
I did some research on it last year, and found that the side effects are very bad. Brain damage in some animals they used it on. When you read research make sure you know how to interpret right. Like the other day I posted the big thread on tendons and the supplements that can help build them stronger. But once I looked more into it I realized that the supplements in the article only effect the Type III coll. and that only represents 9% of the overall tendon. So look very close and also look where the study was done.
Here are a couple of links. Looks like a good place to RESEARCH IGF-1 also. www.promocell.com and www.bioclone.com
- Joined
- Feb 21, 2003
- Messages
- 715
Blood. 1998 Dec 15;92(12):4828-35. Related Articles, Links
Interleukin-15 (IL-15) induces NF-kappaB activation and IL-8 production in human neutrophils.
McDonald PP, Russo MP, Ferrini S, Cassatella MA.
Department of General Pathology, University of Verona, Verona, Italy. [email protected]
Interleukin-2 (IL-2) and IL-15 exert similar biological actions, which largely reflect the fact that their receptors share common beta and gamma subunits; in contrast, distinct subunits are required for high-affinity binding of either cytokine to a heterotrimeric receptor complex. Human neutrophils are known to express both the beta and gamma subunits of the IL-2/IL-15 receptor complex, and we now report that they also constitutively express messenger RNA transcripts encoding the IL-15 receptor chain, suggesting that they possess functional, heterotrimeric IL-15 receptors. Accordingly, we show that in neutrophils, IL-15 elicits several functional responses. In particular, neutrophils synthesize and release IL-8 in response to IL-15, but not to IL-2. Moreover, a nuclear factor-kappaB (NF-kappaB) DNA-binding activity was enhanced in nuclear extracts of IL-15-treated neutrophils, which could be supershifted by antibodies to p50 or RelA. Again, no detectable effect of IL-2 was observed on this response. In peripheral blood lymphocytes (PBL), however, both IL-2 and IL-15 were potent inducers of NF-kappaB activation. Conversely, neither IL-15 nor IL-2 elicited the formation of activator protein-1 (AP-1) DNA-binding complexes in neutrophils, even though both cytokines were found to activate these DNA-binding activities in PBL. Collectively, these observations establish neutrophils as a useful cellular model to discriminate between the actions of IL-15 and IL-2. More importantly, this is the first demonstration that IL-15 has the ability to induce NF-kappaB and AP-1 activation, which further emphasizes the potential relevance of this newly discovered cytokine to immune and inflammatory processes.
PMID: 9845550 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov/entrez/...eve&db=PubMed&list_uids=9845550&dopt=Abstract
Overview
Interleukin 15 (IL-15) is a novel cytokine that shares many biological properties with, but lacks amino acid sequence homology to, IL-2. IL-15 was originally identified in media conditioned by a monkey kidney eipthelial cell line (CVI/EBNA) based on its mitogenic activity on the murine T cell line, CTLL-2 (1). IL-15 was also independently discovered as a cytokine produced by a human adult T cell leukemia cell line (HuT-102) that stimulated T cell proliferation and was designated IL-T (2).
Fig. 1. A structural comparison between the IL-15R alpha and the IL-2R alpha (adapted from Giri, J.G. et al. (1995) EMBO J. 14:3654). Disulfide bridges characteristic of the sushi domain are shown.
Structural Information
Human, simian and mouse IL-15 cDNA, as well as human and mouse IL-15 genomic clones, have been isolated and characterized (1, 3, 4). The IL-15 cDNA clones from all three species encode a 162 amino acid (aa) residue precursor protein containing a 48 aa residue leader that is cleaved to generate the 114 aa residue mature IL-15. Human IL-15 shares approximately 97% and 73% sequence identity with simian and mouse IL-15, respectively. Both human and simian IL-15 are active on mouse cells. Although the structure of IL-15 has not been determined, it is predicted to be similar to IL-2 and other members of the four-helix bundle cytokine family (3, 5).
Receptor
High-affinity cell surface receptors for IL-15 have been detected on a variety of T cells and B cells, as well as non-lymphoid cells (7, 8). It has been demonstrated that the beta and the gamma common chain subunits of the IL-2 high-affinity receptor complex are also required for IL-15 signal transduction and efficient internalization (8). Recently, a novel mouse IL-15-specific binding protein (IL-15R alpha) that is structurally related to the alpha subunit of the IL-2 high-affinity receptor has been cloned and characterized (8). IL-15R alpha shares structural similarities with the IL-2R alpha and both proteins contain the short consensus "sushi domain" repeats. Whereas both human and simian IL-15 can bind to a complex of the human beta and gamma common chain subunits in the absence of the mouse IL-15R alpha subunit, simian IL-15 is not capable of binding to and transducing IL-15 signals through the mouse beta and gamma common chain complex alone. Soluble human IL-2R beta appears to bind human IL-15 with sufficiently high affinity such that it is an excellent IL-15 antagonist (9).
Biological Effects
IL-15 mRNAs have been detected in a number of human tissues and cell types, including heart, lung, liver, placenta, skeletal muscle, adherent peripheral blood mononuclear cells, and epithelial and fibroblast cell lines. However, IL-15 mRNA is not detectable in activated peripheral blood T cells that contain high levels of IL-2 mRNA (1). The IL-15 mRNA from normal cells has been shown to contain 10 upstream AUGs that attenuate IL-15 mRNA translation (4). Thus, in spite of the high levels of IL-15 mRNA present in adherent peripheral blood mononuclear cells, IL-15 protein is not detectable in the culture supernatant using a sensitive ELISA (6).
IL-15 has biological activities similar to IL-2 and has been shown to stimulate the growth of natural killer cells, activated peripheral blood T lymphocytes (1, 7, 8), tumor infiltrating lymphocytes (TILs) (10), and B cells (11). In addition, IL-15 has also been shown to be a chemoattractant for human blood T lymphocytes (12) and to be able to induce lymphokine-activated killer (LAK) activity in NK cells as well as to be able to induce the generation of cytolytic effector cells. It is likely that additional, as yet unidentified, functions for IL-15 will be discovered in the future.
Clinical Interest
By virtue of its activity as a stimulator of T cells, NK cells, LAK cells, and TILs, IL-2 is currently in clinical trials testing its potential use in treatments for cancer and for viral infections. Because of its similar biological activities, IL-15 should have similar therapeutic potential.
References
1. Grabstein, K. et al. (1994) Science 264:965
2. Burton, J.C. et al. (1994) Proc. Natl. Acad. Aci. USA 91:4935
3. Anderson, D.M. et al. (1995) Genomics 25:701
4. Bamford, R.N. et al. (1995) Cytokine 7:595
5. Brandhuber, B.J. et al. (1987) Science 238:1707
6. R&&D Systems, unpublished results
7. Giri, J.G. et al. (1994) EMBO J. 13:2822
8. Giri, J.G. et al. (1995) EMBO J. 15:3654
9. R&D Systems, unpublished results
10. Lewko,W. M. et al. (1995) Cancer Biother. 10:13
11. Armitage, R.J. et al. (1995) J. Immunol. 154:483
12. P. Wilkinson and F. Liew (1995) J. Exp. Med. 181:1255
Cytokines, Growth Factors & Chemokines:ANTIBODIES
(anti-Human and others as indicated)
Research Diagnostics Inc offers a wide line of recombinant growth factors, cytokines and chemokines and antibodies. Since no one antibody works best for all applications (neutralization, blotting, ELISA, etc), we offer many different types of antibodies to help solve this problem. Please inquire for other applications or types of antibodies not listed below.
--------------------------------------------------------------------------------
IL-15 (INTERLEUKIN 15)
see below anit-human, anti-mouse and anti-rat antibodies
--------------------------------------------------------------------------------
Rabbit anti-human IL-15(antigen aff pure, lyophilized, no carrier/no preservative)
cat#RDI-IL15abrP $170.00/50ug
cat#RDI-IL15abrP1 $240.00/100ug
Rabbit anti-human IL-15:Biotin conjugated (antigen aff pure, conjugated toBiotin, lyophilized, carrier free)
cat#RDI-IL15abrPB $170.00/25ug
cat#RDI-IL15abrPB1 $240.00/50ug
Mouse anti-human IL-15 500ug lyophilized
cat#RDI-IL15abmXP $250.00 Bulk on request
--------------------------------------------------------------------------------
Purified Rabbit Anti-mouse IL-15
cat# RDI-MIL15abr $350.00
Packaging: 200ug Purified rabbit immunoglobulins, lyophilized (Reconstitute to 1 mg/ml by adding 200 ul PBS; contains 0.1% sodium azide)
Immunogen: E. coli-expressed mouse IL-15
Use: 0.5-1ug/ml with chemiluminescence detection Western blot detection of mouse IL-15
Cross-reactivity to IL-15 of other species has not been determined.
Storage: 4°C for short term storage or -20°C in small aliquots for long term storage. Avoid repeated freeze and thaw.
Background: IL-15 is 14-15 kDa, a member of the four alpha-helical bundle family of cytokines. It is very similar to IL-2, except that IL-15 has an IL-15 alpha receptor subunit 1. It plays an important role in the growth and differentiation of T and B lymphocytes, natural killer cells, macrophages, and monocytes as well as activation of a number of important intracellular signaling molecules 2. This implies that IL-15 could be essential for the immune responses, allograft rejection, and the pathogenesis of autoimmune diseases 3.
References:
1. Cosman, D, et al. (1995) Interleukin 15 and its receptor. Ciba Found Symp 1955:221-9
2. Waldmann, T, et al. (1998) Interleukin-2, interleukin-15 and their receptors. Int Rev Immunol 16 (3-4): 205-26
3. Kennedy, MK, et al. (1996) Characterization of interleukin-15 (IL-15) and the IL-15 receptor complex. J Clin Immunol 16 (3): 134-43
For Research Use Only
Goat anti-mouse IL-15 (in development)
--------------------------------------------------------------------------------
Purified Rabbit Anti-RAT IL-15
cat# RDI-RTIL15Babr $350.00
Packaging: 200ug Purified rabbit immunoglobulins, lyophilized (Reconstitute to 1 mg/ml by adding 200 ul PBS; contains 0.1% sodium azide)
Immunogen: E. coli-expressed rat IL-15 (aa 104-162)
Use: 0.5-1ug/ml with chemiluminescence detection Western blot detection of rat IL-15
Cross-reactivity to IL-15 of other species has not been determined.
Storage: 4°C for short term storage or -20°C in small aliquots for long term storage. Avoid repeated freeze and thaw.
Background: IL-15 is 14-15 kDa, a member of the four alpha-helical bundle family of cytokines. It is very similar to IL-2, except that IL-15 has an IL-15 alpha receptor subunit 1. It plays an important role in the growth and differentiation of T and B lymphocytes, natural killer cells, macrophages, and monocytes as well as activation of a number of important intracellular signaling molecules 2. This implies that IL-15 could be essential for the immune responses, allograft rejection, and the pathogenesis of autoimmune diseases 3.
References: 1. Cosman, D, et al. (1995) Interleukin 15 and its receptor. Ciba Found Symp 1955:221-9
2. Waldmann, T, et al. (1998) Interleukin-2, interleukin-15 and their receptors. Int Rev Immunol 16 (3-4): 205-26
3. Kennedy, MK, et al. (1996) Characterization of interleukin-15 (IL-15) and the IL-15 receptor complex. J Clin Immunol 16 (3): 134-43
For Research Use Only
--------------------------------------------------------------------------------
Purified Rabbit Anti-RAT IL-15-A (less sensitive than RDI-RTIL15Babr)
cat# RDI-RTIL15Aabr $350.00
Packaging: 200ug Purified rabbit immunoglobulins, lyophilized (Reconstitute to 1 mg/ml by adding 200 ul PBS; contains 0.1% sodium azide
Immunogen: E. coli-expressed rat IL-15 (aa 52-103)
Use: 0.5-1ug/ml with chemiluminescence detection Western blot detection of rat IL-15
Cross-reactivity to IL-15 of other species has not been determined.
--------------------------------------------------------------------------------
Research Diagnostics Inc
Pleasant Hill Road
Flanders NJ 07836
phone (800) 631-9384 or (973) 584-7093
fax (973) 584-0210
EMAIL:[email protected]
Ordering terms
**broken link removed**
Interleukin-15 (IL-15) induces NF-kappaB activation and IL-8 production in human neutrophils.
McDonald PP, Russo MP, Ferrini S, Cassatella MA.
Department of General Pathology, University of Verona, Verona, Italy. [email protected]
Interleukin-2 (IL-2) and IL-15 exert similar biological actions, which largely reflect the fact that their receptors share common beta and gamma subunits; in contrast, distinct subunits are required for high-affinity binding of either cytokine to a heterotrimeric receptor complex. Human neutrophils are known to express both the beta and gamma subunits of the IL-2/IL-15 receptor complex, and we now report that they also constitutively express messenger RNA transcripts encoding the IL-15 receptor chain, suggesting that they possess functional, heterotrimeric IL-15 receptors. Accordingly, we show that in neutrophils, IL-15 elicits several functional responses. In particular, neutrophils synthesize and release IL-8 in response to IL-15, but not to IL-2. Moreover, a nuclear factor-kappaB (NF-kappaB) DNA-binding activity was enhanced in nuclear extracts of IL-15-treated neutrophils, which could be supershifted by antibodies to p50 or RelA. Again, no detectable effect of IL-2 was observed on this response. In peripheral blood lymphocytes (PBL), however, both IL-2 and IL-15 were potent inducers of NF-kappaB activation. Conversely, neither IL-15 nor IL-2 elicited the formation of activator protein-1 (AP-1) DNA-binding complexes in neutrophils, even though both cytokines were found to activate these DNA-binding activities in PBL. Collectively, these observations establish neutrophils as a useful cellular model to discriminate between the actions of IL-15 and IL-2. More importantly, this is the first demonstration that IL-15 has the ability to induce NF-kappaB and AP-1 activation, which further emphasizes the potential relevance of this newly discovered cytokine to immune and inflammatory processes.
PMID: 9845550 [PubMed - indexed for MEDLINE]
http://www.ncbi.nlm.nih.gov/entrez/...eve&db=PubMed&list_uids=9845550&dopt=Abstract
Overview
Interleukin 15 (IL-15) is a novel cytokine that shares many biological properties with, but lacks amino acid sequence homology to, IL-2. IL-15 was originally identified in media conditioned by a monkey kidney eipthelial cell line (CVI/EBNA) based on its mitogenic activity on the murine T cell line, CTLL-2 (1). IL-15 was also independently discovered as a cytokine produced by a human adult T cell leukemia cell line (HuT-102) that stimulated T cell proliferation and was designated IL-T (2).
Fig. 1. A structural comparison between the IL-15R alpha and the IL-2R alpha (adapted from Giri, J.G. et al. (1995) EMBO J. 14:3654). Disulfide bridges characteristic of the sushi domain are shown.
Structural Information
Human, simian and mouse IL-15 cDNA, as well as human and mouse IL-15 genomic clones, have been isolated and characterized (1, 3, 4). The IL-15 cDNA clones from all three species encode a 162 amino acid (aa) residue precursor protein containing a 48 aa residue leader that is cleaved to generate the 114 aa residue mature IL-15. Human IL-15 shares approximately 97% and 73% sequence identity with simian and mouse IL-15, respectively. Both human and simian IL-15 are active on mouse cells. Although the structure of IL-15 has not been determined, it is predicted to be similar to IL-2 and other members of the four-helix bundle cytokine family (3, 5).
Receptor
High-affinity cell surface receptors for IL-15 have been detected on a variety of T cells and B cells, as well as non-lymphoid cells (7, 8). It has been demonstrated that the beta and the gamma common chain subunits of the IL-2 high-affinity receptor complex are also required for IL-15 signal transduction and efficient internalization (8). Recently, a novel mouse IL-15-specific binding protein (IL-15R alpha) that is structurally related to the alpha subunit of the IL-2 high-affinity receptor has been cloned and characterized (8). IL-15R alpha shares structural similarities with the IL-2R alpha and both proteins contain the short consensus "sushi domain" repeats. Whereas both human and simian IL-15 can bind to a complex of the human beta and gamma common chain subunits in the absence of the mouse IL-15R alpha subunit, simian IL-15 is not capable of binding to and transducing IL-15 signals through the mouse beta and gamma common chain complex alone. Soluble human IL-2R beta appears to bind human IL-15 with sufficiently high affinity such that it is an excellent IL-15 antagonist (9).
Biological Effects
IL-15 mRNAs have been detected in a number of human tissues and cell types, including heart, lung, liver, placenta, skeletal muscle, adherent peripheral blood mononuclear cells, and epithelial and fibroblast cell lines. However, IL-15 mRNA is not detectable in activated peripheral blood T cells that contain high levels of IL-2 mRNA (1). The IL-15 mRNA from normal cells has been shown to contain 10 upstream AUGs that attenuate IL-15 mRNA translation (4). Thus, in spite of the high levels of IL-15 mRNA present in adherent peripheral blood mononuclear cells, IL-15 protein is not detectable in the culture supernatant using a sensitive ELISA (6).
IL-15 has biological activities similar to IL-2 and has been shown to stimulate the growth of natural killer cells, activated peripheral blood T lymphocytes (1, 7, 8), tumor infiltrating lymphocytes (TILs) (10), and B cells (11). In addition, IL-15 has also been shown to be a chemoattractant for human blood T lymphocytes (12) and to be able to induce lymphokine-activated killer (LAK) activity in NK cells as well as to be able to induce the generation of cytolytic effector cells. It is likely that additional, as yet unidentified, functions for IL-15 will be discovered in the future.
Clinical Interest
By virtue of its activity as a stimulator of T cells, NK cells, LAK cells, and TILs, IL-2 is currently in clinical trials testing its potential use in treatments for cancer and for viral infections. Because of its similar biological activities, IL-15 should have similar therapeutic potential.
References
1. Grabstein, K. et al. (1994) Science 264:965
2. Burton, J.C. et al. (1994) Proc. Natl. Acad. Aci. USA 91:4935
3. Anderson, D.M. et al. (1995) Genomics 25:701
4. Bamford, R.N. et al. (1995) Cytokine 7:595
5. Brandhuber, B.J. et al. (1987) Science 238:1707
6. R&&D Systems, unpublished results
7. Giri, J.G. et al. (1994) EMBO J. 13:2822
8. Giri, J.G. et al. (1995) EMBO J. 15:3654
9. R&D Systems, unpublished results
10. Lewko,W. M. et al. (1995) Cancer Biother. 10:13
11. Armitage, R.J. et al. (1995) J. Immunol. 154:483
12. P. Wilkinson and F. Liew (1995) J. Exp. Med. 181:1255
Cytokines, Growth Factors & Chemokines:ANTIBODIES
(anti-Human and others as indicated)
Research Diagnostics Inc offers a wide line of recombinant growth factors, cytokines and chemokines and antibodies. Since no one antibody works best for all applications (neutralization, blotting, ELISA, etc), we offer many different types of antibodies to help solve this problem. Please inquire for other applications or types of antibodies not listed below.
--------------------------------------------------------------------------------
IL-15 (INTERLEUKIN 15)
see below anit-human, anti-mouse and anti-rat antibodies
--------------------------------------------------------------------------------
Rabbit anti-human IL-15(antigen aff pure, lyophilized, no carrier/no preservative)
cat#RDI-IL15abrP $170.00/50ug
cat#RDI-IL15abrP1 $240.00/100ug
Rabbit anti-human IL-15:Biotin conjugated (antigen aff pure, conjugated toBiotin, lyophilized, carrier free)
cat#RDI-IL15abrPB $170.00/25ug
cat#RDI-IL15abrPB1 $240.00/50ug
Mouse anti-human IL-15 500ug lyophilized
cat#RDI-IL15abmXP $250.00 Bulk on request
--------------------------------------------------------------------------------
Purified Rabbit Anti-mouse IL-15
cat# RDI-MIL15abr $350.00
Packaging: 200ug Purified rabbit immunoglobulins, lyophilized (Reconstitute to 1 mg/ml by adding 200 ul PBS; contains 0.1% sodium azide)
Immunogen: E. coli-expressed mouse IL-15
Use: 0.5-1ug/ml with chemiluminescence detection Western blot detection of mouse IL-15
Cross-reactivity to IL-15 of other species has not been determined.
Storage: 4°C for short term storage or -20°C in small aliquots for long term storage. Avoid repeated freeze and thaw.
Background: IL-15 is 14-15 kDa, a member of the four alpha-helical bundle family of cytokines. It is very similar to IL-2, except that IL-15 has an IL-15 alpha receptor subunit 1. It plays an important role in the growth and differentiation of T and B lymphocytes, natural killer cells, macrophages, and monocytes as well as activation of a number of important intracellular signaling molecules 2. This implies that IL-15 could be essential for the immune responses, allograft rejection, and the pathogenesis of autoimmune diseases 3.
References:
1. Cosman, D, et al. (1995) Interleukin 15 and its receptor. Ciba Found Symp 1955:221-9
2. Waldmann, T, et al. (1998) Interleukin-2, interleukin-15 and their receptors. Int Rev Immunol 16 (3-4): 205-26
3. Kennedy, MK, et al. (1996) Characterization of interleukin-15 (IL-15) and the IL-15 receptor complex. J Clin Immunol 16 (3): 134-43
For Research Use Only
Goat anti-mouse IL-15 (in development)
--------------------------------------------------------------------------------
Purified Rabbit Anti-RAT IL-15
cat# RDI-RTIL15Babr $350.00
Packaging: 200ug Purified rabbit immunoglobulins, lyophilized (Reconstitute to 1 mg/ml by adding 200 ul PBS; contains 0.1% sodium azide)
Immunogen: E. coli-expressed rat IL-15 (aa 104-162)
Use: 0.5-1ug/ml with chemiluminescence detection Western blot detection of rat IL-15
Cross-reactivity to IL-15 of other species has not been determined.
Storage: 4°C for short term storage or -20°C in small aliquots for long term storage. Avoid repeated freeze and thaw.
Background: IL-15 is 14-15 kDa, a member of the four alpha-helical bundle family of cytokines. It is very similar to IL-2, except that IL-15 has an IL-15 alpha receptor subunit 1. It plays an important role in the growth and differentiation of T and B lymphocytes, natural killer cells, macrophages, and monocytes as well as activation of a number of important intracellular signaling molecules 2. This implies that IL-15 could be essential for the immune responses, allograft rejection, and the pathogenesis of autoimmune diseases 3.
References: 1. Cosman, D, et al. (1995) Interleukin 15 and its receptor. Ciba Found Symp 1955:221-9
2. Waldmann, T, et al. (1998) Interleukin-2, interleukin-15 and their receptors. Int Rev Immunol 16 (3-4): 205-26
3. Kennedy, MK, et al. (1996) Characterization of interleukin-15 (IL-15) and the IL-15 receptor complex. J Clin Immunol 16 (3): 134-43
For Research Use Only
--------------------------------------------------------------------------------
Purified Rabbit Anti-RAT IL-15-A (less sensitive than RDI-RTIL15Babr)
cat# RDI-RTIL15Aabr $350.00
Packaging: 200ug Purified rabbit immunoglobulins, lyophilized (Reconstitute to 1 mg/ml by adding 200 ul PBS; contains 0.1% sodium azide
Immunogen: E. coli-expressed rat IL-15 (aa 52-103)
Use: 0.5-1ug/ml with chemiluminescence detection Western blot detection of rat IL-15
Cross-reactivity to IL-15 of other species has not been determined.
--------------------------------------------------------------------------------
Research Diagnostics Inc
Pleasant Hill Road
Flanders NJ 07836
phone (800) 631-9384 or (973) 584-7093
fax (973) 584-0210
EMAIL:[email protected]
Ordering terms
**broken link removed**
- Joined
- Feb 21, 2003
- Messages
- 715
**broken link removed**
DESCRIPTION: Interleukin-15 (IL-15) is a potent lymphoid cell growth factor which exerts its biological activities primarily on T-cells. Human IL-15 is a 12.9 kDa protein containing 114 amino acid residues.
APPLICATIONS: For most in vitro applications, IL-15 exerts its biological activity in the concentration range of 0.1 to 10 ng/mL. Responding cells are (partial list): T-cells, NK cells, LAK cells.
ACTIVITY: Human IL-15 is fully biologically active when compared to standards. The ED(50) as determined by the dose-dependent proliferation of CTLL-2 cells was found to be <= 0.5 ng/mL, corresponding to a specific activity of >= 2 x 10(E6) units/mg.
PURITY: Greater than 98% by SDS-PAGE and HPLC analyses
SOURCE: E.coli
PRESENTATION: Protein lyophilized from 20mM Tris, pH 8.0.
STORAGE/HANDLING: The lyophilized powder, though stable at room temperature, is best stored desiccated below 0°C. Reconstitute in water to a concentration 100 mg/uL. This solution can be diluted into water or other buffered solutions. Reconstituted IL-15 should be stored in working aliquots at -20°C. Avoid repeated freeze/thaw cycles.
DESCRIPTION: Interleukin-15 (IL-15) is a potent lymphoid cell growth factor which exerts its biological activities primarily on T-cells. Human IL-15 is a 12.9 kDa protein containing 114 amino acid residues.
APPLICATIONS: For most in vitro applications, IL-15 exerts its biological activity in the concentration range of 0.1 to 10 ng/mL. Responding cells are (partial list): T-cells, NK cells, LAK cells.
ACTIVITY: Human IL-15 is fully biologically active when compared to standards. The ED(50) as determined by the dose-dependent proliferation of CTLL-2 cells was found to be <= 0.5 ng/mL, corresponding to a specific activity of >= 2 x 10(E6) units/mg.
PURITY: Greater than 98% by SDS-PAGE and HPLC analyses
SOURCE: E.coli
PRESENTATION: Protein lyophilized from 20mM Tris, pH 8.0.
STORAGE/HANDLING: The lyophilized powder, though stable at room temperature, is best stored desiccated below 0°C. Reconstitute in water to a concentration 100 mg/uL. This solution can be diluted into water or other buffered solutions. Reconstituted IL-15 should be stored in working aliquots at -20°C. Avoid repeated freeze/thaw cycles.
- Joined
- Feb 21, 2003
- Messages
- 715
1: Nagamura-Inoue T, Mori Y, Yizhou Z, Watanabe N, Takahashi TA. Related Articles, Links
Differential expansion of umbilical cord blood mononuclear cell-derived natural killer cells dependent on the dose of interleukin-15 with Flt3L.
Exp Hematol. 2004 Feb;32(2):202-209.
PMID: 15102482 [PubMed - as supplied by publisher]
2: Kim WU, Cho ML, Jung YO, Min SY, Park SW, Min DJ, Yoon JH, Kim HY. Related Articles, Links
Type II collagen autoimmunity in rheumatoid arthritis.
Am J Med Sci. 2004 Apr;327(4):202-11.
PMID: 15084916 [PubMed - in process]
3: Kim JV, Latouche JB, Riviere I, Sadelain M. Related Articles, Links
The ABCs of artificial antigen presentation.
Nat Biotechnol. 2004 Apr;22(4):403-10.
PMID: 15060556 [PubMed - in process]
4: Bernard J, Harb C, Mortier E, Quemener A, Meloen RH, Vermot-Desroches C, Wijdeness J, Van Dijken P, Grotzinger J, Slootstra JW, Plet A, Jacques Y. Related Articles, Links
Identification of an interleukin-15 alpha receptor binding site on human interleukin-15.
J Biol Chem. 2004 Mar 23 [Epub ahead of print]
PMID: 15039446 [PubMed - as supplied by publisher]
5: Forcina G, D'Ettorre G, Mastroianni CM, Carnevalini M, Scorzolini L, Ceccarelli G, D'Agostino C, Lichtner M, Massetti AP, Vullo V. Related Articles, Links
Interleukin-15 modulates interferon-gamma and beta-chemokine production in patients with HIV infection: implications for immune-based therapy.
Cytokine. 2004 Mar 21;25(6):283-90.
PMID: 15036244 [PubMed - in process]
6: Mastroianni CM, d'Ettorre G, Forcina G, Vullo V. Related Articles, Links
Teaching tired T cells to fight HIV: time to test IL-15 for immunotherapy?
Trends Immunol. 2004 Mar;25(3):121-5. Review. No abstract available.
PMID: 15036038 [PubMed - indexed for MEDLINE]
7: Cho ML, Yoon CH, Hwang SY, Park MK, Min SY, Lee SH, Park SH, Kim HY. Related Articles, Links
Effector function of type II collagen-stimulated T cells from rheumatoid arthritis patients: cross-talk between T cells and synovial fibroblasts.
Arthritis Rheum. 2004 Mar;50(3):776-84.
PMID: 15022319 [PubMed - indexed for MEDLINE]
8: Zhang J, Sun R, Wei H, Zhang J, Tian Z. Related Articles, Links
Characterization of interleukin-15 gene-modified human natural killer cells: implications for adoptive cellular immunotherapy.
Haematologica. 2004 Mar;89(3):338-47.
PMID: 15020274 [PubMed - in process]
9: Salkowitz JR, Sieg SF, Harding CV, Lederman MM. Related Articles, Links
In vitro muman memory CD8 T cell expansion in response to cytomegalovirus requires CD4+ T cell help.
J Infect Dis. 2004 Mar 15;189(6):971-83. Epub 2004 Mar 01.
PMID: 14999599 [PubMed - indexed for MEDLINE]
10: Ripley D, Shoup B, Majewski A, Chegini N. Related Articles, Links
Differential expression of interleukins IL-13 and IL-15 in normal ovarian tissue and ovarian carcinomas.
Gynecol Oncol. 2004 Mar;92(3):761-8.
PMID: 14984938 [PubMed - indexed for MEDLINE]
11: Bouchard A, Ratthe C, Girard D. Related Articles, Links
Interleukin-15 delays human neutrophil apoptosis by intracellular events and not via extracellular factors: role of Mcl-1 and decreased activity of caspase-3 and caspase-8.
J Leukoc Biol. 2004 Feb 24 [Epub ahead of print]
PMID: 14982947 [PubMed - as supplied by publisher]
12: Taylor MW, Grosse WM, Schaley JE, Sanda C, Wu X, Chien SC, Smith F, Wu TG, Stephens M, Ferris MW, McClintick JN, Jerome RE, Edenberg HJ. Related Articles, Links
Global effect of PEG-IFN-alpha and ribavirin on gene expression in PBMC in vitro.
J Interferon Cytokine Res. 2004 Feb;24(2):107-18.
PMID: 14980075 [PubMed - in process]
13: Pulendran B, Dillon S, Joseph C, Curiel T, Banchereau J, Mohamadzadeh M. Related Articles, Links
Dendritic cells generated in the presence of GM-CSF plus IL-15 prime potent CD8+ Tc1 responses in vivo.
Eur J Immunol. 2004 Jan;34(1):66-73.
PMID: 14971031 [PubMed - indexed for MEDLINE]
14: Shi R, Yang J, Jaramillo A, Steward NS, Aloush A, Trulock EP, Alexander Patterson G, Suthanthiran M, Mohanakumar T. Related Articles, Links
Correlation between interleukin-15 and granzyme B expression and acute lung allograft rejection.
Transpl Immunol. 2004 Jan;12(2):103-8.
PMID: 14967307 [PubMed - in process]
15: Okada H, Nakajima T, Yasuda K, Kanzaki H. Related Articles, Links
Interleukin-1 inhibits interleukin-15 production by progesterone during in vitro decidualization in human.
J Reprod Immunol. 2004 Feb;61(1):3-12.
PMID: 14967219 [PubMed - in process]
16: Chklovskaia E, Nowbakht P, Nissen C, Gratwohl A, Bargetzi M, Wodnar-Filipowicz A. Related Articles, Links
Reconstitution of dendritic and natural killer cell subsets after allogeneic stem cell transplantation: Effects of endogenous flt3 ligand.
Blood. 2004 Feb 5 [Epub ahead of print]
PMID: 14764540 [PubMed - as supplied by publisher]
17: Grzegorzewska AE, Mlot M. Related Articles, Links
Dialysate interleukin-15 concentration and ultrafiltration capacity in patients undergoing peritoneal dialysis.
Adv Perit Dial. 2003;19:67-72.
PMID: 14763036 [PubMed - indexed for MEDLINE]
18: Klebanoff CA, Finkelstein SE, Surman DR, Lichtman MK, Gattinoni L, Theoret MR, Grewal N, Spiess PJ, Antony PA, Palmer DC, Tagaya Y, Rosenberg SA, Waldmann TA, Restifo NP. Related Articles, Links
IL-15 enhances the in vivo antitumor activity of tumor-reactive CD8+ T cells.
Proc Natl Acad Sci U S A. 2004 Feb 17;101(7):1969-74. Epub 2004 Feb 04.
PMID: 14762166 [PubMed - indexed for MEDLINE]
19: Hofmann SR, Ettinger R, Zhou YJ, Gadina M, Lipsky P, Siegel R, Candotti F, O'Shea JJ. Related Articles, Links
Cytokines and their role in lymphoid development, differentiation and homeostasis.
Curr Opin Allergy Clin Immunol. 2002 Dec;2(6):495-506.
PMID: 14752332 [PubMed - in process]
20: Cohen Y, Nagler A. Related Articles, Links
Cord blood biology and transplantation.
Isr Med Assoc J. 2004 Jan;6(1):39-46. Review.
PMID: 14740509 [PubMed - indexed for MEDLINE]
Differential expansion of umbilical cord blood mononuclear cell-derived natural killer cells dependent on the dose of interleukin-15 with Flt3L.
Exp Hematol. 2004 Feb;32(2):202-209.
PMID: 15102482 [PubMed - as supplied by publisher]
2: Kim WU, Cho ML, Jung YO, Min SY, Park SW, Min DJ, Yoon JH, Kim HY. Related Articles, Links
Type II collagen autoimmunity in rheumatoid arthritis.
Am J Med Sci. 2004 Apr;327(4):202-11.
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3: Kim JV, Latouche JB, Riviere I, Sadelain M. Related Articles, Links
The ABCs of artificial antigen presentation.
Nat Biotechnol. 2004 Apr;22(4):403-10.
PMID: 15060556 [PubMed - in process]
4: Bernard J, Harb C, Mortier E, Quemener A, Meloen RH, Vermot-Desroches C, Wijdeness J, Van Dijken P, Grotzinger J, Slootstra JW, Plet A, Jacques Y. Related Articles, Links
Identification of an interleukin-15 alpha receptor binding site on human interleukin-15.
J Biol Chem. 2004 Mar 23 [Epub ahead of print]
PMID: 15039446 [PubMed - as supplied by publisher]
5: Forcina G, D'Ettorre G, Mastroianni CM, Carnevalini M, Scorzolini L, Ceccarelli G, D'Agostino C, Lichtner M, Massetti AP, Vullo V. Related Articles, Links
Interleukin-15 modulates interferon-gamma and beta-chemokine production in patients with HIV infection: implications for immune-based therapy.
Cytokine. 2004 Mar 21;25(6):283-90.
PMID: 15036244 [PubMed - in process]
6: Mastroianni CM, d'Ettorre G, Forcina G, Vullo V. Related Articles, Links
Teaching tired T cells to fight HIV: time to test IL-15 for immunotherapy?
Trends Immunol. 2004 Mar;25(3):121-5. Review. No abstract available.
PMID: 15036038 [PubMed - indexed for MEDLINE]
7: Cho ML, Yoon CH, Hwang SY, Park MK, Min SY, Lee SH, Park SH, Kim HY. Related Articles, Links
Effector function of type II collagen-stimulated T cells from rheumatoid arthritis patients: cross-talk between T cells and synovial fibroblasts.
Arthritis Rheum. 2004 Mar;50(3):776-84.
PMID: 15022319 [PubMed - indexed for MEDLINE]
8: Zhang J, Sun R, Wei H, Zhang J, Tian Z. Related Articles, Links
Characterization of interleukin-15 gene-modified human natural killer cells: implications for adoptive cellular immunotherapy.
Haematologica. 2004 Mar;89(3):338-47.
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9: Salkowitz JR, Sieg SF, Harding CV, Lederman MM. Related Articles, Links
In vitro muman memory CD8 T cell expansion in response to cytomegalovirus requires CD4+ T cell help.
J Infect Dis. 2004 Mar 15;189(6):971-83. Epub 2004 Mar 01.
PMID: 14999599 [PubMed - indexed for MEDLINE]
10: Ripley D, Shoup B, Majewski A, Chegini N. Related Articles, Links
Differential expression of interleukins IL-13 and IL-15 in normal ovarian tissue and ovarian carcinomas.
Gynecol Oncol. 2004 Mar;92(3):761-8.
PMID: 14984938 [PubMed - indexed for MEDLINE]
11: Bouchard A, Ratthe C, Girard D. Related Articles, Links
Interleukin-15 delays human neutrophil apoptosis by intracellular events and not via extracellular factors: role of Mcl-1 and decreased activity of caspase-3 and caspase-8.
J Leukoc Biol. 2004 Feb 24 [Epub ahead of print]
PMID: 14982947 [PubMed - as supplied by publisher]
12: Taylor MW, Grosse WM, Schaley JE, Sanda C, Wu X, Chien SC, Smith F, Wu TG, Stephens M, Ferris MW, McClintick JN, Jerome RE, Edenberg HJ. Related Articles, Links
Global effect of PEG-IFN-alpha and ribavirin on gene expression in PBMC in vitro.
J Interferon Cytokine Res. 2004 Feb;24(2):107-18.
PMID: 14980075 [PubMed - in process]
13: Pulendran B, Dillon S, Joseph C, Curiel T, Banchereau J, Mohamadzadeh M. Related Articles, Links
Dendritic cells generated in the presence of GM-CSF plus IL-15 prime potent CD8+ Tc1 responses in vivo.
Eur J Immunol. 2004 Jan;34(1):66-73.
PMID: 14971031 [PubMed - indexed for MEDLINE]
14: Shi R, Yang J, Jaramillo A, Steward NS, Aloush A, Trulock EP, Alexander Patterson G, Suthanthiran M, Mohanakumar T. Related Articles, Links
Correlation between interleukin-15 and granzyme B expression and acute lung allograft rejection.
Transpl Immunol. 2004 Jan;12(2):103-8.
PMID: 14967307 [PubMed - in process]
15: Okada H, Nakajima T, Yasuda K, Kanzaki H. Related Articles, Links
Interleukin-1 inhibits interleukin-15 production by progesterone during in vitro decidualization in human.
J Reprod Immunol. 2004 Feb;61(1):3-12.
PMID: 14967219 [PubMed - in process]
16: Chklovskaia E, Nowbakht P, Nissen C, Gratwohl A, Bargetzi M, Wodnar-Filipowicz A. Related Articles, Links
Reconstitution of dendritic and natural killer cell subsets after allogeneic stem cell transplantation: Effects of endogenous flt3 ligand.
Blood. 2004 Feb 5 [Epub ahead of print]
PMID: 14764540 [PubMed - as supplied by publisher]
17: Grzegorzewska AE, Mlot M. Related Articles, Links
Dialysate interleukin-15 concentration and ultrafiltration capacity in patients undergoing peritoneal dialysis.
Adv Perit Dial. 2003;19:67-72.
PMID: 14763036 [PubMed - indexed for MEDLINE]
18: Klebanoff CA, Finkelstein SE, Surman DR, Lichtman MK, Gattinoni L, Theoret MR, Grewal N, Spiess PJ, Antony PA, Palmer DC, Tagaya Y, Rosenberg SA, Waldmann TA, Restifo NP. Related Articles, Links
IL-15 enhances the in vivo antitumor activity of tumor-reactive CD8+ T cells.
Proc Natl Acad Sci U S A. 2004 Feb 17;101(7):1969-74. Epub 2004 Feb 04.
PMID: 14762166 [PubMed - indexed for MEDLINE]
19: Hofmann SR, Ettinger R, Zhou YJ, Gadina M, Lipsky P, Siegel R, Candotti F, O'Shea JJ. Related Articles, Links
Cytokines and their role in lymphoid development, differentiation and homeostasis.
Curr Opin Allergy Clin Immunol. 2002 Dec;2(6):495-506.
PMID: 14752332 [PubMed - in process]
20: Cohen Y, Nagler A. Related Articles, Links
Cord blood biology and transplantation.
Isr Med Assoc J. 2004 Jan;6(1):39-46. Review.
PMID: 14740509 [PubMed - indexed for MEDLINE]
- Joined
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- 7,226
I don't know what aliquotes are but I know 0° C is freezing (32° F)!!BrooklynJuice said:
xcel
- Joined
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aliquotes are integers that are exact divisors of some quantity; "4 is an aliquot part of 12".
freezing is nowhere near absolute zero (-459º Fahrenheit, -273º Celsius, or simply 0 degrees Kelvin (K),
freezing is nowhere near absolute zero (-459º Fahrenheit, -273º Celsius, or simply 0 degrees Kelvin (K),
Last edited:
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alliquots means pre-measured segregated dosage units
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- Feb 21, 2003
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- 715
Its very good shit the problem is transportation and storage
- Joined
- Feb 21, 2003
- Messages
- 715
And cycle it right and not loose all that dough but getting it is not that hard.
Bottom line if you aint upper tier in your sport it aint worth it IMO
Bottom line if you aint upper tier in your sport it aint worth it IMO
xcelbeyond said:
Yeah, if you get say 500mL of something then you would make 1 mL aliquotes in something like a microcentrifuge tube so that you would only take out 1 mL at a time to work with. This would be for research purposes because you keep all the aliquotes you are not using at -20 so that little proteases would hopefully not be active enough to degrade the protein.
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No off course your not gonna use it at -20C but it does degrade quite rapidly from thaw to refreeze to thaw to use from the literature Ive seen.
I haven't found that study on increased hypertrophy in skeletal muscle but I know that normally cytokines are made by cells in your body as an immunological response to some foreign thing like bacteria. It causes your white blood cells and lymphocytes to start proliferating to fight the infection. It doesn't seem like it would be good for you unless you had an immunodeficiency. But I know they are finding new cytokines and new uses for them everyday.
I found some interesting abstracts on pubmed, I will have to go to the library to get the full article though.
Interleukin-15 increases myosin accretion in human skeletal myogenic cultures.
Furmanczyk PS, Quinn LS.
University of Washington, School of Medicine, Seattle, WA 98195, USA.
Interleukin-15 (IL-15) has been shown to have anabolic effects on skeletal muscle in rodent studies conducted in vitro and in vivo. The mechanism of IL-15 action on muscle appears to be distinct from that of the well-characterized muscle anabolic factor insulin-like growth factor-I (IGF-I). IL-15 action has not been investigated in a human culture system nor in detail in primary skeletal myogenic cells. The purpose of this study was to compare the effects of IL-15 and IGF-I in primary human skeletal myogenic cells. Accretion of a major myofibrillar protein, myosin heavy chain (MHC), was used as a measure of muscle anabolism. We found that both growth factors induced increases in MHC accretion in primary human skeletal myogenic cultures; however, IL-15 and IGF-I actions were temporally distinct. IL-15 was more effective at stimulating MHC accretion when added to cultures after differentiation of myoblasts had occurred. In contrast, IGF-I was more effective at stimulating MHC accretion when added to cultures prior to differentiation of myoblasts. These results using a human system support recent findings from rodent models which indicate that the primary mode of IGF-I action on skeletal muscle anabolism is through stimulation of myogenic precursor cells, whereas the primary target of IL-15 action is the differentiated muscle fiber. Further, since clinical and experimental studies have shown IGF-I is not effective in preventing skeletal muscle wasting, the distinct mode of action of IL-15 suggests it may be of potential usefulness in the treatment of muscle wasting disorders.
Overexpression of interleukin-15 induces skeletal muscle hypertrophy in vitro: implications for treatment of muscle wasting disorders.
Quinn LS, Anderson BG, Drivdahl RH, Alvarez B, Argiles JM.
Division of Gerontology and Geriatric Medicine, University of Washington, Seattle 98195, USA. [email protected]
Interleukin-15 (IL-15) is a novel anabolic factor for skeletal muscle which inhibits muscle wasting associated with cancer (cachexia) in a rat model. To develop a cell culture system in which the mechanism of the anabolic action of IL-15 on skeletal muscle could be examined, the mouse C2 skeletal myogenic cell line was transduced with a retroviral expression vector for IL-15 and compared to sister cells transduced with a control vector. Overexpression of IL-15 induced fivefold higher levels of sarcomeric myosin heavy chain and alpha-actin accumulation in differentiated myotubes. Secreted factors from IL-15-overexpressing myogenic cells, but not from control cells, induced increased myofibrillar protein accumulation in cocultured control myotubes. IL-15 overexpression induced a hypertrophic myotube morphology similar to that described for cultured myotubes which overexpressed the well-characterized anabolic factor insulin-like growth factor-I (IGF-I). However, in contrast to IGF-I, the hypertrophic action of IL-15 on skeletal myogenic cells did not involve stimulation of skeletal myoblast proliferation or differentiation. IL-15 induced myotube hypertrophy at both low and high IGF-I concentrations. Furthermore, in contrast to IGF-I, which stimulated only protein synthesis under these culture conditions, IL-15 both stimulated protein synthesis and inhibited protein degradation in cultured skeletal myotubes. These findings indicate that IL-15 action on skeletal myogenic cells is distinct from that of IGF-I. Due to the ability of IGF-I to stimulate cell division and its association with several forms of cancer, controversy exists concerning the advisability of treating cachexia or age-associated muscle wasting with IGF-I. Administration of IL-15 or modulation of the IL-15 signaling pathway may represent an alternative strategy for maintaining skeletal muscle mass under these conditions.
Interleukin-15 mediates reciprocal regulation of adipose and muscle mass: a potential role in body weight control.
Carbo N, Lopez-Soriano J, Costelli P, Alvarez B, Busquets S, Baccino FM, Quinn LS, Lopez-Soriano FJ, Argiles JM.
Departament de Bioquimica i Biologia Molecular, Facultat de Biologia, Universitat de Barcelona, Spain.
Interleukin (IL)-15 is a cytokine which is highly expressed in skeletal muscle. Cell culture studies have indicated that IL-15 may have an important role in muscle fiber growth and anabolism. However, data concerning the metabolic effects of this cytokine in vivo are lacking. In the present study, IL-15 was administered to adult rats for 7 days. While IL-15 did not cause changes in either muscle mass or muscle protein content, it induced significant changes in the fractional rates of both muscle protein synthesis and degradation, with no net changes in protein accumulation. Additionally, IL-15 administration resulted in a 33% decrease in white adipose tissue mass and a 20% decrease in circulating triacylglycerols; this was associated with a 47% lower hepatic lipogenic rate and a 36% lower plasma VLDL triacylglycerol content. The decrease in white fat induced by IL-15 was in adipose tissue. No changes were observed in the rate of lipolysis as a result of cytokine administration. These findings indicate that IL-15 has significant effects on both protein and lipid metabolism, and suggest that this cytokine may participate in reciprocal regulation of muscle and adipose tissue mass.
Interleukin-15: a novel anabolic cytokine for skeletal muscle.
Quinn LS, Haugk KL, Grabstein KH.
Geriatric Research, Education, and Clinical Center, American Lake VA Medical Center, Tacoma, WA 98493, USA.
Interleukin-15 (IL-15) is a recently discovered growth factor which is highly expressed in skeletal muscle. In order to determine a functional role for IL-15 in skeletal myogenesis, the effects of IL-15 on myoblast proliferation and muscle-specific myosin heavy chain (MHC) expression were analyzed using the mouse C2 skeletal myogenic cell line and primary fetal bovine skeletal myogenic cultures. IL-15 had no effect on [3H]thymidine incorporation, nor on the rate of myoblast differentiation, assessed by anti-MHC immunocytochemical staining, in either type of culture. However, Western blot analyses revealed that IL-15 used at concentrations of 10 or 100 ng/ml increased MHC accumulation five-fold in C2 myoblast cultures and 2.5-fold in primary bovine myogenic cultures. Moreover, C2 myotubes formed in the presence of IL-15 appeared larger than controls. These findings indicate IL-15 can stimulate differentiated myocytes and muscle fibers to accumulate increased amounts of contractile proteins. Well-fused primary bovine myogenic cultures treated with the mitotic inhibitor aphidicolin, then administered IL-15 and/or the anabolic growth factor insulin-like growth factor-I (IGF-I), were analyzed for MHC accumulation using Western blots. IL-15 used at 10 ng/ml doubled MHC accumulation and was as effective as IGF-I used at 10 or 100 ng/ml. IL-15 and IGF-I used together increased MHC accumulation close to five-fold, indicating these two factors can act additively on muscle fibers. These findings indicate IL-15 affects parameters associated with skeletal muscle fiber hypertrophy, and suggest that IL-15 may be a novel anabolic agent to increase skeletal muscle mass.
Interleukin-15 increases myosin accretion in human skeletal myogenic cultures.
Furmanczyk PS, Quinn LS.
University of Washington, School of Medicine, Seattle, WA 98195, USA.
Interleukin-15 (IL-15) has been shown to have anabolic effects on skeletal muscle in rodent studies conducted in vitro and in vivo. The mechanism of IL-15 action on muscle appears to be distinct from that of the well-characterized muscle anabolic factor insulin-like growth factor-I (IGF-I). IL-15 action has not been investigated in a human culture system nor in detail in primary skeletal myogenic cells. The purpose of this study was to compare the effects of IL-15 and IGF-I in primary human skeletal myogenic cells. Accretion of a major myofibrillar protein, myosin heavy chain (MHC), was used as a measure of muscle anabolism. We found that both growth factors induced increases in MHC accretion in primary human skeletal myogenic cultures; however, IL-15 and IGF-I actions were temporally distinct. IL-15 was more effective at stimulating MHC accretion when added to cultures after differentiation of myoblasts had occurred. In contrast, IGF-I was more effective at stimulating MHC accretion when added to cultures prior to differentiation of myoblasts. These results using a human system support recent findings from rodent models which indicate that the primary mode of IGF-I action on skeletal muscle anabolism is through stimulation of myogenic precursor cells, whereas the primary target of IL-15 action is the differentiated muscle fiber. Further, since clinical and experimental studies have shown IGF-I is not effective in preventing skeletal muscle wasting, the distinct mode of action of IL-15 suggests it may be of potential usefulness in the treatment of muscle wasting disorders.
Overexpression of interleukin-15 induces skeletal muscle hypertrophy in vitro: implications for treatment of muscle wasting disorders.
Quinn LS, Anderson BG, Drivdahl RH, Alvarez B, Argiles JM.
Division of Gerontology and Geriatric Medicine, University of Washington, Seattle 98195, USA. [email protected]
Interleukin-15 (IL-15) is a novel anabolic factor for skeletal muscle which inhibits muscle wasting associated with cancer (cachexia) in a rat model. To develop a cell culture system in which the mechanism of the anabolic action of IL-15 on skeletal muscle could be examined, the mouse C2 skeletal myogenic cell line was transduced with a retroviral expression vector for IL-15 and compared to sister cells transduced with a control vector. Overexpression of IL-15 induced fivefold higher levels of sarcomeric myosin heavy chain and alpha-actin accumulation in differentiated myotubes. Secreted factors from IL-15-overexpressing myogenic cells, but not from control cells, induced increased myofibrillar protein accumulation in cocultured control myotubes. IL-15 overexpression induced a hypertrophic myotube morphology similar to that described for cultured myotubes which overexpressed the well-characterized anabolic factor insulin-like growth factor-I (IGF-I). However, in contrast to IGF-I, the hypertrophic action of IL-15 on skeletal myogenic cells did not involve stimulation of skeletal myoblast proliferation or differentiation. IL-15 induced myotube hypertrophy at both low and high IGF-I concentrations. Furthermore, in contrast to IGF-I, which stimulated only protein synthesis under these culture conditions, IL-15 both stimulated protein synthesis and inhibited protein degradation in cultured skeletal myotubes. These findings indicate that IL-15 action on skeletal myogenic cells is distinct from that of IGF-I. Due to the ability of IGF-I to stimulate cell division and its association with several forms of cancer, controversy exists concerning the advisability of treating cachexia or age-associated muscle wasting with IGF-I. Administration of IL-15 or modulation of the IL-15 signaling pathway may represent an alternative strategy for maintaining skeletal muscle mass under these conditions.
Interleukin-15 mediates reciprocal regulation of adipose and muscle mass: a potential role in body weight control.
Carbo N, Lopez-Soriano J, Costelli P, Alvarez B, Busquets S, Baccino FM, Quinn LS, Lopez-Soriano FJ, Argiles JM.
Departament de Bioquimica i Biologia Molecular, Facultat de Biologia, Universitat de Barcelona, Spain.
Interleukin (IL)-15 is a cytokine which is highly expressed in skeletal muscle. Cell culture studies have indicated that IL-15 may have an important role in muscle fiber growth and anabolism. However, data concerning the metabolic effects of this cytokine in vivo are lacking. In the present study, IL-15 was administered to adult rats for 7 days. While IL-15 did not cause changes in either muscle mass or muscle protein content, it induced significant changes in the fractional rates of both muscle protein synthesis and degradation, with no net changes in protein accumulation. Additionally, IL-15 administration resulted in a 33% decrease in white adipose tissue mass and a 20% decrease in circulating triacylglycerols; this was associated with a 47% lower hepatic lipogenic rate and a 36% lower plasma VLDL triacylglycerol content. The decrease in white fat induced by IL-15 was in adipose tissue. No changes were observed in the rate of lipolysis as a result of cytokine administration. These findings indicate that IL-15 has significant effects on both protein and lipid metabolism, and suggest that this cytokine may participate in reciprocal regulation of muscle and adipose tissue mass.
Interleukin-15: a novel anabolic cytokine for skeletal muscle.
Quinn LS, Haugk KL, Grabstein KH.
Geriatric Research, Education, and Clinical Center, American Lake VA Medical Center, Tacoma, WA 98493, USA.
Interleukin-15 (IL-15) is a recently discovered growth factor which is highly expressed in skeletal muscle. In order to determine a functional role for IL-15 in skeletal myogenesis, the effects of IL-15 on myoblast proliferation and muscle-specific myosin heavy chain (MHC) expression were analyzed using the mouse C2 skeletal myogenic cell line and primary fetal bovine skeletal myogenic cultures. IL-15 had no effect on [3H]thymidine incorporation, nor on the rate of myoblast differentiation, assessed by anti-MHC immunocytochemical staining, in either type of culture. However, Western blot analyses revealed that IL-15 used at concentrations of 10 or 100 ng/ml increased MHC accumulation five-fold in C2 myoblast cultures and 2.5-fold in primary bovine myogenic cultures. Moreover, C2 myotubes formed in the presence of IL-15 appeared larger than controls. These findings indicate IL-15 can stimulate differentiated myocytes and muscle fibers to accumulate increased amounts of contractile proteins. Well-fused primary bovine myogenic cultures treated with the mitotic inhibitor aphidicolin, then administered IL-15 and/or the anabolic growth factor insulin-like growth factor-I (IGF-I), were analyzed for MHC accumulation using Western blots. IL-15 used at 10 ng/ml doubled MHC accumulation and was as effective as IGF-I used at 10 or 100 ng/ml. IL-15 and IGF-I used together increased MHC accumulation close to five-fold, indicating these two factors can act additively on muscle fibers. These findings indicate IL-15 affects parameters associated with skeletal muscle fiber hypertrophy, and suggest that IL-15 may be a novel anabolic agent to increase skeletal muscle mass.
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