Dat
Could this quoted question on Humalog be employed then ?
Also whats your opinion on raised insulin levels during training, I consume a carb drink during training gaspari Sizeon + WMS (50g C) so was thinking as Humalog peaks at around 1-1.5 hours it could be taken at beginning of WO and the the peak will hit pretty much as the WO's over ?
See i like to keep the bulk of my carb intake around training PreWO, PWO and PWO meals 1-2. So was thinking with using Humalog i have tighter control of duration of action and as i train after breakfast (breakfast is my PreWO meal) so could use 3-4 spread out shots starting before breakfast up until just before WO of humalog so my raised insulin levels start with breakfast with a gluco i control prolonged peak till pretty much PWO then let it taper off clearing by my PWO meal 2.
Currently my diet goes
7.00am:
GH
Breakfast (100g C)
9.00am:
Train
Intra WO drink & PWO, Gaspari Sizeon + WMS (50g C)
11.00am:
PWO meal 1 (75g C)
2.00pm:
PWO meal 2 (50g C)
So this is based on glucose reading but thinking starting with 3iu Humalog dosed at 7.00,8.00 and 9.00am
Even if "they" call your peptide CJC-1295, they probably sold you GRF(1-29) period.
So dose it like GRF(1-29) and hit it three times a day with GHRP-6.
"Straight forward answer" okay sure.
Why can't you lose weight without growth hormone?
How old are you?
Fatloss is simple. You need to maximize the time period during the day when your body will burn fat. It won't do so in the presence of insulin or elevated blood glucose.
So buy a blood glucose monitor, prick your finger and figure out how to minimize the blood glucose spike post meal and how to lessen its duration.
Here is a hint. Use low GI foods. Construct meals with low Glycemic Load. Add fiber. Keep meals smaller and spaced out by 3 hours. Speed up the metabolism with cardio. Do cardio when blood glucose is not elevated. Don't be in a hurry and recognize that fat comes off the periphery before it comes off the core.
Growth Hormone does not melt fat off.
As my friend vadim_b1 just pointed out it is great for contest prep when you are striving for lower single digits in bodyfat...it helps keep muscle in those states.
But for a non-competitor who desires to get to 10% bodyfat GH is most definately not needed.
If you are say 40+ years of age having a youthful restoration of GH levels year around will help keep your core tighter if you have everything else in check.
But for young guys who really are just fat asses and lazy as well to think that GH will do all or even most of the work is just ridiculous. They think that they aren't lazy because they go to the gym and push a piece of iron for 30 seconds and then put it down several times. As my friend Razor Ripped has repeatedly pointed out you don't burn many calories that way.
Then all these young guy fat asses and lazy fucks to boot never ever seem to understand the use and misuse of food. So they spend way to much time looking for the magic compound that will overcome their laziness and help them get rid of their fat asses so they use Clenbuterol, T3, steroids, Growth Hormone, etc. and still they never accomplish what they want and if they do they never hold it for very long.
bmoney I'm not saying you are one of these guys but I'm asking. Are you one of these fat ass lazy fucks?
I'm 22 and I'm not one of those lazy fucks, i like the idea of the monitor and will go buy one tonight, how will i know what my optimum level for fat loss is?. i don't need the gh for fat loss, i want to use it to help keep some size during my pct along with all of the other health promoting effects like the sleeping part. I bust my ass in the gym and try to do cardio in the am for 30 minutes on my stair master. I weigh out and portion my food the best i can and try to eat clean with a few cheat meals a week. I have been on a lean bulker and its going well and would like to trim down a little fat, I'm not expecting this to be a miracle. I really appreciate your time and will use your advice to help me out. thanks
...Hey dat, how do you feel about the theroy that the slowing of the natty t3 levels and rise in prolactin is less of a problem if you shoot your gh in one dose 3x per week opposed to daily mulitple times. Gavin Kane wrote this, and im just wondering if there is any science behind it....
I read an article of his on how to use MGF....he spends a lot of time creating protocols to follow and the timing of compounds and idiots blithefully follow.
The problem with all of that is that MGF will NEVER behave as MGF if injected. Doesn't matter whether you pegylate it or not. MGF is expressed from within and mediates its actions in the nulceus of the cell. Unlike IGF-1 it has no receptor. So writing on and on about timing it with IGF-1 is of zero value because MGF will behave like IGF-1 when injected and will NEVER behave as MGF.
"Gavin Kane wrote this" is a sure way to get me not to respond...don't bother rephrasing it because I have zero interest in this question.
ERRATUM 1/20/2009: Wow. What a jerk I was during this time period!!!!! Thankfully 4thgen messaged me and called me on it ....plus I soon got over the flu that kept me bed ridden during this time. I apologize to anyone who comes along and reads the negativity in my posts during this time frame.
You have to really know what you are doing. I assume that YOU do but I just want to emphasize that THAT is a very advanced protocol and 99.9% of the people that read these boards should not consider it EVER.
Now you do need to know exactly how/when Humalog peaks. I don't use it so my numbers may not be spot on BUT I believe there is a significant hit that is much harsher then any that Hum-R will generate 30 minutes post injection.
In addition physical exertion can alter the peaks a little.
Then on top of that you do have one course of insulin running up into the next course which will add to the unpredictability of the peaks...it is like ocean waves running up against each other...
So again you have to know exactly what you are doing. One of the things that is important is for you to have experience with different components of your protocol.
For instance have you ever worked out with insulin peaking in your system? 50gram of carbs to meet 3iu of insulin looks sufficient... but you need to understand both subjectively & most importantly objectively (with a glucose meter) what is happening during this time frame.
Have you ever dosed humalog at 3iu's back to back within an hour? If not that needs to be done and mental notes taken BEFORE undertaking a back to back to back mode of administration.
I can not recommend your protocol or any other one for that matter. The one you propose has less margin for error then one involving Hum-R and allowing the peaks to hit when you have a kitchen full of life-saving carbs at your immediate disposal rather then being in a gym environment.
What happens if you go to the gym and spill your shake? For me I would never venture away from my kitchen while insulin is peaking....
I read an article of his on how to use MGF....he spends a lot of time creating protocols to follow and the timing of compounds and idiots blithefully follow.
The problem with all of that is that MGF will NEVER behave as MGF if injected. Doesn't matter whether you pegylate it or not. MGF is expressed from within and mediates its actions in the nulceus of the cell. Unlike IGF-1 it has no receptor. So writing on and on about timing it with IGF-1 is of zero value because MGF will behave like IGF-1 when injected and will NEVER behave as MGF.
"Gavin Kane wrote this" is a sure way to get me not to respond...don't bother rephrasing it because I have zero interest in this question.
You have to really know what you are doing. I assume that YOU do but I just want to emphasize that THAT is a very advanced protocol and 99.9% of the people that read these boards should not consider it EVER.
Now you do need to know exactly how/when Humalog peaks. I don't use it so my numbers may not be spot on BUT I believe there is a significant hit that is much harsher then any that Hum-R will generate 30 minutes post injection.
In addition physical exertion can alter the peaks a little.
Then on top of that you do have one course of insulin running up into the next course which will add to the unpredictability of the peaks...it is like ocean waves running up against each other...
So again you have to know exactly what you are doing. One of the things that is important is for you to have experience with different components of your protocol.
For instance have you ever worked out with insulin peaking in your system? 50gram of carbs to meet 3iu of insulin looks sufficient... but you need to understand both subjectively & most importantly objectively (with a glucose meter) what is happening during this time frame.
Have you ever dosed humalog at 3iu's back to back within an hour? If not that needs to be done and mental notes taken BEFORE undertaking a back to back to back mode of administration.
I can not recommend your protocol or any other one for that matter. The one you propose has less margin for error then one involving Hum-R and allowing the peaks to hit when you have a kitchen full of life-saving carbs at your immediate disposal rather then being in a gym environment.
What happens if you go to the gym and spill your shake? For me I would never venture away from my kitchen while insulin is peaking....
Dat
Fully understand were you are coming from and value your input, but goes without saying i would not try any method blind or without taking certain measures needed (trial runs, taper dosages, etc)
I have pretty much got my GH, IGF and insulin schedules laid out but have had mixed opinions and views on PegMGF use and your post above got me intersted again in your opinion/view on PegMGF use ?
Two methodsi have looked into based on keeping PegMGF and IGF intake apart are
1)
Mon: GH/Insulin-Train-IGF
Tue: GH/Insulin-Train-IGF
Wed: Rest day-250mcg PegMGF
Thur: GH/Insulin-Train-IGF
Fri: GH/Insulin-Train-IGF
Sat: Rest day-250mcg PegMGF
Sun Rest day
2)
Mon: GH/Insulin-Train-IGF
Tue: GH/Insulin-Train-IGF
Wed: Rest day
Thur: GH/Insulin-Train-IGF
Fri: GH/Insulin-Train-IGF
Sat: Rest day-500mcg PegMGF
Sun Rest day
Both use 500mcg PegMGF EW either taken twice weekly or once weekly, whats your opinion on these schedules ?
To quickly summarize the difference in function, MGF stimulates muscle stem cells (satellite cells) to reenter the cell cycle and proliferate, whereas IGF-1 is necessary for the differentiation of newly generated muscle precursor cells into myoblasts and myofibers. See material from Goldspink posted earlier in this thread at: Post #158 Mechanical Signals, IGF-I Gene Splicing, and Muscle Adaptation
Growth Hormone bound to its receptor in the liver activates the STAT5b signaling pathway which promotes movement of that activated signaling protein to the nucleus where it induces transcription of the IGF-1 gene. From studies in mice and humans, it is evident that GH induces expression of both the endocrine form of IGF-1, the muscle form of IGF-1 and MGF. 1 Mice deficient in GH (lit/lit mice) respond to administration of GH with an acute increase in MGF, but not IGF-1, in skeletal muscle, although IGF-1 in liver is increased. 2 However the precise mechanism by which GH has distinct effects on IGF-1 and MGF expression in muscle is not completely known.
What is known is that in response to stretch overload and the presence of growth hormone combined gene transcription in muscle and its subsequent "blueprint" assembly" are induced to create mechano growth factor (MGF also known as IGF-1Ec in humans or IGF-1EB in mice) instead of muscle IGF-1. 3
How does the behavior of IGF-1 and MGF differ?
"MGF is a non-secreted form of IGF-1 that can be found in the nucleus of cells in culture or in a perinuclear location in hippocampal cells after ischemia (restriction in blood supply)". 4
In other words MGF never leaves the cell it was created in. For emphasis I quote from another source:
"...MGF... is not normally secreted." 5
Geoffrey Goldspink has written "that MGF increases myoblast proliferation via a different signalling pathway" then IGF-1.
To reiterate & expand upon this concept I quote from another source:
"IGF-1 isoforms differ in the signaling pathways they activate. By over-expressing IGF-1Ea and MGF in muscle, it has been shown that both isoforms can activate IGF-1R and AKT phosphorylation. In addition, MGF was shown to induce phosphorylation of ERK, a property not shared with IGF-1Ea." 6
So IGF-1 and MGF work through different pathways not receptors. There is only one receptor, IGF-1-receptor (also insulin, IGF-II & hybrid receptors which are not relevant to this discussion). There is no MGF receptor. The reason why it would be nonsensical to have an MGF receptor is that MGF does not leave the cell.
This contrasts with IGF-1 which is released from the liver into circulation and which is created in muscle and translocates to the cell surface. Both events result in IGF-1 binding to the IGF-1 receptor.
So what happens in plain language please?
During the process of gene transcription pieces of DNA are transcribed and then spliced together by RNA and this code is taken to the ribosomes where the peptide is manufactured. In splicing MGF there is a subtle frame shift such that the right side of the code is a little different then IGF-1. Everything else is identical.
This subtle difference means that when MGF & IGF-1 are manufactured by the riboomes MGF MUST because of the signal pull that is part of its make up, translocate to the Nucleus of the cell and more specifically the Nucleolus.
IGF-1 because of its makeup MUST move to the cytoplasm where it forms a pool of IGF-1 which will transloacte to the cell membrane where it will bind w/ an IGF-1 receptor.
MGF has NO receptor. It does not need it to mediate events. Too many times people think that a lock/key ligand/receptor is needed to intiate signals. That is not always true especially when proteins move to the nucleus.
MGF is NEVER found in circulation. It is produced in a muscle cell as described and it will act there always.
IGF-1 however does circulate. It is produced in the liver and secreted into the blood stream. If it is made in muscle tissue or in local tissue it makes its way to the surface and can bind to a receptor on that cell or nearby cells. The latter is how muscle made IGF-1 can effect nearby bone growth.
In lab experiments with MGF they usually do one of two things. One they use a viral vector of MGF cDNA to increase the cDNA of MGF in the cell so that more MGF is made internally. When they do this they get a 25% increase in muscle in a three week period. If they use the same approach to get IGF-1 to express itself from within they get less muscle growth (15%) and it takes 4 months.
The second approach is to actually inject MGF into a cell (i.e. penetrate the cell membrane). Unfortunately for scientists this also invokes a damage repair function in cells so it is difficult to actually attribute all of the benefits that ensue to MGF.
You follow neither of these approaches when you inject MGF or Peg MGF.
MGF is identical to IGF-1 in chemical makeup on the leftside of the peptide. This allows it to bind with IGF-1 receptors should it ever be injected or find itself outside of the cell. However because of the difference in right-side structure MGF is incapable of binding to IGF-1 binding proteins (which would prolong its life).
MGF has a very short half-life in blood plasma. If it is pegylated it has a longer half-life. I do not know the extent to which pegylation reduces binding affinity but it probably does to some extent depending on where it is pegylated.
Injecting Peg MGF will, if it survives, probably bind to an IGF-1 receptor. If it does so it activates the IGF-1 signaling pathways just as IGF-1 would.
I do not have any data on how strongly MGF will bind to IGF-1 receptors. A pegylated MGF is small enough to penetrate the vascular wall and travel systemically. It will not be confined to the area injected as IGF-1 bound to IGF-BindingProtein3 bound to Acid laibile subunit (i.e. the ternary complex) will. Thats why injecting large amounts of MGF brings vacularization, pumps, glucose uptake, in essence insulin-like activity....because it is behaving as IGF-1...and doing so in systemic fashion.
Some science (derived from ref:5) followed by both a reiteration and an elaboration on my part.
The IGF-1 gene consists of 6 exons (DNA bases that are transcribed into mRNA and eventually code for amino acids in the proteins), separated by 5 introns (DNA bases, which are found between exons, but are not transcribed). Transcription is controlled by alternate use of two upstream promoters and starts at several transcription start sites located in exons 1 and 2. Together, alternate promoter usage and alternative splicing at the 5' and 3' ends of the gene generate several distinct mRNAs depending on their exon sequences, which code for three isoforms of precursor IGF-1.
Note: The notation 5' and 3' refer to the direction of the DNA template in the chromosome and is used to distinguish between the two untranslated regions (grey). See the example below:
These isoforms have characteristic N-terminal signal peptide sequences and C-terminal extension (E) peptide domains. Exons 1 and 2 and part of exon 3 encode the signal peptides. The remainder of exon 3 and exon 4 encode the mature IGF-1 peptide and the proximal part of the E peptide, which are shared by all isoforms. Splicing of exon 4 to exon 6 generates the predominant transcript IGF-1Ea. Splicing of exon 4 to exon 5 generates IGF- 1Eb, which encodes an isoform with 47 distinct amino acids in the E domain. When part of exon 5 is spliced to exon 6, the IGF- 1Ec (IGF-1EB in mouse) variant is generated. In this case, a frame-shift occurs in exon 5 followed by premature transcription stop in exon 6 that results in a stretch of 25 amino acids unique to this variant.
As a result these templates produce in cellular ribosomes IGF-1 peptide forms that differ in amino acid structure in the E peptide region. This results in different C-terminal regions for the IGF-1 & MGF peptides. MGF BECAUSE of its C-terminal sequence, upon "birth" becomes rapidly localized in the nucleus. It is the carboxy portion which draws either MGF or the altered portion to the nucleus rather than to the cell membrane.
"We found that the isoform of the human IGF-I precursor encoded by exon 5 [MGF] localized to the nucleus and strongly to the nucleolus. Precursors containing exon 6 or the upstream portion of exon 5 did not...The findings are consistent with the presence of a nuclear and nucleolar localization signal situated in the C-terminal part of the exon 5-encoded domain." 4
MGF is an autocrine growth factor, and this is THE different signaling pathway...a pathway that does not involve any receptor. The action of MGF via this pathway is one of promoting myoblast proliferation.
However MGF maintains a dual action. It "activates the muscle stem cell pool through its C-terminal domain (encoded in exons 5 and 6) as mentioned above AND according to the various studies by Geoffrey Goldspink "increases anabolic effects as the result of its IGF-I receptor binding domain (encoded in exons 3 and 4), which all the IGF-I genes possess."
The unaltered portion of MGF is still capable of binding to the IGF-Receptor. The altered carboxy portion renders MGF incapable of binding to the IGF-1-Binding proteins BUT it possesses the ability to bind to the IGF-1-Receptor via the unaltered side.
So what if MGF is injected into plasma? Presumably it would bind to the IGF-1-Receptor and initiate the AKT signaling pathway which will stimulate cell growth signals. In other words MGF stops being MGF and behaves like IGF-1 in initiating anabolic events. But it has been shown but is not yet fully understood that MGF is capable of AKT phosphorylation (an IGF-1-IGF-1-receptor mediated event) without ever coming in contact with the IGF-1-receptor.
This brings up an interesting point. MGF seems to be capable of performing both its unique duties and those of IGF-1 as well (at times).
What about studies that inject MGF into subjects?
Actually they don't do it that way.
"One of the methods we used to establish the biological action of MGF was to engineer a gene into which its cDNA was inserted into a vector. To our surprise a single intramuscular injection into a mouse muscle resulted in a 25% increase in mean muscle fibre cross section area within three weeks." - Goldspink G, Yang SY. Method of treating muscular disorders,United States Patent. Patent No US 6,221,842 B1, Apr 24, 2001.
This contrasts with, "similar experiments carried out using the systemic or liver type of IGF-I in an adenoviral vector under the control of a muscle regulatory sequence. This took four months to produce a 15% increase and is probably due to the anabolic effect of IGF-I, which is common to all the splice variants." - Barton-Davis E, Shoturma DI, Musaro A, et al.Viral mediated expression of insulin-like growth factor-I blocks the aging-related loss of skeletal muscle function. Proc Natl Acad Sci USA 1998;95:15603–7.
So obviously the endogenous expression of MGF is much more powerful then the endogenous expression of IGF-1. Therefore we want MGF to behave as MGF and not as IGF-1 and do so in autocrine fashion.
In fact in an anti-doping article Goldspink made the following observation "The use of the DNA of IGF-I and particularly MGF is therefore a prime candidate for gene doping for enhancement of athletic performance."
Compare this to how bodybuilders have been attempting to use MGF. They simply inject the peptide. So even if it is resistant to breakdown (via PEGylation) and it binds locally to the IGF-1 receptor there will be NO MGF primary action. Instead MGF will behave as an IGF-1 ligand, binding to the IGF-1-Receptor to mediate IGF-1 signaling events.
References:
1 - Hameed, M., Lange, K.H., Andersen, J.L., Schjerling, P., Kjaer, M., Harridge, S.D., Goldspink, G., 2004. The effect of recombinant human growth hormone and resistance training on IGF-I mRNA expression in the muscles of elderly men. J. Physiol. 555, 231–240.
2 - Iida, K., Itoh, E., Kim, D.S., del Rincon, J.P., Coschigano, K.T., Kopchick, J.J., Thorner, M.O., 2004. Muscle mechano growth factor is preferentially induced by growth hormone in growth hormone-deficient lit/lit mice. J. Physiol. 560, 341–349.
3 - McKoy, Godfrina et al.,Expression of insulin growth factor-1 splice variants and structural genes in rabbit skeletal muscle induced by stretch and stimulation, Journal of Physiology (1999), 516.2, pp. 583—592 583
4 - Tan DS, Cook A, and Chew SL. Nucleolar localization of an isoform of the IGF-I precursor. BMC Cell Biol 3: 17, 2002.
5 - Scrable, Heidi, Running on empty: How p53 controls INS/IGF signaling and affects life span, Experimental Gerontology xxx (2008) xxx–xxx
6 - Barton, E.R., 2006. Viral expression of insulin-like growth factor-I isoforms promotes different responses in skeletal muscle. J. Appl. Physiol. 100, 1778– 1784.
I'm not Dat, but I'll answer anyways with my 2 cents
Since you are already planning on using exo IGF, then there does not seem any reason to add exo MGF in any form. This is without debating whether IGF-1 is even necessary in the 1st place....
The main point of this is that exogenous injected MGF/PegMGF cannot make it past the cell membrane to initiate its unique "MGF" action at the nucleus, thus it will only be able to bind to an IGF-1 receptor just as IGF would, causing the same signaling pathways to be initiated.
This is without taking into account the possible differences in binding affinities of both peptides for the IGF-1 receptor.
Thus, its possible to simply consider that by taking both MGF and IGF in a protocol would be similar to taking IGF and IGF in a protocol.
I'm not Dat, but I'll answer anyways with my 2 cents
Since you are already planning on using exo IGF, then there does not seem any reason to add exo MGF in any form. This is without debating whether IGF-1 is even necessary in the 1st place....
The main point of this is that exogenous injected MGF/PegMGF cannot make it past the cell membrane to initiate its unique "MGF" action at the nucleus, thus it will only be able to bind to an IGF-1 receptor just as IGF would, causing the same signaling pathways to be initiated.
This is without taking into account the possible differences in binding affinities of both peptides for the IGF-1 receptor.
Thus, its possible to simply consider that by taking both MGF and IGF in a protocol would be similar to taking IGF and IGF in a protocol.
Thank you my friend. That is exactly what I was going to write just as soom as I recovered :f;od-smil
I feel I am recovering from my illness today so I hope to not be an asshole to any more people. If I offended you in the last two weeks please forgive me. If I offended you more then 2 weeks ago then I probably meant it.
Thank you my friend. That is exactly what I was going to write just as soom as I recovered :f;od-smil
I feel I am recovering from my illness today so I hope to not be an asshole to any more people. If I offended you in the last two weeks please forgive me. If I offended you more then 2 weeks ago then I probably meant it.
Hell yeah, Dat's answered in depth every single question in this topic i've posted ! Not just a basic reply but actually taken the time to explain his reasoning behind his answer... Will admit i've been a little lost in the explaination sometimes
I know you don't address dosages that much in this topic but would like your opinion on the below
Currently use this on each training day (4x each week) apart from thyroid meds which are ED
8iu GH (admin breakfast which is 3-4 before WO)
12.5mcg T3/50mcg T4 (empty stomach 1 hour before breakfast)
6-8iu insulin (working with the multi Humalog shots spread PreWO/PWO)
50mcg IGF (taken PWO)
PegMGF (from above post will drop after last shot from opened vial)
Do all the dosage in your opinion look suited and if anyone area was lacking or would be of benefit to up which would it be ?
Now having said all of this the following needs to be pointed out.
MGF (modified for survival in plasma) does convey (at least in a single study) a neuroprotective effect when injected into the carotid artery independent of IGF-1 & the IGF-1 receptor.
This after Ischemia injury (restriction in blood supply to the brain) was induced and MGF was administered in conjunction with a reperfusion (return of the blood supply to the site of injury).
It should be noted that the brain ischemia induced an increase in the endogenous expression of MGF but the injected MGF seemed to add to the endogenic benefit.
It is difficult to understand fully because the authors of the study themselves didn't fully understand. It is interesting to note though that one of the authors patented the procedure of using a virus to insert cDNA that expresses MGF from within. So maybe that tells us something because I didn't find a patent on the procedure of injecting MGF from without.
This instance doesn't effect my previous post. I just wanted to be complete.
The best advice I can ever give is "go with what you know and experiment around the periphery."
Only if you have the time should you make changes with underminable outcomes. These types of changes will always give you the best knowledge for your databank BUT could either propel you forward or set you back.
So I am going to assume that with the protocol you just outlined that you are going with what you know and experimenting around the periphery.
There is nothing wrong with those doses but I have to ask where is the testosterone?
GH & testosterone both operate through different pathways to increase protein synthesis. Taken together the benefits are at least additive and thought to be synergistic.
The best advice I can ever give is "go with what you know and experiment around the periphery."
Only if you have the time should you make changes with underminable outcomes. These types of changes will always give you the best knowledge for your databank BUT could either propel you forward or set you back.
So I am going to assume that with the protocol you just outlined that you are going with what you know and experimenting around the periphery.
There is nothing wrong with those doses but I have to ask where is the testosterone?
GH & testosterone both operate through different pathways to increase protein synthesis. Taken together the benefits are at least additive and thought to be synergistic.
I just started researching a little bit about "fibroblast growth factor" as an agent for myoblast proliferation perhaps to be used in place of MGF.
Anyway I came across this abstract on Trenbolone that was of interest in relation to proliferation and differentiation of satellite cells. Kinda makes me wish I could tolerate Trenbolone.
Trenbolone alters the responsiveness of skeletal muscle satellite cells to fibroblast growth factor and insulin-like growth factor I
SH Thompson, LK Boxhorn, WY Kong and RE Allen
Department of Animal Sciences, University of Arizona, Tucson 85721.
Endocrinology, Vol 124, 2110-2117, 1989
The potential role of satellite cells in mediating the effect of trenbolone [17 beta-hydroxyestra-4,9-11-trien-3-one (TBOH)] on skeletal muscle hypertrophy was examined.
Young female Sprague-Dawley rats received TBOH injections daily for 2 weeks; growth, body composition, and the composition of selected muscles were assessed. Treated rats grew more rapidly and deposited less body lipid and more protein. The semimembranosus muscle from treated rats was larger and had approximately 60% more DNA per muscle than muscles from control rats.
The addition of trenbolone directly to the medium of cultured satellite cells did not stimulate cell proliferation, nor did it augment the stimulatory response of these cells to fibroblast growth factor (FGF) or insulin-like growth factor I (IGF-I). In contrast, satellite cells cultured from TBOH-treated rats exhibited greater proliferative responses to FGF and IGF-I than satellite cells from control rats. In addition, serum from TBOH-treated rats stimulated greater cell proliferation in satellite cell cultures than serum from control rats.
These experiments suggest that one possible mechanism responsible for the ability of TBOH to stimulate skeletal muscle hypertrophy may be through enhanced proliferation and differentiation of satellite cells as a result of the increased sensitivity of these cells to IGF-I and FGF.
Dat,
What is your opinion on PWO insulin?
Am I right into thinking it is not needed PWO since glucose absorption is not insulin dependent but is dependent on GLUT 4 transporters?And since exogenous insulin lowers blood glucose, during PWO don't we need carbs for the insulin spike?I see a contradiction here.
Also is it true that after injecting GH, one should wait 1.5-2hrs before eating as ingesting carbs with GH is actually a bad idea?
Thank you for your time and contribution.Much appreciated.
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