IGF: Gains vs. Sides
- 04-14-2004, 11:06 PM
IGF: Gains vs. Sides
I'm unbias on IGF but I did find this....
posted by buffness on SBI
You be the judge, their will always be two sides to a story. It's up to you to pick which one is right for you....
By Cy Willson.....
IGF-1: Worst Bodybuilding Drug Ever?
Q: What ever happened to IGF-1? It was talked about in 'roid books in the early '90s but you don't hear much about it now, except for a few sleazy supplement companies who are using the name.
A: IGF-1 can allow for hypertrophy of muscle. Will it do such a thing when administered to humans? Yes. However, the gains seen really arenít spectacular. More often than not, they donít even come close to gains seen using androgens.
For the most part, people should realize that IGF-1 is primarily responsible for GHís anabolic effects in skeletal muscle as well as cell proliferation, leading to enlarged internal organs and increasing the risk for cancer dramatically. Oh, and this most certainly includes Long R3 IGF-I as I know some people will try to argue that it's much safer.
Well, in order to give you the total picture, Iím going to go over some basic molecular biology as well as list the direct evidence we have concerning the side effects of IGF-1 and yes, that includes Long R3 IGF-I.
First, people should understand that in the human cell cycle, growth requires growth factors in general. Seems simple enough. The next thing people need to understand is that for a normal cell, death is something that'll inevitably occur via loss of telomerase or apoptosis (programmed cell death). Again, I canít overemphasize enough that the default pathway in humans is death, not growth. (Reassuring, isn't it?)
Now, when you hear of cancer, malignant cancer, people tend to think of uncontrolled cell division. Essentially though, these transformed cancerous cells are immortalized. Now, many changes are required for this to occur (i.e. increased telomerase, increased bcl-2, increased myc and decreased p53). In the development of cancer, we tend to think of carcingogens consisting of both initiators and promoters. For instance, some initiators are UV radiation and tobacco smoke, usually causing DNA damage or mutation, whereas promoters tend to stimulate cell division. A few examples are phorbol esters, hormones (e.g. estrogens) and yes, growth factors.
Now, keep in mind both events, initiation and promotion, are required for the development of malignant cells. As a side note, viral infection can also lead to the two events, but I digress. Anyhow, normally a cell serves its purpose and then dies via apoptosis. However, malignant cells donít undergo apoptosis. They are, as I said before, immortal. The normal triggers to apoptosis are DNA damage, loss of cell-matrix contact, loss of cell to cell contact, and last but most certainly not least, lack of growth factors.
When you introduce growth factors, youíre providing the catalyst for cancer formation, so to speak. Letís say, for instance, you get many sunburns during your lifetime. Now, letís say that one cell has its DNA damaged or altered. This, in and of itself, isnít too much of a concern as this is only one part of the equation, the iniation. The second part is the promoter (including growth factors).
Well, letís imagine we introduce growth factors to the cell which has damaged or mutated DNA and it then begins to divide at a more and more rapid rate until it wonít stop. Voila, you have a tumor, which is now capable of even faster growth as well as being invasive (able to invade surrounding tissues) and metastatic (able to cause growth in completely unrelated and distant tissues) in regard to other tissues.
In other words, you now have a malignant tumor, which we commonly refer to as cancer. The fact is, cancer stems from just one cell, just one cell, which begins to divide uncontrollably. People often talk about GH and the side effects thereof, but what most donít realize is that many of those side effects aren't necessarily mediated by growth hormone but by IGF-1.
Many people may go their whole lives with some DNA damage (or mutation rather) and never have cancer, but with the addition of growth factors, youíre asking for trouble. Even more specifically, you can increase the risk of developing rare forms of cancer, like sarcomas, which are tumors commonly found in connective tissues (i.e. muscle, bone, cartilage, etc.)
Okay, now on to the more cosmetic side effects. With Long R3 IGF-I, it was shown to stimulate growth of the gastrointestinal tract. IGF-1 actually had no effect on body weight and wet tissue weight of the small and large intestine, whereas Long R3 IGF-I resulted in a 20% increase in the weight of the small and large intestine. This is what's causing a "GH gut" although using Long R3 IGF-I is much, much worse than using GH.
Something else to keep in mind is that Long R3 IGF-I was shown to be even more potent than IGF-1 in inhibiting apoptosis and thus its potential for causing cancer is many times greater.
Another idea is that IGF-1 may also keep telomerase activity high, which as we noted previously is a contributing factor for the loss of regulation in terms of cell division. In other words, it again can substantially increase the risk for developing cancer. Long R3 IGF-I was shown to increase telomerase activity in human prostate cancer cells, whereas IGF-1 had no effect.
So, when I tell you to stay away from IGF-1, Iím actually referring to Long R3 IGF-I as itís what's most commonly circulated and used. Although both aren't something a person should use, Long R3 IGF-1 is probably the worst choice you can make.
So, unless youíre an IFBB pro who consistently places in the top ten at popular contests, you should forget about using IGF-1, or specifically the analogue of IGF-1 called Long R3 IGF-I. Itís really not worth the risk. This, out of all the compounds that bodybuilders may use, is probably the worst in terms of potential side effects.
If you want a true distended belly and increased risk of cancer, be my guest. (47-52)
1. Tuzcu A, et al. "Insulin sensitivity and hyperprolactinemia." J Endocrinol Invest. 2003 Apr;26(4):341-6
2. Freemark M, et al. "Body weight and fat deposition in prolactin receptor-deficient mice." Endocrinology. 2001 Feb;142(2):532-7
3. Wasada T, Kawahara R, Iwamoto Y. "Lack of evidence for bromocriptine effect on glucose tolerance, insulin resistance, and body fat stores in obese type 2 diabetic patients." Diabetes Care. 2000 Jul;23(7):1039-40
4. Pijl H, et al. "Bromocriptine: a novel approach to the treatment of type 2 diabetes." Diabetes Care. 2000 Aug;23(8):1154-61
5. Ohem N, Holzl J. Some new investigations on Ilex paraguariensis - Flavonoids and triterpenes. Planta Med 1988; 54: 576
6. Bisset NG, ed. Herbal Drugs and Phytopharmaceuticals (Wichtl M, ed., German edition). Stuttgart: Medpharm, 1994
7. Duke JA. Handbook of Medicinal Herbs. Boca Raton: CRC, 1985
8. Martindale: The Extra Pharmacopoeia, 29th edn. (Reynolds JEF, ed.). London: The Pharmaceutical Press, 1989
9. The Merck Index. An Encyclopedia of Chemicals, Drugs and Biologicals, 11th edn. Rahway, NJ: Merck, 1989
10. Carani C, et al. "Role of oestrogen in male sexual behaviour: insights from the natural model of aromatase deficiency." Clin Endocrinol (Oxf). 1999 Oct;51(4):517-24
11. Scordalakes EM, Imwalle DB, Rissman EF. "Oestrogen's masculine side: mediation of mating in male mice." Reproduction. 2002 Sep;124(3):331-8
12. Brady BM, et al. "Demonstration of progesterone receptor-mediated gonadotrophin suppression in the human male." Clin Endocrinol (Oxf) 2003 Apr;58(4):506-12
13. Bauer ER, et al. "Characterisation of the affinity of different anabolics and synthetic hormones to the human androgen receptor, human sex hormone binding globulin and to the bovine progestin receptor." APMIS. 2000 Dec;108(12):838-46
14. Markiewicz L, Gurpide E. "Estrogenic and progestagenic activities of physiologic and synthetic androgens, as measured by in vitro bioassays. Methods Find Exp Clin Pharmacol. 1997 May;19(4):215-22
15. Breithaupt-Grogler K, Niebch G, Schneider E et al: Dose-proportionality of oral thioctic acid - coincidence of assessments via pooled plasma and individual data. Eur J Pharm Sci 1999; 8(1):57-65
16. Hermann R, Niebch G, Borbe HO et al: Enantioselective pharmacokinetics and bioavailability of different racemic alpha-lipoic acid formulations in healthy volunteers. Eur J Pharm Sci 1996; 4:167-174
17. Gleiter CH, Schug BS, Hermann R et al: Influence of food intake on the bioavailability of thioctic acid enantiomers. Eur J Clin Pharmacol 1996; 50(6):513-514
18. Fachinformation: Pleomix-Alpha(R), alpha-Liponsaeure. Illa Health Care GmbH, Geretsried, 1996
19. Streeper RS, Henriksen EJ, Jacob S et al: Differential effects of lipoic acid steroisomers on glucose metabolism in insulin-resistant skeletal muscle. Am J Physiol 1997; 273(1 pt 1):E185-E191
20. Khamaisi M, Potashnik R, Tirosh A et al: Lipoic acid reduces glycemia and increases muscle GLUT4 content in streptozotocin-diabetic rats. Metabolism 1997; 46(7):763-768
21. Henriksen EJ, Jacob S, Streeper RS et al: Stimulated by alpha-lipoic acid of glucose transport activity in skeletal muscle of lean and obese Zucker rats. Life Sci 1997; 61(8):805-812
22. Wickramasinghe SN & Hasan R: In vitro effects of vitamin C, thioctic acid and dihydrolipoic acid on the cytotoxicity of post-ethanol serum. Biochem Pharmacol 1992; 43(3):407-411
23. Dimpfel W, Spueler M, Pierau F-K et al: Thioctic acid induces dose-dependent sprouting of neurites in cultured rat neuroblastoma cells. Dev Pharmacol Ther 1990; 14(3):193-199
24. Prehn JHM, Karkoutly C, Nuglisch J et al: Dihyrolipoate reduces neuronal injury after cerebral ischemia. J Cereb Blood Flow Metab 1992; 12(1):78-87
25. Burkart V, Koike T, Brenner HH et al: Dihydrolipoic acid protects pancreatic islet cells from inflammatory attack. Agents Actions 1993; 38(1-2):60-65
26. Bauer A, Harrer T, Peukert M et al: Alpha-lipoic acid is an effective inhibitor of human immuno-deficiency Virus (HIV-1) replication. Klin Wochenschr 1991; 69(15):722-724
27. Suzuki YJ, Aggarwal BB & Packer L: alpha-Lipoic acid is a potent inhibitor of NF-kappaB activation in human T cells. Biochem Biophys Res Commun 1992; 189(3):1709-1715
28. Bierhaus A, Chevion S, Chevion M et al: Advanced glycation end product-induced activation of NF-kappaB is suppressed by alpha-lipoic acid in cultured endothelial cells. Diabetes 1997; 46(9):1481-1490
29. Constantinescu A, Tritschler H & Packer L: alpha-Lipoic acid protects against hemolysis of human erythrocytes induced by peroxyl radicals. Biochem Mol Biol Int 1994; 33(4):669-679
30. Greene EL, Nelson BA, Robinson KA, Buse MG. "alpha-Lipoic acid prevents the development of glucose-induced insulin resistance in 3T3-L1 adipocytes and accelerates the decline in immunoreactive insulin during cell incubation." Metabolism 2001 Sep;50(9):1063-9
31. Maddux BA, et al. "Protection against oxidative stress-induced insulin resistance in rat L6 muscle cells by mircomolar concentrations of alpha-lipoic acid." Diabetes 2001 Feb;50(2):404-10
32. Weinstein RB, Tritschler HJ, Henriksen EJ. "Antioxidant alpha-lipoic acid and protein turnover in insulin-resistant rat muscle." Free Radic Biol Med 2001 Feb 15;30(4):383-8
33. Yaworsky K, Somwar R, Ramlal T, Tritschler HJ, Klip A. "Engagement of the insulin-sensitive pathway in the stimulation of glucose transport by alpha-lipoic acid in 3T3-L1 adipocytes." Diabetologia 2000 Mar;43(3):294-303
34. Jacob S, et al. "Oral administration of RAC-alpha-lipoic acid modulates insulin sensitivity in patients with type-2 diabetes mellitus: a placebo-controlled pilot trial." Free Radic Biol Med 1999 Aug;27(3-4):309-14
35. Estrada DE, et al. "Stimulation of glucose uptake by the natural coenzyme alpha-lipoic acid/thioctic acid: participation of elements of the insulin signaling pathway." Diabetes 1996 Dec;45(12):1798-804
36. Hundal RS, et al. "Mechanism by which metformin reduces glucose production in type 2 diabetes." Diabetes 2000 Dec;49(12):2063-9
37. Anderwald C, et al. "Inhibition of glucose production and stimulation of bile flow by R (+)-alpha-lipoic acid enantiomer in rat liver." Liver 2002 Aug;22(4):355-62
38. Saengsirisuwan V, Perez FR, Kinnick TR, Henriksen EJ. "Effects of exercise training and antioxidant R-ALA on glucose transport in insulin-sensitive rat skeletal muscle." J Appl Physiol 2002 Jan;92(1):50-8
39. Evans JL, Goldfine ID. "Alpha-lipoic acid: a multifunctional antioxidant that improves insulin sensitivity in patients with type 2 diabetes." Diabetes Technol Ther 2000 Autumn;2(3):401-13
40. Saengsirisuwan V, Kinnick TR, Schmit MB, Henriksen EJ. "Interactions of exercise training and lipoic acid on skeletal muscle glucose transport in obese Zucker rats." J Appl Physiol 2001 Jul;91(1):145-53
41. Konrad T. "alpha-Lipoic acid treatment decreases serum lactate and pyruvate concentrations and improves glucose effectiveness in lean and obese patients with type 2 diabetes." Diabetes Care 1999 Feb;22(2):280-7
42. Jacob S, et al. "Enhancement of glucose disposal in patients with type 2 diabetes by alpha-lipoic acid." Arzneimittelforschung 1995 Aug;45(8):872-4
43. Jacob S, Rett K, Henriksen EJ, Haring HU. "Thioctic acidóeffects on insulin sensitivity and glucose-metabolism." Biofactors 1999;10(2-3):169-74
44. Jacob S, Henriksen EJ, Tritschler HJ, Augustin HJ, Dietze GJ. "Improvement of insulin-stimulated glucose-disposal in type 2 diabetes after repeated parenteral administration of thioctic acid." Exp Clin Endocrinol Diabetes 1996;104(3):284-8
45. Bigsby RM, Caperell-Grant A, Madhukar BV. "Xenobiotics released from fat during fasting produce estrogenic effects in ovariectomized mice." Cancer Res. 1997 Mar 1;57(5):865-9
46. McCurdy CE, Davidson RT, Cartee GD. "Brief calorie restriction increases Akt2 phosphorylation in insulin-stimulated rat skeletal muscle." Am J Physiol Endocrinol Metab. 2003 Oct;285(4):E693-E700.
47. Steeb CB, Trahair JF, Read LC. "Administration of insulin-like growth factor-I (IGF-I) peptides for three days stimulates proliferation of the small intestinal epithelium in rats." Gut. 1995 Nov;37(5):630-8
48. Wetterau LA, Francis MJ, Ma L, Cohen P. "Insulin-like growth factor I stimulates telomerase activity in prostate cancer cells." J Clin Endocrinol Metab. 2003 Jul;88(7):3354-9
49. Devi GR, Graham DL, Oh Y, Rosenfeld RG. "Effect of IGFBP-3 on IGF- and IGF-analogue-induced insulin-like growth factor-I receptor (IGFIR) signalling." Growth Horm IGF Res. 2001 Aug;11(4):231-9
50. Nickerson T, Huynh H, Pollak M. "Insulin-like growth factor binding protein-3 induces apoptosis in MCF7 breast cancer cells." Biochem Biophys Res Commun. 1997 Aug 28;237(3):690-3
51. Vink-van Wijngaarden T, Pols HA, Buurman CJ, Birkenhager JC, van Leeuwen JP. "Inhibition of insulin- and insulin-like growth factor-I-stimulated growth of human breast cancer cells by 1,25-dihydroxyvitamin D3 and the vitamin D3 analogue EB1089." Eur J Cancer. 1996 May;32A(5):842-8
52. Wetterau LA, Francis MJ, Ma L, Cohen P. "Insulin-like growth factor I stimulates telomerase activity in prostate cancer cells." J Clin Endocrinol Metab. 2003 Jul;88(7):3354-9
- 04-14-2004, 11:42 PM
I think that was posted before and some there has been disagreements with some of the conculsions drawn from the research cited..
04-15-2004, 04:06 PM
04-15-2004, 05:08 PM
It is very incorrect. If you actually go through the studies, they support the opposite of what he says. This has one has been torn apart many times.
For answers to board issues, read the Suggestion and News forum at the bottom of the main page.
04-15-2004, 07:51 PM
Wow. I thought I did my reasearch on this product. I have not found any literature this alarming. Bobo, a little reassurance out of a vet would come in handy right now. I'm on day 4 of R3.
04-15-2004, 09:30 PM
Here is an example:
"Okay, now on to the more cosmetic side effects. With Long R3 IGF-I, it was shown to stimulate growth of the gastrointestinal tract. IGF-1 actually had no effect on body weight and wet tissue weight of the small and large intestine, whereas Long R3 IGF-I resulted in a 20% increase in the weight of the small and large intestine. This is what's causing a "GH gut" although using Long R3 IGF-I is much, much worse than using GH."
The GH gut is caused from extreme high doses of GH over a long peroid of time. GH's anabolic effect and growth is FROM IGF-1 (increased GH equates to increased heaptic IGF-1) yet he says regular IGF-1 has no effect on weight and wet tissue. He contradicts himself more than once in this article.
Here is another:
"When you introduce growth factors, youíre providing the catalyst for cancer formation, so to speak. Letís say, for instance, you get many sunburns during your lifetime. Now, letís say that one cell has its DNA damaged or altered. This, in and of itself, isnít too much of a concern as this is only one part of the equation, the iniation. The second part is the promoter (including growth factors)."
One cell has its DNA damaged? In other words, a mutation. Guess what, the same chances apply whether your using IGF-1 or not. If you get cancer, stop using IGF-1. If you get cancer stop using ANYTHING that increased growth and that includes steroids and/or prohormones. In no way does IGF-1 increase the chance of cancer. It will increase the rate of growth of cancerous cells if you actually get cancer. By then, you have bigger fish to fry.
And yet another:
"So, unless youíre an IFBB pro who consistently places in the top ten at popular contests, you should forget about using IGF-1, or specifically the analogue of IGF-1 called Long R3 IGF-I. Itís really not worth the risk. This, out of all the compounds that bodybuilders may use, is probably the worst in terms of potential side effects."
Wrong. rIGF-1 will cause many more side effects due to the amount AND frequency you need to use it because of its short half-life compared to Long R3.
The whole problem with this article is that he uses studies from pigs, rats and humans. Usually you can form a decent theory but in this case you can't because IGF-1 has clearly shown to react different'y in all those examples. Its anabolic in rats, catabolic in pigs and has different effect in humans. What he's doing is finding a negative study done on rats and pigs then euqating it to humans when the effects are clearly not the same.
Here is a good artilce from Dr. Katz about the effects of IGF-1.
Passages taken from "Grow Young With HGH" by Ronald Klatz, MD, president of the Academy of Anti-Aging Medicine.
The most abundant hormone made by the pituitary gland is human growth hormone, also called somatotrophin. Growth hormone production hits its peak during adolescence. Most HGH is secreted into the bloodstream in brief bursts, and most HGH secretion takes place during the early hours of REM (deep) sleep.
Once in the bloodstream, human growth hormone stays there for only a short time, only a few minutes, just long enough to stimulate its uptake into the liver, where it is then converted into growth factors. The most important of these growth factors is called IGF-1, short for Insulin-like Growth Factor-1. IGF-1 is also known as somatomedin C.
Growth hormone exerts its actions either directly or indirectly through its intermediary insulin growth factors (IGF-1) to every organ system of the body. Almost nothing escapes its magic touch. In the same ways that it grows the bones of young children, it increases the size of most organs and tissue. Even the brain is affected. The latest studies in animals show that it can regenerate damaged brain tissue.
It is IGF-1, rather than growth hormone itself, which can vary widely through the day, that is used as a measurement of how much growth hormone is being secreted by the body. IGF-1 is directly responsible for most of the benefits and actions associated with HGH. IGF-1 is 10 times more potent than human growth hormone and is now under investigation as a separate drug for many of the same indications of human growth hormone. Phil Micans of International Aging Systems in London believes that IGF-1 will be the hormone of choice in a few years.
HGH and IGF-1 Get at the Blueprint of Aging
"The blueprint of aging is in the DNA under the hood of the telomere", the "clock" at the end of every chromosome that is shortened with each cell division, says noted plastic surgeon and antiaging researcher, Vincent Giampapa, MD, director of clinical research at the Longevity Institute International in Montclair, New Jersey. To actually reverse aging at the cellular level, we will need a substance that will restore telomere length and like a genie turn old cells into young ones. That is not yet available, although Giampapa believes it will be in less than a decade. Until then, growth hormone and its attendant hormone IGF-1 can do the next best thing, help keep the cell in as healthy a state as possible.
The cell's ability to function depends on the genetic material, the DNA, in the nucleus of the cell which codes for all the proteins, hormones, and enzymes that make the cell run. The DNA is like an army under constant attack from oxygen free-radicals, ultraviolet light, the heat of the body, and other damaging factors. Although the DNA has the ability to repair itself, it falls down on the job with age, a victim of the same aging process that affects the cell. At the same time, damage is accumulating in the energy center of the cell, the mitochondria, which has its own DNA. Up until now, one of the few ways we could limit the damage to the DNA was to take antioxidant supplements such as vitamin C and E to bolster our own defenses.
But, according to Dr. Giampapa and Thierry Hertoghe, MD, a physician specializing in hormone replacement therapy in Brussels, the latest European research shows that human growth hormone and IGF-1 can go further than antioxidants and can do what antioxidants cannot. Human growth hormone and IGF-1 act like carriers to bring the cell the raw materials it needs for renovation and repair. IGF-1 launches the delivery of the nucleic acids, DNA and RNA, right into the cell nucleus, where the DNA resides. The nucleic acids are used to repair damage to the DNA and stimulate cell division. Growth hormone initiates the transport of amino acids, the building blocks of protein, and nucleic acids into the cytoplasm of the cell, the area outside the nucleus. This includes the cell membranes and intracellular organelles, such as the mitochondria. In this way, human growth hormone and IGF-1 don't just minimize the damage to the DNA and cellar structures, they help heal the cell and the DNA. These two hormones actually treat the blueprints of aging.
Information on IGF-1
IGF-1 is the other end of the growth hormone chain, the downstream player that actually exerts most of the effects we associate with human growth hormone. IGF-1 is causing a great deal of excitement among two groups, researchers who are exploring its vast potential and bodybuilders who are already using it and claiming eyepopping gains in muscle.
IGF-1 More Potent Than Human Growth Hormone
Human growth hormone exerts most of its effects through IGF-1. Therefore, it is not surprising that IGF-1 injections will do for you what human growth hormone does--and then some, according to its proponents. It increases lean body mass, reduces fat, builds bone, muscle, and nerves. By taking it directly, you bypass the pituitary gland, which may be "burnt out" with aging.
IGF-1 appears to be even more potent than growth hormone in its anti-aging action. According to Keith Kelly, Ph.D., who did the work showing that growth hormone reversed the shrinking of the thymus, when he does his experiments on cells in culture, only IGF-1--and not growth hormone-- works. But both IGF-1 and growth hormone work in the living animal. "I know that both growth hormone and IGF-1 are substantially elevated in the old animals treated with growth hormone," he says, "but my prediction is that the main player is going to be IGF-1."
IGF-1 and It's Potentials
IGF-1 Preventing Brain Aging and Disease
One of the spectacularly exciting uses of growth hormone and IGF-1 may be to prevent and treat the effects of brain aging. In an experiment that has momentous implications for brain injury, stroke, aging, and neurodegenerative disease, a team of scientists in New Zealand showed that IGF-1 can stop the death of cells in the brain. Barbara Johnston, Peter Gluckman, and their colleagues at the University of Auckland found that injections of IGF-1 given 2 hours after brain injury in fetal lambs rescued the damaged neurons and salvaged cells that would otherwise have died during apoptosis, which is the programmed cell death that is believed to cause the loss of brain cells for up to 3 days after the original injury. The treatment was effective in stopping the cell death throughout the brain, including the hippocampus, the cortex, the areas associated with thinking and memory. The treatment was also effective in the striatum, the part of the brain that plays a role in Parkinson's disease in humans. IGF-1 replacement was also found to reduce seizures in animals with brain damage.
These researchers also suggest that IGF-1 might be used to inhibit the effects of neonatal hypoxia during birth (lack of oxygen to the brain) which can leave a baby with permanent brain damage. If IGF-1 can stop the programmed death of cells, then this opens up a world of undreamed-of-possibilities. For instance, the programmed death of cardiac cells after a heart attack leaves the victim with a heart full of dead tissue that before could not be repaired. Brain tissue is destroyed due to a stroke (CVA), and this cell death many times leaves the victim unable to walk, talk, or think clearly. It may also play a role in other neurodegenerative diseases such as Alzheimer's disease, muscular dystrophy, and multiple sclerosis. For the first time we may have a weapon against death at the cellular level.
IGF-1 Improving Glucose Metabolism
As its name indicates IGF-1, or insulin-like growth factor-1, has similar properties to insulin, and it has been shown to improve blood sugar profiles in type 2 diabetic patients. High doses of growth hormone have been shown to increase insulin resistance, but IGF-1 administration actually normalized the insulin resistance in a group of healthy volunteers.
In the latter study, Nelly Mauras and Bernard Beaufrere of the Nemours Children's Clinic in Jacksonville, Florida, were looking at several different things: the effect of IGF-1 on protein metabolism; its ability to stop the protein-wasting caused by glucocorticosteroid drugs like prednisone, and its effect on insulin and glucose metabolism. They divided the volunteers into three groups who got one of the following: IGF-1 alone, IGF-1 plus prednisone, and prednisone alone. The study found that IGF-1 at 100 micrograms per kilogram of body weight given twice daily enhanced the body's protein metabolism in the same way as growth hormone. Like growth hormone, it markedly decreased the protein breakdown in the volunteers who were taking prednisone. But whereas growth hormone in an earlier study caused carbohydrate intolerance and insulin resistance when given in combination with prednisone, IGF-1 did not cause these diabetes-like effects. Instead, those subjects who received IGF-1 along with prednisone had normal glucose metabolism. This was remarkable, say the researchers, in light of the fact that glucocorticoids are known to suppress circulating insulin and decrease insulin sensitivity. As a result of this and previous studies, the researchers believe that IGF-1 offers promise in the treatment of protein catabolic states, such as patients who require IV feedings after surgery.
IGF-1 Helping Diabetes
Two 1997 double-blind clinical studies showed that recombinant IGF-1 injections can markedly reduce the need for insulin by up to 45% in patients with insulin-dependent diabetes mellitus. One study involved 8 adults between ages 24 and 49 and the other 43 children and adolescents between the ages of 8 and 17. In the adult trial, IGF-1 also lowered the total cholesterol and triglycerides after only four days of treatment.
While these were short term trials lasting nineteen days and four weeks, respectively, that fact that the insulin requirement dropped markedly and there were no serious side effects make IGF-1 a promising drug for the treatment of diabetes. While it does not do away with the need for insulin, it improved the control of blood sugar and thus may help prevent the dire complications of diabetes, including heart disease, blindness, and peripheral nerve damage that can lead to amputation.
IGF-1 Regenerating Nerves
Another exciting potential use of IGF-1 is in the repair of peripheral nerve tissue that has been damaged by injury or illness. If a nerve is torn in the arm or leg, it means that the connection to the muscle may be impaired, and as a result there is loss of movement and the muscle atrophies. While peripheral nerves can regenerate to some extent, severe tears of more than a few millimeters may result in permanent injury. Now IGF-1 has repaired and reconnected severed nerve endings of up to a distance of 6 millimeters, a feat previously unheard of.
Swedish scientist Hans-Arne Hansson of the Institute of Neurobiology at the University of Goteborg found that IGF-1 in combination with other growth factors could stimulate even more dramatic regeneration. "IGF-1 by itself and in combination with other growth factors is likely to be of importance in promoting healing and repair processes in clinical practice within a few years," he writes.
In studies of cells in culture and in animals, IGF-1 has been shown to have remarkable effects on the spinal cord motor neurons. It increased motor neuron activity in spinal cord cultures by 150 to 270 percent. And it significantly decreased programmed cell death in developing chick embryos. In animal studies, it enhanced the sprouting of axons of the spinal cord motor neurons. And it increased intramuscular nerve sprouting a whopping ten fold when it was given to normal adult rats. In fact, according to a group of researchers at Cephalon, Inc., in West Chester, Pennsylvania, IGF-1 may be the "long-sought endogenous motor neuron sprouting factor."
The implications of this work for helping people is nothing short of mind-boggling. If IGF-1 can regenerate spinal cord motor neurons, it may be useful in treating amyotrophic lateral sclerosis (ALS), a devastating disease in which the loss of spinal cord and cortical motor neurons results in complete paralysis and death. It may also be useful for peripheral neuropathies, such as Charcot-Marie-Tooth syndrome.
John Wittig, MD, of UCLA has been using IGF-1 to prevent AIDS wasting in HIV infected patients. IGF-1 may allow more aggressive chemotherapy of certain cancers, since drugs like vincristine and cisplatin can cause peripheral neuropathies at higher doses.
The Growth Factor Army
IGF-1 is only one of the body's many growth factors that are now being identified, isolated, and cloned using genetic engineering technology for use as drugs. As growth factor researcher Eric Dupont, Ph.D., says, "Growth hormone is the general and growth factors are the foot soldiers." Growth factors function like hormones, hooking onto the receptors of cells and sending a biochemical signal across the cell's interior. Whereas hormones usually send long distance messages, growth factors for the most part do local calls.
IGF-1, The Bodybuilder's Dream
A number of world-class bodybuilders are using IGF-1 and reporting massive muscle magnification of up to 20 pounds. An article in Muscle Mass 2000 trumpets IGF-1 as "Possibly the Most Potent Bodybuilding Drug Ever!" According to author T.C. Luoma, "IGF-1 is out there on the streets of America right now; it's being sold out of the trunks of cars in Venice and brown paper packages containing it are being discreetly handed out at Southern California gyms." While there are no controlled studies supporting the musclemen's claims, the anecdotal evidence is building up. "Bodybuilders are claiming they are experiencing drops of 5% body fat in a month, while increases in lean body mass and strength are 'incredible.' Statements like, 'It's the most wonderful stuff in the world, and 'I couldn't believe it man' are the norm."
There are skeptics, such as Mauro Di Pasquale, MD, an expert in performance-enhancing compounds, but there is a rationale for the belief that HGH taken with IGF-1 will work better. There is a feedback mechanism between the human growth hormone in the pituitary gland and the IGF-1 in the liver. The human growth hormone stimulates the release of IGF-1, but when the levels of IGF-1 rise to a certain point in the circulation, it signals the shutdown of growth hormone. But there is a lag time in all of this, which means that growth hormone levels increase at night and IGF-1 levels increase during the day. Bodybuilders hope that taking the two together will have a double-fisted effect on protein synthesis
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04-16-2004, 08:51 AM
Isn't it great guys, that we have such knowledgeable bro's for mods in here?! Amen to that.
I admit that after readint this first post I was mildly disburbed. After reading Bobo's post w/studies, I'm less so, but still realize that this stuff is a double edge sword in terms of benefits/potential risks.
I am curious about something, if you Bobo, or anyone else knows the answer to this..........
Under another thread in this topic, I read an article that talks about taking L3 IGF within 15 minutes PWO. I'm paraphrasing here, but in essence, the damage to our muscle tissue induced by heavy weight training actually increases the number of "receptors" of our muscle tissue for IGF, and that by taking IGF in conjunction with heavy weight training, we are in effect, increasing the affinity for IGF to specifically targeet where we desire it's effects......... in our muscle tissue, RATHER than it generally affecting all tissue throughout our bodies.
#1. Is this concept true?
#2. Is a dosage of between 25 mcgs and 50 mcgs each P.w.o. day over a 30 day period a small enough dosage that it's target is (all, or at most probably) our muscle tissue, rather than say, damaged skin cells from childhood sun tans with mutated DNA?
I suppose that like most things in life, these things can't be known with certainty, and that we're all different insofar as risks of sides from ANYTHING. But I'd be interested in hearing even an educated best guess.
04-18-2004, 06:44 PM
PC1, it easily could be true. IGF-1 and insulin's actions are similar in some aspects so post workout should be an optimal time to dose it.
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