IGF-1
- Stock #966-1 (1 fl. oz. Spray)
Antler velvet is the soft, growing tissue that surrounds the forming antlers before they become calcified and hard. During the velvet stage, antlers quickly grow at a tremendous rate (up to 1 inch per day in some species). In order to maintain such accelerated growth, the cartilage, bones and supporting tissues such as blood vessels and nerves must also grow at an expedited rate. Scientists have identified multiple growth factors in antler velvet, which are responsible for stimulating such fast growth. Growth factors are proteins that bind to receptors on the surface of cells, in order to activate cellular growth and differentiation (the process by which cells acquire completely individual characteristics and/or functions). In particular, researchers have confirmed the presence of high amounts of an important growth factor called insulin-like growth factor-1 (IGF-1) in antler velvet.1-8
IGF-1 (originally called somatomedin-C) is a natural growth factor found in both animals and humans. IGF-1 is used by scientists as a marker for the level of growth hormone present in the body, as IGF-1 elicits many of the growth-promoting and metabolic effects associated with growth hormone in vivo. During youth, concentrations of IGF-1 and growth hormone are relatively high, which promote healthy muscle development and lower body fat. Following adolescence and during the early twenties, IGF-1 levels begin to decline. With advancing age, blood levels of IGF-1 decrease continuously, thus giving rise to the conclusion that the acceleration of aging is related to the decline in IGF-1 and growth hormone—this process of decline is referred to as somatopause.Thus, somatopause is associated with the loss of muscle mass and strength, as well as slower muscle protein synthesis. Somatopause is also listed among the causes of the development of bone disorders such as osteopenia (reduced bone mass).1,7-14
Although there is much still to be learned concerning the role of IGF-1 in the body, research has shown that IGF-1 stimulates whole body protein synthesis, as well as increases fat-free mass and decreases fat mass. IGF-1 plays a key role in the formation and maintenance of skeletal muscle and has been shown to produce significant increases in muscle mass and strength in animal experiments. IGF-1 has been shown to increase levels of triiodothyronine (T3), a thyroid hormone, as well as contribute to healthy immune function through its role in the regulation of thymulin secretion (a hormone produced by the thymus gland). IGF-1 even appears to be involved in sperm production in men—a recent study found that men with the lowest sperm-counts also had the lowest mean and median IGF-1 levels.9,10,15-20
In addition, because IGF-1 is structurally similar to insulin, it shares many of the biologic properties of insulin. For example, IGF-1 lowers blood glucose, suppresses circulating insulin, and increases insulin sensitivity. Studies indicate that adding IGF-I to insulin therapy improves insulin sensitivity and glycemic control, and decreases insulin requirements in individuals with Type 1 diabetes (insulin-dependent diabetes mellitus). Since IGF-I appears to improve insulin sensitivity, it may also be helpful in Type 2 diabetes (non-insulin-dependent diabetes mellitus) and other conditions associated with insulin resistance.7,10,15,21-25
There is also growing evidence that IGF-1 may be beneficial in the treatment of heart disease. Recent studies have shown that IGF-1 inhibits apoptosis (programmed cell death) of heart muscle cells and improves myocardial (heart muscle) function in experimental heart failure. Research has also shown that IGF-1 may help prevent coronary artery disease—a condition where blood vessels supplying blood to the heart (coronary arteries) are narrowed or blocked—by decreasing blood levels of lipoprotein(a), a substance similar to LDL cholesterol. Elevated serum lipoprotein(a) is a strong risk factor for coronary artery disease, because it may contribute to atherosclerotic activity—the forming of fatty plaque within the arteries—and thrombogenic activity—the forming of blood clots.26,27
Furthermore, IGF-I is an essential factor for bone formation and long bone growth and is strongly associated with bone mineral density and bone quality. In fact, serum IGF-I has been found to be an independent predictor of total bone mineral content. IGF-1 stimulates collagen synthesis, encourages the absorption of chondroitin sulfate (a structural component of connective tissue, particularly cartilage), and decreases bone matrix degradation, thus playing a role in the maintenance of bone mass. Not surprisingly, IGF-1 has been shown to be significantly lower in postmenopausal women with osteoporosis.8,28-34
The relatively high levels of IGF-1 found in deer antler velvet, along with other related growth factors, may help to explain why this ancient Asian remedy is proving to be such a remarkable natural anti-aging supplement. Unlike other “growth hormone” products available, deer antler velvet is neither the glandular extract of a dead animal, nor the result of recombinant DNA technology (genetic engineering).1,5,8
Each bottle of NSP’s IGF-1 contains at least 2,500 nanograms of IGF-1 and other naturally-occurring growth factors, derived from premium deer antler velvet. Additional contents include stevia leaf extract, purified water, natural and artificial flavors, xylitol, citric acid, lecithin, and potassium sorbate (to protect freshness).
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4Garcia, R.L., et. al. “Expression of neurotrophin-3 in the growing velvet antler of the red deer Cervus elaphus.” Journal of Molecular Endocrinology; 1997, 19(2):173-182.
5Suttie, J.M., et. al. “Elevated plasma IGF-1 levels in stags prevented from growing antlers.” Endocrinology; 1988, 122(6):3005-3007.
6Francis, S.M. & Suttie, J.M. „Detection of growth factors and proto-oncogene mRNA in the growing tip of red deer (Cervus elaphus) antler using reverse-transcriptase polymerase chain reaction (RT-PCR).” Journal of Experimental Zoology; 1998 May 1;281(1):36-42.
7“Growth Factors and Cytokines.” http://www.med.unibs.it/~marchesi/growfact.html
8Kamen PhD, B. & Kamen, P.The Remarkable Healing Power of Velvet Antler. Novato, CA: Nutrition Encounter, 1999.
9Hussain, M.A., et. al. “Insulin-like growth factor I alters peripheral thyroid hormone metabolism in humans: comparison with growth hormone.” European Journal of Endocrinology; 1996 May;134(5):563-567.
10Mauras, N., et. al. “Insulin-Like Growth Factor I and Growth Hormone (GH) Treatment in GH-Deficient Humans: Differential Effects on Protein, Glucose, Lipid, and Calcium Metabolism.” Journal of Clinical Endocrinology & Metabolism; 2000, 85(4):1686-1694.
11Ruiz-Torres, A. “The role of insulin-like growth factor 1 and insulin in ageing and atherosclerosis.” Novartis Foundation Symposium2002;242:143-153.
12Hoffman, A.R., et. al. “Functional consequences of the somatopause and its treatment.” Endocrine; 1997 Aug;7(1):73-76.
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14Kozakowski, J., et. al. “[The effect of growth hormone replacement therapy on markers of bone formation and bone mineral density in elderly men].” Polskie Archiwum Medycyny Wewnetrznej; 1998, 100(4):306-312.
15Mauras, N. & Haymond, M.W. “Metabolic effects of recombinant human insulin-like growth factor-I in humans: comparison with recombinant human growth hormone.” Pediatric Nephrology; 1996, 10(3):318-323.
16Lawlor, M. & Rotwein, P. “Coordinate Control of Muscle Cell Survival by Distinct Insulin-like Growth Factor Activated Signaling Pathways.” Journal of Cell Biology; 2000, 151(6):1131-1140.
17Barton-Davis, E.R., et. al. “Contribution of satellite cells to IGF-I induced hypertrophy of skeletal muscle.” ACTA Physiologica Scandinavica; 1999, 167(4):301-305.
18Consolini, R., et. al. “Distribution of age-related thymulin titres in normal subjects through the course of life.” Clinical and Experimental Immunology; 2000, 121(3):444-447.
19Savino, W., et. al. “The thymus gland: a target organ for growth hormone.” Scandinavian Journal of Immunology; 2002, 55(5):442-452.
20Colombo, J.B. & Naz, R.K. “Modulation of insulin-like growth factor-1 in the seminal plasma of infertile men.”Journal of Andrology; 1999, 20(1):118-125.
21Froesch, E.R., et. al. “Insulin-like growth factor-I in the therapy of non-insulin-dependent diabetes mellitus and insulin resistance.” Diabetes & Metabolism; 1996, 22(4):261-267.
22Bereket, A., et. al. “Alterations in the growth hormone-insulin-like growth factor axis in insulin dependent diabetes mellitus.” Hormone & Metabolic Research; 1999, 31(2-3):172-181.
23Carroll, P., et. al. „rhIGF-I administration reduces insulin requirements, decreases growth hormone secretion, and improves the lipid profile in adults with IDDM.” Diabetes; 1997, 46(9):1453-1458.
24—. “IGF-I treatment in adults with type 1 diabetes: effects on glucose and protein metabolism in the fasting state and during a hyperinsulinemic-euglycemic amino acid clamp.” Diabetes; 2000, 49(5):789-796.
25Zenobi, P.D., et. al. “Insulin-like growth factor-I improves glucose and lipid metabolism in type 2 diabetes mellitus.” Journal of Clinical Investigation; 1992, 90(6):2234-2241.
26Wu, W., et. al. “Expression of constitutively active phosphatidylinositol 3-kinase inhibits activation of caspase 3 and apoptosis of cardiac muscle cells.” Journal of Biological Chemistry; 2000, 275(51):40113-40119.
27Laron, Z., et. al. “Growth hormone increases and insulin-like growth factor-I decreases circulating lipoprotein(a).”European Journal of Endocrinology; 1997, 136(4):377-381.
28Bonjour, J.P., et. al. “Protein intake and bone growth.” Canadian Journal of Applied Physiology; 2001, 26 Supplement:S153-166.
29Seino, Y. „Cytokines and growth factors which regulate bone cell function.” ACTA Astronautica; 1994, 33:131-136.
30Munoz-Torres, M., et. al. “The contribution of IGF-I to skeletal integrity in postmenopausal women.” Clinical Endocrinology; 2001, 55(6):759-766.
31Boonen, S., et. al. “Deficiency of the growth hormone-insulin-like growth factor-I axis potentially involved in age-related alterations in body composition.” Gerontology; 1996, 42(6):330-338.
32Zhang, J. & Hussian, Z.M. “Insulin-like growth factor 1 regulates collagen synthesis of periodontal ligament cells by a mechanism involving inhibition of poly(ADP-ribose) synthesis]” Zhonghua Kou Qiang Yi Xue Za Zhi; 1998, 33(1):10-12.
33Silbergeld, A., et. al. “The effect of insulin-like growth factor (IGF) and of human serum on steps in proteoglycan synthesis.” ACTA Endocrinologica; 1981, 97(4):503-507.
34Boonen, S., et. al. “The prevention or treatment of age-related osteoporosis in the elderly by systemic recombinant growth factor therapy (rhIGF-I or rhTGF beta): a perspective.” Journal of Internal Medicine; 1997, 242(4):285-290.
