IGF-1 LR3 1mg x 2ml and Peg MGF 2mg x 2ml
$89.99Product is out of stock
Expected return date: 04/15/2011
IGF-1 LR3 1mg (10-pack
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Sale Price: $599.99Compared at: $699.99You Save: $100.00Product ID : IGF-1 LR3 (10-pack)Product is out of stockDescription
Insulin-like growth factor 1 (IGF-1) also known as somatomedin C or mechano growth factor is a protein that in humans is encoded by the IGF1gene.[1][2] IGF-1 has also been referred to as a "sulfation factor"[3] and its effects were termed "nonsuppressible insulin-like activity" (NSILA) in the 1970s. IGF-1 is a hormone similar in molecular structure to insulin. It plays an important role in childhood growth and continues to have anabolic effects in adults. A synthetic analog of IGF-1, mecasermin is used for the treatment of growth failure.[4] IGF-1 consists of 70 amino acids in a single chain with three intramolecular disulfide bridges. IGF-1 has a molecular weight of 7649 daltons Synthesis and circulation IGF-1 is produced primarily by the liver as an endocrine hormone as well as in target tissues in a paracrine/autocrine fashion. Production is stimulated by growth hormone (GH) and can be retarded by undernutrition, growth hormone insensitivity, lack of growth hormone receptors, or failures of the downstream signalling pathway post GH receptor including SHP2 and STAT5B. Approximately 98% of IGF-1 is always bound to one of 6 binding proteins (IGF-BP). IGFBP-3, the most abundant protein, accounts for 80% of all IGF binding. IGF-1 binds to IGFBP-3 in a 1:1 molar ratio. In rat experiments the amount of IGF-1 mRNA in the liver was positively associated with dietary casein and negatively associated with a protein free diet. Mechanism of action Its primary action is mediated by binding to its specific receptor, the Insulin-like growth factor 1 receptor, abbreviated as ""IGF1R"", present on many cell types in many tissues. Binding to the IGF1R, a receptor tyrosine kinase, initiates intracellular signaling; IGF-1 is one of the most potent natural activators of the AKTsignaling pathway, a stimulator of cell growth and proliferation, and a potent inhibitor of programmed cell death. IGF-1 is a primary mediator of the effects of growth hormone (GH). Growth hormone is made in the anterior pituitary gland, is released into the blood stream, and then stimulates the liver to produce IGF-1. IGF-1 then stimulates systemic body growth, and has growth-promoting effects on almost every cell in the body, especially skeletal muscle, cartilage, bone, liver, kidney, nerves, skin, hematopoietic cell, and lungs. In addition to the insulin-like effects, IGF-1 can also regulate cell growth and development, especially in nerve cells, as well as cellular DNA synthesis. Deficiency of either growth hormone or IGF-1 therefore results in diminished stature. GH-deficient children are given recombinant GH to increase their size. IGF-1 deficient humans, who are categorized as having Laron syndrome, or Laron's dwarfism, are treated with recombinant IGF-1. In beef cattle, circulating IGF-I concentrations are related to reproductive performance. Receptors IGF-1 binds to at least two cell surface receptors: the IGF-1 receptor (IGF1R), and the insulin receptor. The IGF-1 receptor seems to be the "physiologic" receptor - it binds IGF-1 at significantly higher affinity than IGF-1 is bound to the insulin receptor. Like the insulin receptor, the IGF-1 receptor is a receptor tyrosine kinase - meaning it signals by causing the addition of a phosphate molecule on particular tyrosines. IGF-1 activates the insulin receptor at approximately 0.1x the potency of insulin. Part of this signaling may be via IGF1R/Insulin Receptor heterodimers (the reason for the confusion is that binding studies show that IGF1 binds the insulin receptor 100-fold less well than insulin, yet that does not correlate with the actual potency of IGF1 in vivo at inducing phosphorylation of the insulin receptor, and hypoglycemia).. IGF-1 is produced throughout life. The highest rates of IGF-1 production occur during the pubertal growth spurt. The lowest levels occur in infancy and old age. Other IGFBPs are inhibitory. For example, both IGFBP-2 and IGFBP-5 bind IGF-1 at a higher affinity than it binds its receptor. Therefore, increases in serum levels of these two IGFBPs result in a decrease in IGF-1 activity. Related growth factors IGF-1 is closely related to a second protein called "IGF-2". IGF-2 also binds the IGF-1 receptor. However, IGF-2 alone binds a receptor called the "IGF II receptor" (also called the mannose-6 phosphate receptor). The insulin growth factor-II receptor (IGF2R) lacks signal transduction capacity, and its main role is to act as a sink for IGF-2 and make less IGF-2 available for binding with IGF-1R. As the name "insulin-like growth factor 1" implies, IGF-1 is structurally related to insulin, and is even capable of binding the insulin receptor, albeit at lower affinity than insulin. Regulation of aging The daf-2gene encodes an insulin-like receptor in the worm C. elegans. Mutations in daf-2 have been shown by Cynthia Kenyon to double the lifespan of the worms.[7] The gene is known to regulate reproductive development, aging, resistance to oxidative stress, thermotolerance, resistance to hypoxia, and also resistance to bacterial pathogens.[8] DAF-2 is the only insulin/IGF-1 like receptor in the worm. Insulin/IGF-1-like signaling is conserved from worms to humans. DAF-2 acts to negatively regulate the forkheadtranscription factor DAF-16 through a phosphorylation cascade. Genetic analysis reveals that DAF-16 is required for daf-2-dependent lifespan extension and dauer formation. When not phosphorylated, DAF-16 is active and present in the nucleus. Factors influencing the levels in the circulation Factors that are known to cause variation in the levels of growth hormone (GH) and IGF-1 in the circulation include: genetic make-up, the time of day, age, sex, exercise status, stress levels, nutrition level and body mass index (BMI), disease state, race, estrogen status and xenobiotic intake.[9] The later inclusion of xenobiotic intake as a factor influencing GH-IGF status highlights the fact that the GH-IGF axis is a potential target for certain endocrine disrupting chemicals - see also endocrine disruptor. Diseases of deficiency and resistance Rare diseases characterized by inability to make or respond to IGF-1 produce a distinctive type of growth failure. One such disorder, termed Laron dwarfism does not respond at all to growth hormone treatment due to a lack of GH receptors. The FDA has grouped these diseases into a disorder called severe primary IGF deficiency. Patients with severe primary IGFD typically present with normal to high GH levels, height below -3 standard deviations (SD), and IGF-1 levels below -3SD. Severe primary IGFD includes patients with mutations in the GH receptor, post-receptor mutations or IGF mutations, as previously described. As a result, these patients cannot be expected to respond to GH treatment. The IGF signaling pathway appears to play a crucial role in cancer. Several studies have shown that increased levels of IGF lead to an increased risk of cancer.[citation needed] Studies done on lung cancer cells show that drugs inhibiting such signaling can be of potential interest in cancer therapy. Use as a diagnostic test IGF-1 levels can be measured in the blood in 10-1000 ng/ml amounts. As levels do not fluctuate greatly throughout the day for an individual person, IGF-1 is used by physicians as a screening test for growth hormone deficiency and excess in acromegaly and gigantism. Interpretation of IGF-1 levels is complicated by the wide normal ranges, and variations by age, sex, and pubertal stage. Clinically significant conditions and changes may be masked by the wide normal ranges. Sequential management over time is often useful for the management of several types of pituitary disease, undernutrition, and growth problems
IGF-1 LR3 1mg x 2ml and Peg MGF 2mg x 2ml
$89.99Product is out of stock
Expected return date: 04/15/2011
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IGF-1 LR3 1mg x 2ml and Peg MGF 2mg x 2ml
$89.99
Product is out of stock
Expected return date: 04/15/2011
IGF-1 LR3 1mg (10-pack
.png "IGF-1 LR3 1mg (10-pack)")
Sale Price: $599.99
Compared at: $699.99
You Save: $100.00
Product ID : IGF-1 LR3 (10-pack)
Product is out of stock
Description
Insulin-like growth factor 1 (IGF-1) also known as somatomedin C or mechano growth factor is a protein that in humans is encoded by the IGF1gene.[1][2] IGF-1 has also been referred to as a "sulfation factor"[3] and its effects were termed "nonsuppressible insulin-like activity" (NSILA) in the 1970s.
IGF-1 is a hormone similar in molecular structure to insulin. It plays an important role in childhood growth and continues to have anabolic effects in adults. A synthetic analog of IGF-1, mecasermin is used for the treatment of growth failure.[4]
IGF-1 consists of 70 amino acids in a single chain with three intramolecular disulfide bridges. IGF-1 has a molecular weight of 7649 daltons
Synthesis and circulation
IGF-1 is produced primarily by the liver as an endocrine hormone as well as in target tissues in a paracrine/autocrine fashion. Production is stimulated by growth hormone (GH) and can be retarded by undernutrition, growth hormone insensitivity, lack of growth hormone receptors, or failures of the downstream signalling pathway post GH receptor including SHP2 and STAT5B. Approximately 98% of IGF-1 is always bound to one of 6 binding proteins (IGF-BP). IGFBP-3, the most abundant protein, accounts for 80% of all IGF binding. IGF-1 binds to IGFBP-3 in a 1:1 molar ratio.
In rat experiments the amount of IGF-1 mRNA in the liver was positively associated with dietary casein and negatively associated with a protein free diet.
Mechanism of action
Its primary action is mediated by binding to its specific receptor, the Insulin-like growth factor 1 receptor, abbreviated as ""IGF1R"", present on many cell types in many tissues. Binding to the IGF1R, a receptor tyrosine kinase, initiates intracellular signaling; IGF-1 is one of the most potent natural activators of the AKTsignaling pathway, a stimulator of cell growth and proliferation, and a potent inhibitor of programmed cell death.
IGF-1 is a primary mediator of the effects of growth hormone (GH). Growth hormone is made in the anterior pituitary gland, is released into the blood stream, and then stimulates the liver to produce IGF-1. IGF-1 then stimulates systemic body growth, and has growth-promoting effects on almost every cell in the body, especially skeletal muscle, cartilage, bone, liver, kidney, nerves, skin, hematopoietic cell, and lungs. In addition to the insulin-like effects, IGF-1 can also regulate cell growth and development, especially in nerve cells, as well as cellular DNA synthesis.
Deficiency of either growth hormone or IGF-1 therefore results in diminished stature. GH-deficient children are given recombinant GH to increase their size. IGF-1 deficient humans, who are categorized as having Laron syndrome, or Laron's dwarfism, are treated with recombinant IGF-1. In beef cattle, circulating IGF-I concentrations are related to reproductive performance.
Receptors
IGF-1 binds to at least two cell surface receptors: the IGF-1 receptor (IGF1R), and the insulin receptor. The IGF-1 receptor seems to be the "physiologic" receptor - it binds IGF-1 at significantly higher affinity than IGF-1 is bound to the insulin receptor. Like the insulin receptor, the IGF-1 receptor is a receptor tyrosine kinase - meaning it signals by causing the addition of a phosphate molecule on particular tyrosines. IGF-1 activates the insulin receptor at approximately 0.1x the potency of insulin. Part of this signaling may be via IGF1R/Insulin Receptor heterodimers (the reason for the confusion is that binding studies show that IGF1 binds the insulin receptor 100-fold less well than insulin, yet that does not correlate with the actual potency of IGF1 in vivo at inducing phosphorylation of the insulin receptor, and hypoglycemia)..
IGF-1 is produced throughout life. The highest rates of IGF-1 production occur during the pubertal growth spurt. The lowest levels occur in infancy and old age.
Other IGFBPs are inhibitory. For example, both IGFBP-2 and IGFBP-5 bind IGF-1 at a higher affinity than it binds its receptor. Therefore, increases in serum levels of these two IGFBPs result in a decrease in IGF-1 activity.
Related growth factors IGF-1 is closely related to a second protein called "IGF-2". IGF-2 also binds the IGF-1 receptor. However, IGF-2 alone binds a receptor called the "IGF II receptor" (also called the mannose-6 phosphate receptor). The insulin growth factor-II receptor (IGF2R) lacks signal transduction capacity, and its main role is to act as a sink for IGF-2 and make less IGF-2 available for binding with IGF-1R. As the name "insulin-like growth factor 1" implies, IGF-1 is structurally related to insulin, and is even capable of binding the insulin receptor, albeit at lower affinity than insulin.
Regulation of aging The daf-2gene encodes an insulin-like receptor in the worm C. elegans. Mutations in daf-2 have been shown by Cynthia Kenyon to double the lifespan of the worms.[7] The gene is known to regulate reproductive development, aging, resistance to oxidative stress, thermotolerance, resistance to hypoxia, and also resistance to bacterial pathogens.[8] DAF-2 is the only insulin/IGF-1 like receptor in the worm. Insulin/IGF-1-like signaling is conserved from worms to humans. DAF-2 acts to negatively regulate the forkheadtranscription factor DAF-16 through a phosphorylation cascade. Genetic analysis reveals that DAF-16 is required for daf-2-dependent lifespan extension and dauer formation. When not phosphorylated, DAF-16 is active and present in the nucleus.
Factors influencing the levels in the circulation
Factors that are known to cause variation in the levels of growth hormone (GH) and IGF-1 in the circulation include: genetic make-up, the time of day, age, sex, exercise status, stress levels, nutrition level and body mass index (BMI), disease state, race, estrogen status and xenobiotic intake.[9] The later inclusion of xenobiotic intake as a factor influencing GH-IGF status highlights the fact that the GH-IGF axis is a potential target for certain endocrine disrupting chemicals - see also endocrine disruptor.
Diseases of deficiency and resistance
Rare diseases characterized by inability to make or respond to IGF-1 produce a distinctive type of growth failure. One such disorder, termed Laron dwarfism does not respond at all to growth hormone treatment due to a lack of GH receptors. The FDA has grouped these diseases into a disorder called severe primary IGF deficiency. Patients with severe primary IGFD typically present with normal to high GH levels, height below -3 standard deviations (SD), and IGF-1 levels below -3SD. Severe primary IGFD includes patients with mutations in the GH receptor, post-receptor mutations or IGF mutations, as previously described. As a result, these patients cannot be expected to respond to GH treatment. The IGF signaling pathway appears to play a crucial role in cancer. Several studies have shown that increased levels of IGF lead to an increased risk of cancer.[citation needed] Studies done on lung cancer cells show that drugs inhibiting such signaling can be of potential interest in cancer therapy.
Use as a diagnostic test
IGF-1 levels can be measured in the blood in 10-1000 ng/ml amounts. As levels do not fluctuate greatly throughout the day for an individual person, IGF-1 is used by physicians as a screening test for growth hormone deficiency and excess in acromegaly and gigantism. Interpretation of IGF-1 levels is complicated by the wide normal ranges, and variations by age, sex, and pubertal stage. Clinically significant conditions and changes may be masked by the wide normal ranges. Sequential management over time is often useful for the management of several types of pituitary disease, undernutrition, and growth problems
Anastrozole 1mg x 30ml
While officially indicated for women, this drug has proven effective in the off-label use of reducing estrogens (in particular and more importantly, estradiol) in men.[citation needed] Excess estradiol in men can cause benign prostatic hyperplasia,gynecomastia, and symptoms of hypogonadism.[citation needed] Some athletes and body builders will also use anastrozole as a part of their steroid cycle to reduce and prevent symptoms of excess estrogens; in particular, gynecomastia and water retention.[citation needed] Study data currently suggest that dosages of 0.5 mg to 1 mg a day reduce serum estradiol by about 50% in men, which differs from the typical reduction in postmenopausal women.[citation needed] However the reduction may be different for men with grossly elevated estradiol (clinical data are currently lacking).
THIS PRODUCT IS NOT FOR HUMAN USE NOR IS IT INTENDED TO TREAT PREVENT OR CURE ANY DISEASES. EXTREME PEPTIDE WILL DENY ANY ORDER IF WE FEEL IT WILL NOT BE USED TO THE CONDITIONS SPECIFIED IN OUR DISCLAIMER WHICH IS AGREED UPON BEFORE ENTERING THE STORE
Product Reviews
AICA ribonucleotide (AICAR) 100mg x 2ml (5-pack)
.png "AICA ribonucleotide (AICAR) 100mg x 2ml (5-pack)")
Description
AICA ribonucleotide or AICAR (aminoimidazolecarboxamideribonucleotide) is an intermediate in the generation of inosine monophosphate, which acts as an AMP-activated protein kinase agonist.[1] It stimulates glucose uptake and increases the activity of p38 mitogen-activated protein kinases ? and ? in skeletal muscle tissue,[2] as well as suppressing apoptosis by reducing production of reactive oxygen compounds inside the cell.[3] In 2008, researchers at the Salk Institute discovered that AICAR given to experimental mice significantly improves their performance in endurance-type exercise, apparently by converting fast-twitch muscle fibers to the more energy-efficient, fat-burning, slow-twitch type. They also looked at the administration of GW 501516 (also called GW1516) in combination with AICAR. Given to mice that did not exercise, this combination activated 40% of the genes that were turned on when mice were given GW1516 and made to exercise. This suggests it may be possible to obtain some of the benefits of exercising without actually exercising.[4] Because of the enhanced endurance effects, this could potentially be used by athletes to enhance their performance
CJC 1293 2mg
Description
CJC-1293 Modified GRF (1-29)
Sequence: Tyr-d-ALA-Asp-Ala-Ile-Phe-Thr-Gln-Ser-Tyr-Arg-Lys-Val-Leu-Ala-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Leu-Ser-Arg-NH2
In the healthy human body, large amounts of growth hormone are stored in the pituitary. The cells within the pituitary release growth hormone in response to signaling by GHRH (Growth Hormone Releasing Hormone), Ghrelin (of which GHRPs - Growth Hormone Releasing Peptides - are mimetics), and are inhibited from releasing these stores by Somatostatin. GHRH and Ghrelin act on different populations of somatotropes (GH releasing cells). GHRP/Ghrelin increases the number of somatotropes releasing GH but not the amount released by each cell; GHRH affects both the number of secreting cells and - more so - the amount they each secrete. [1] GHRH and Ghrelin are released in specific patterns that vary depending on event and environment: post-exercise, in response to slow wave sleep, in certain stages of life and physical development, and so on.
Most people (even the diseased) continue to possess the ability to make GH in the pituitary. The problem is in the signalling of the pituitary to release it and make more. Even most people with diseases that affect growth hormone secretion retain the ability to continue to make GH in their pituitaries. The disease states and symptoms result, most typically, in altered (dysfunctional) GH release signaling and this also affects the ability of the pituitary to continue to make more GH. [2]
Endogenous-type GHRH, which has a forty-four amino acid long chain (and a specific shape - thus making it a peptide as well as a hormone), has been marketed for the longest as Sermorelin in comparison to the other GHRH-type peptides. However, Sermorelin has been demonstrated to be degraded rapidly in the body and is cost-inefficient. But because most patients in need of GH therapy do retain the ability to produce and secrete their own GH, treatment with a GHRH-type analog remained hypothetically preferable to exogenous GH treatment. GH itself when administered exogenously results not only in "unnatural" release patterns, it results universally in down regulation of endogenous GH production - as do many hormones when applied exogenously.[3]
Sermorelin's limitations naturally resulted in a variety of formulations of GHRH analogs for therapeutic usage. CJC-1295, discussed in another article, is a GHRH analogue with attached MPA (aka DAC), binds to albumin in the bloodstream and circulates for a week or longer. Modified GRF 1-29, which is also called D-Ala2-GHRH-(1-29), [Nle27]-hGHRH(1-29)-NH2, GHRH (1-29)NH2, or ModGRF1-29, is the bioactive portion of GHRH(1-44) with fifteen amino acids subtracted and four amino acids replaced at the weakest points in the peptide structure.
Soule et al write that "D-Ala2 substitution contributes to the enhancement of biological activity by reducing metabolic clearance." [3] In a comparison study with synthetic exogenous GH for treating prepubertal GH deficiency, Lanes and Carillo concluded that "GHRH (1-29) at the dose and schedule used is generally effective in the treatment of GH deficiency." [4]
Campbell et al explain both GHRH(1-44)'s shortcomings in treatment as well as advantages offered by Modified GRF (1-29) and specific structural differences:
Native human GRF(1-44)-NH2(hGRF44) is subject to biological inactivation by both enzymatic and chemical routes. In plasma, hGRF44 is rapidly degraded via dipeptidylpeptidase IV (DPP-IV) cleavage between residues Ala2 and Asp3. The hGRF44 is also subject to chemical rearrangement (Asn8-->Asp8, beta-Asp8 via aminosuccinimide formation) and oxidation [Met27-->Met(O)27] in aqueous environments, greatly reducing its bioactivity. It is therefore advantageous to develop long-acting GRF analogues using specific amino acid replacements at the amino-terminus (to prevent enzymatic degradation): residue 8 (to reduce isomerization) and residue 27 (to prevent oxidation). Inclusion of Ala15 substitution (for Gly15), previously demonstrated to enhance receptor binding affinity, would be predicted to improve GRF analogue potency. Substitution of [His1,Val2]-(from the mouse GRF sequence) for [Tyr1,Ala2]-(human sequence) in [Ala15,Leu27]hGRF(1-32)-OH analogues completely inhibited (24-h incubation) DPP-IV cleavage and greatly increased plasma stability in vitro. Additional substitution of Thr8 (mouse GRF sequence), Ser8 (rat GRF sequence), or Gln8 (not naturally occurring) for Asn8 (human GRF sequence) resulted in analogues with enhanced aqueous stability in vitro (i.e., decreased rate of isomerization). These three highly stable and enzymatically resistant hGRF(1-32)-OH analogues, containing His1, Val2, Thr/Gln8, Ala15, and Leu27 replacements, were then bioassay for growth hormone (GH)-releasing activity in vitro (rat pituitary cell culture) and in vivo (SC injection into pigs). Enhanced bioactivity was observed with all three hGRF(1-32)-OH analogues. In vitro, these analogues were approximately threefold more potent than hGRF44, whereas in vivo they were eleven- to thirteen fold more potent.[5]
Just as GHRH and Ghrelin work in conjunction through different means for maximal GH release within the body, exogenous GHRH such as Modified GRF (1-29) results in a synergistic effect when used with a Ghrelin mimetic, such as the hexapeptide known as GHRP-6. [6] Pandya et al also conclude that "GHRH is necessary for most of the GH response to GHRP-6 in humans." [6] Massoud et al conclude that "Hexarelin and GHRH-(1-29)-NH2 are synergistic" [7] (Ed note: Hexarelin is another Ghrelin mimetic).
Sawada writes that "findings suggest that the KP-102-induced GH secretion largely depends on GRF and the secretagogue potentiates the GRF effect by antagonizing the SS action at the level of somatotropes. It is concluded that KP-102 alone or in combination with GRF provides a means of stimulating GH secretion in the face of elevated inhibitory tone mediated by SS." [8] (Ed note: KP-102 is the Ghrelin mimetic GHRP-2)
An abstract of a review by Hamilton touches on the main advantage of GRF(1-29) over, for example, CJC-1295 or synthetic GH: ...growth hormone secretion occurs in a rhythmic pattern regulated by intricate interactions between two neurohormones: growth hormone-releasing hormone (GHRH) and somatotropin release-inhibiting factor (SRIF).[...] research also indicates that there are sexual differences in the pattern of growth hormone release and that growth hormone regulates its own secretion by means of a negative feedback system. [9]
By mimicking natural release patterns with properly dosed and timed GHRPs (Ghrelin mimetics) and GHRH-analogues, negative feedback and undesirable side effects that are typically seen in synthetic GH therapy or even with past forms of GHRH administration (such as constant low-dose administration via pump) can be avoided.
CJC 1295(MOD GRF 1-29) 2mg and GHRP-6 5mg
Sale Price: $29.99
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Product ID : CJC 1295 and GHRP-6
Description
Cjc 1295 (no dac) 2mg x 2ml and GHRP – 6 5mg x 2ml - Please see descriptions for CJC-1295 and GHRP-6
GnRH (Triptorelin) 100mcg (Buy two get one FREE!)
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Sale Price: $59.99
Compared at: $99.99
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Product ID : GnRH (Triptorelin)
Special Offer
Purchase 2 of GnRH (Triptorelin) 100mcg (Buy two get one FREE!) and get:
A $59.99 VALUE!
Description
Anabolic steroids purchased on the Internet as a cause of prolonged hypogonadotropic hypogonadism
To report a case of hypogonadotropic hypogonadism due to the chronic abuse of anabolic steroids.
Design
Case report.
Setting
Endocrinology unit of the University of Brescia.
Patient(s)
A 34-year-old man.
Intervention(s)
A single dose (100 μg) of triptorelin (triptorelin test).
Main Outcome Measure(s)
Clinical symptoms, androgen normalization, levels of serum testosterone, follicle-stimulating hormone, and luteinizing hormone.
Result(s)
Within 1 month, the patient's serum testosterone was in the normal range, and he reported a return to normal energy and libido.
Case report
A 34-year-old man presented to our department in September 2008 for loss of libido and energy and for mild depression. He was a computer programmer and a nonprofessional bodybuilder with an unremarkable personal medical history. He admitted to having used doping drugs since he was 21 years old. More specifically, he would perform cycles of intramuscular injections of nandrolone (25 mg) and stanazol (25 mg) daily for 8 weeks, followed by mesterolone (50 mg/day) for 15 days. Then he would then take clomiphene citrate (50 mg/day) for 1 week, followed by an injection of human chorionic gonadotropin (2,000 IU) three times in 1 week. He had repeated these cycles from 1995 to 2005. From 2005 to August 2008, to his nandrolone and stanazol cycle he added an intramuscular injection of boldenone (50 mg) daily for 3 weeks. He said he had bought all the drugs on the Internet.
The patient was 175 cm tall and 80 kg, and he appeared very muscular and toned. His blood pressure and pulse rate were normal. Examination of his heart, lungs, and abdomen were likewise unremarkable. The physical examination showed normal secondary sexual characteristics, but the genital examination revealed bilateral testicular atrophy (volume 2.9 mL and weak consistence). Despite his testicular atrophy, the semen analysis revealed a normal count (79 × x106spermatozoa/mlmL) and mild morphology derangements (between 46% and 58%). The blood count and chemistry were normal, but his level of creatine kinase was 454 IU/L (normal range: 20–170 IU/L), alanine aminotransferase 61 IU/L (normal range: 5–50 IU/L), and aspartate aminotransferase 23 IU/L (normal range: 5–50 IU/L).
In February 2009, the patient continued to report loss of libido and great tiredness. A second physical examination was performed. His levels of alanine transferase and creatine kinase were all within the normal range, but the endocrinologic investigations were still abnormal with the exception of sex hormone-binding globulin level. *The patients testosterone measured 0.3 ng/mL - normal range is between 2.0 ng/mL and 12 ng/ML. Because the situation had persisted for months after ASS withdrawal, we administered a single dose (100 μg) of triptorelin (triptorelin test), which showed a normal response (Fig. 1). Ten days after the triptorelin test, the patient reported a great amelioration of energy, and his serum testosterone was 7.0 ng/mL. One month later, his serum testosterone was within the normal range, and he reported a return to normal libido and energy.
Figure 1.
Triptorelin test showing a normal response.
*The latter article is intended for educational / informational purposes only. THIS PRODUCT IS INTENDED AS A RESEARCH CHEMICAL ONLYAICA ribonucleotide (AICAR) 100mg x 2ml
Description
AICA ribonucleotide or AICAR (aminoimidazolecarboxamideribonucleotide) is an intermediate in the generation of inosine monophosphate, which acts as an AMP-activated protein kinase agonist.[1] It stimulates glucose uptake and increases the activity of p38 mitogen-activated protein kinases ? and ? in skeletal muscle tissue,[2] as well as suppressing apoptosis by reducing production of reactive oxygen compounds inside the cell.[3] In 2008, researchers at the Salk Institute discovered that AICARgiven to experimental mice significantly improves their performance in endurance-type exercise, apparently by converting fast-twitch muscle fibers to the more energy-efficient, fat-burning, slow-twitch type. They also looked at the administration of GW 501516 (also called GW1516) in combination with AICAR. Given to mice that did not exercise, this combination activated 40% of the genes that were turned on when mice were given GW1516 and made to exercise. This suggests it may be possible to obtain some of the benefits of exercising without actually exercising.[4] Because of the enhanced endurance effects, this could potentially be used by athletes to enhance their performance.IGF-1 LR3 1MG (5-pack)
.png "IGF-1 LR3 1MG (5-pack)")
Sale Price: $329.99Compared at: $399.95You Save: $69.96Product ID : IGF-1 LR3 (5-pack)Product is out of stockDescription
Insulin-like growth factor 1 (IGF-1) also known as somatomedin C or mechano growth factor is a protein that in humans is encoded by the IGF1gene.[1][2] IGF-1 has also been referred to as a "sulfation factor"[3] and its effects were termed "nonsuppressible insulin-like activity" (NSILA) in the 1970s.IGF-1 is a hormone similar in molecular structure to insulin. It plays an important role in childhood growth and continues to have anabolic effects in adults. A synthetic analog of IGF-1, mecasermin is used for the treatment of growth failure.[4]IGF-1 consists of 70 amino acids in a single chain with three intramolecular disulfide bridges. IGF-1 has a molecular weight of 7649 daltonsSynthesis and circulationIGF-1 is produced primarily by the liver as an endocrine hormone as well as in target tissues in a paracrine/autocrine fashion. Production is stimulated by growth hormone (GH) and can be retarded by undernutrition, growth hormone insensitivity, lack of growth hormone receptors, or failures of the downstream signalling pathway post GH receptor including SHP2 and STAT5B. Approximately 98% of IGF-1 is always bound to one of 6 binding proteins (IGF-BP). IGFBP-3, the most abundant protein, accounts for 80% of all IGF binding. IGF-1 binds to IGFBP-3 in a 1:1 molar ratio.In rat experiments the amount of IGF-1 mRNA in the liver was positively associated with dietary casein and negatively associated with a protein free diet.Mechanism of actionIts primary action is mediated by binding to its specific receptor, the Insulin-like growth factor 1 receptor, abbreviated as ""IGF1R"", present on many cell types in many tissues. Binding to the IGF1R, a receptor tyrosine kinase, initiates intracellular signaling; IGF-1 is one of the most potent natural activators of the AKTsignaling pathway, a stimulator of cell growth and proliferation, and a potent inhibitor of programmed cell death.IGF-1 is a primary mediator of the effects of growth hormone (GH). Growth hormone is made in the anterior pituitary gland, is released into the blood stream, and then stimulates the liver to produce IGF-1. IGF-1 then stimulates systemic body growth, and has growth-promoting effects on almost every cell in the body, especially skeletal muscle, cartilage, bone, liver, kidney, nerves, skin, hematopoietic cell, and lungs. In addition to the insulin-like effects, IGF-1 can also regulate cell growth and development, especially in nerve cells, as well as cellular DNA synthesis.Deficiency of either growth hormone or IGF-1 therefore results in diminished stature. GH-deficient children are given recombinant GH to increase their size. IGF-1 deficient humans, who are categorized as having Laron syndrome, or Laron's dwarfism, are treated with recombinant IGF-1. In beef cattle, circulating IGF-I concentrations are related to reproductive performance.ReceptorsIGF-1 binds to at least two cell surface receptors: the IGF-1 receptor (IGF1R), and the insulin receptor. The IGF-1 receptor seems to be the "physiologic" receptor - it binds IGF-1 at significantly higher affinity than IGF-1 is bound to the insulin receptor. Like the insulin receptor, the IGF-1 receptor is a receptor tyrosine kinase - meaning it signals by causing the addition of a phosphate molecule on particular tyrosines. IGF-1 activates the insulin receptor at approximately 0.1x the potency of insulin. Part of this signaling may be via IGF1R/Insulin Receptor heterodimers (the reason for the confusion is that binding studies show that IGF1 binds the insulin receptor 100-fold less well than insulin, yet that does not correlate with the actual potency of IGF1 in vivo at inducing phosphorylation of the insulin receptor, and hypoglycemia)..IGF-1 is produced throughout life. The highest rates of IGF-1 production occur during the pubertal growth spurt. The lowest levels occur in infancy and old age.Other IGFBPs are inhibitory. For example, both IGFBP-2 and IGFBP-5 bind IGF-1 at a higher affinity than it binds its receptor. Therefore, increases in serum levels of these two IGFBPs result in a decrease in IGF-1 activity.Related growth factors IGF-1 is closely related to a second protein called "IGF-2". IGF-2 also binds the IGF-1 receptor. However, IGF-2 alone binds a receptor called the "IGF II receptor" (also called the mannose-6 phosphate receptor). The insulin growth factor-II receptor (IGF2R) lacks signal transduction capacity, and its main role is to act as a sink for IGF-2 and make less IGF-2 available for binding with IGF-1R. As the name "insulin-like growth factor 1" implies, IGF-1 is structurally related to insulin, and is even capable of binding the insulin receptor, albeit at lower affinity than insulin.Regulation of aging The daf-2gene encodes an insulin-like receptor in the worm C. elegans. Mutations in daf-2 have been shown by Cynthia Kenyon to double the lifespan of the worms.[7] The gene is known to regulate reproductive development, aging, resistance to oxidative stress, thermotolerance, resistance to hypoxia, and also resistance to bacterial pathogens.[8] DAF-2 is the only insulin/IGF-1 like receptor in the worm. Insulin/IGF-1-like signaling is conserved from worms to humans. DAF-2 acts to negatively regulate the forkheadtranscription factor DAF-16 through a phosphorylation cascade. Genetic analysis reveals that DAF-16 is required for daf-2-dependent lifespan extension and dauer formation. When not phosphorylated, DAF-16 is active and present in the nucleus.Factors influencing the levels in the circulationFactors that are known to cause variation in the levels of growth hormone (GH) and IGF-1 in the circulation include: genetic make-up, the time of day, age, sex, exercise status, stress levels, nutrition level and body mass index (BMI), disease state, race, estrogen status and xenobiotic intake.[9] The later inclusion of xenobiotic intake as a factor influencing GH-IGF status highlights the fact that the GH-IGF axis is a potential target for certain endocrine disrupting chemicals - see also endocrine disruptor.Diseases of deficiency and resistanceRare diseases characterized by inability to make or respond to IGF-1 produce a distinctive type of growth failure. One such disorder, termed Laron dwarfism does not respond at all to growth hormone treatment due to a lack of GH receptors. The FDA has grouped these diseases into a disorder called severe primary IGF deficiency. Patients with severe primary IGFD typically present with normal to high GH levels, height below -3 standard deviations (SD), and IGF-1 levels below -3SD. Severe primary IGFD includes patients with mutations in the GH receptor, post-receptor mutations or IGF mutations, as previously described. As a result, these patients cannot be expected to respond to GH treatment. The IGF signaling pathway appears to play a crucial role in cancer. Several studies have shown that increased levels of IGF lead to an increased risk of cancer.[citation needed] Studies done on lung cancer cells show that drugs inhibiting such signaling can be of potential interest in cancer therapy.Use as a diagnostic testIGF-1 levels can be measured in the blood in 10-1000 ng/ml amounts. As levels do not fluctuate greatly throughout the day for an individual person, IGF-1 is used by physicians as a screening test for growth hormone deficiency and excess in acromegaly and gigantism. Interpretation of IGF-1 levels is complicated by the wide normal ranges, and variations by age, sex, and pubertal stage. Clinically significant conditions and changes may be masked by the wide normal ranges. Sequential management over time is often useful for the management of several types of pituitary disease, undernutrition, and growth problemsHGH Frag 176-191 5mg
Description
The (HGH fragment 176-191) is a stabilized analogue of the growth hormone-releasing factor (GRF) that induces growth hormone (GH) in a specific and physiological manner. To date studies suggest that (HGH fragment 176-191) has several beneficial features: it reduces abdominal fat (in particular visceral fat), without compromising glycemic control (blood glucose), it increases muscle mass and improves the lipid profile. These characteristics make it an ideal candidate for the treatment of excess abdominal fat, an important aspect of HIV-associated lipodystrophy. At a dosage of 500mcg the (HGH fragment 176-191) was shown to increase lipolytic activity in adipose tissue. In other words this fragment potently burns body fat, especially stubborn adipose body fat, and it does so potently! Of significance, is that the fragment has no negative impact on insulin sensitivity, a stark contrast from its Human Growth Hormone counterpart.(Ng FM, Sun J,Sharma L, Libinaka R, Jiang WJ, and Gianello R 2000). Not only does the (HGH fragment 176-191) not interfere with the body’s natural insulin regulation as Human Growth Hormone can, the (HGH fragment 176-191) does not result in cellular proliferation as Human Growth Hormone does.
.png "AICA ribonucleotide (AICAR) 100mg x 2ml")
.png "IGF-1 LR3 1MG (5-pack)")
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