somatomedin C

ソマトメジンC

WordNet

1. the 3rd letter of the Roman alphabet (同)c
2. (music) the keynote of the scale of C major
3. a general-purpose programing language closely associated with the UNIX operating system

PrepTutorEJDIC

1. carbonの化学記号
2. cesiumの化学記号
3. cadmiumの化学記号

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/03/25 14:13:52」(JST)

wiki en

[Wiki en表示]

Insulin-like growth factor 1 (somatomedin C)
PDB rendering based on 1bqt.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1B9G, 1BQT, 1GF1, 1GZR, 1GZY, 1GZZ, 1H02, 1H59, 1IMX, 1PMX, 1TGR, 1WQJ, 2DSP, 2DSQ, 2DSR, 2GF1, 3GF1, 3LRI
Identifiers
Symbols	IGF1 ; IGF-I; IGF1A; IGFI
External IDs	OMIM: 147440 MGI: 96432 HomoloGene: 515 GeneCards: IGF1 Gene
Gene ontology Molecular function • insulin receptor binding • insulin-like growth factor receptor binding • integrin binding • hormone activity • protein binding • growth factor activity Cellular component • extracellular region • extracellular space • plasma membrane • insulin-like growth factor binding protein complex • platelet alpha granule lumen Biological process • skeletal system development • cell activation • blood vessel remodeling • platelet degranulation • DNA replication • cellular component movement • signal transduction • Ras protein signal transduction • muscle organ development • blood coagulation • positive regulation of cell proliferation • negative regulation of cell proliferation • glycolate metabolic process • glial cell differentiation • positive regulation of cardiac muscle hypertrophy • positive regulation of phosphatidylinositol 3-kinase signaling • skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration • muscle hypertrophy • myotube cell development • positive regulation of smooth muscle cell migration • positive regulation of cerebellar granule cell precursor proliferation • water homeostasis • proteoglycan biosynthetic process • platelet activation • mammary gland development • exocrine pancreas development • regulation of establishment or maintenance of cell polarity • positive regulation of protein import into nucleus, translocation • negative regulation of smooth muscle cell apoptotic process • multicellular organism growth • bone mineralization involved in bone maturation • regulation of multicellular organism growth • positive regulation of activated T cell proliferation • positive regulation of tyrosine phosphorylation of Stat5 protein • positive regulation of DNA binding • positive regulation of MAPK cascade • positive regulation of insulin-like growth factor receptor signaling pathway • cellular protein metabolic process • myoblast differentiation • positive regulation of osteoblast differentiation • positive regulation of glycogen biosynthetic process • positive regulation of DNA replication • positive regulation of glycolytic process • positive regulation of mitosis • positive regulation of transcription, DNA-templated • positive regulation of transcription from RNA polymerase II promoter • positive regulation of glucose import • positive regulation of Ras protein signal transduction • insulin-like growth factor receptor signaling pathway • phosphatidylinositol-mediated signaling • positive regulation of fibroblast proliferation • lung alveolus development • positive regulation of smooth muscle cell proliferation • branching morphogenesis of an epithelial tube • inner ear development • chondroitin sulfate proteoglycan biosynthetic process • positive regulation of epithelial cell proliferation • positive regulation of peptidyl-tyrosine phosphorylation • myoblast proliferation • positive regulation of protein kinase B signaling • lung vasculature development • lung lobe morphogenesis • Type I pneumocyte differentiation • Type II pneumocyte differentiation • prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis • prostate gland growth • prostate gland stromal morphogenesis • negative regulation of androgen receptor signaling pathway • negative regulation of ERK1 and ERK2 cascade • positive regulation of calcineurin-NFAT signaling cascade • negative regulation of release of cytochrome c from mitochondria • extrinsic apoptotic signaling pathway in absence of ligand • positive regulation of myoblast proliferation • negative regulation of extrinsic apoptotic signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3479	16000
Ensembl	ENSG00000017427	ENSMUSG00000020053
UniProt	P05019	P05017
RefSeq (mRNA)	NM_000618	NM_001111274
RefSeq (protein)	NP_000609	NP_001104744
Location (UCSC)	Chr 12: 102.79 – 102.87 Mb	Chr 10: 87.86 – 87.94 Mb
PubMed search	[1]	[2]

Insulin-like growth factor 1 (IGF-1), also called somatomedin C, is a protein that in humans is encoded by the IGF1 gene. IGF-1 has also been referred to as a "sulfation factor" 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.

IGF-1 consists of 70 amino acids in a single chain with three intramolecular disulfide bridges. IGF-1 has a molecular weight of 7,649 daltons.

Synthesis and circulation

See also: Neurobiological effects of physical exercise § IGF-1 signaling

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.IGFBP-1 is regulated by insulin.

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.

3-d model of IGF-1

Protein intake increases IGF-1 levels in humans, independent of total calorie consumption. Factors that are known to cause variation in the levels of growth hormone (GH) and IGF-1 in the circulation include: insulin levels, 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.

Fasting, including intermittent fasting, can reduce IGF-1 levels rapidly and dramatically. It may be, however, that fasting increases IGF-1 levels because fasting causes very low blood sugar, which in turn stimulates the release of growth hormone by the pituitary, which in turn increases IGF-1.

Mechanism of action

Its primary action is mediated by binding to its specific receptor, the insulin-like growth factor 1 receptor (IGF1R), which is 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 AKT signaling pathway, a stimulator of cell growth and proliferation, and a potent inhibitor of programmed cell death . 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 the IGF-1 that 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 0.1 times 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 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.

Insulin-like growth factor 1 receptor (IGF-1R) and other tyrosine kinase growth factor receptors signal through multiple pathways. A key pathway is regulated by phosphatidylinositol-3 kinase (PI3K) and its downstream partner, the mammalian target of rapamycin (mTOR). Rapamycins complex with FKBPP12 to inhibit the mTORC1 complex. mTORC2 remains unaffected and responds by upregulating Akt, driving signals through the inhibited mTORC1. Phosphorylation of eukaryotic initiation factor 4e (eif-4E) [4EBP] by mTOR inhibits the capacity of 4EBP to inhibit eif-4E and slow metabolism.

Insulin-like growth factor 1 has been shown to bind and interact with all the IGF-1 binding proteins (IGFBPs), of which there are seven: IGFBP1, IGFBP2, IGFBP3, IGFBP4, IGFBP5, IGFBP6, and IGFBP7. Some 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-2 receptor" (also called the mannose-6 phosphate receptor). The insulin-like 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.

A splice variant of IGF-1 sharing an identical mature region, but with a different E domain is known as mechano-growth factor (MGF).

Clinical significance

Dwarfism

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 3 SD. 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.

People with Laron syndrome have strikingly low rates of cancer and diabetes.

Acromegaly

Acromegaly is s a syndrome that results when the anterior pituitary gland produces excess growth hormone (GH). A number of disorders may increase the pituitary's GH output, although most commonly it involves a tumor called pituitary adenoma, derived from a distinct type of cell (somatotrophs). It leads to anatomical changes and metabolic dysfunction caused by elevated GH and insulin-like growth factor I (IGF-I) levels.

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 marked 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.

As a therapeutic agent

Patients with severe primary insulin-like growth factor-1 deficiency (IGFD) may be treated with either IGF-1 alone or in combination with IGFBP-3. Mecasermin (brand name Increlex) is a synthetic analog of IGF-1 which is approved for the treatment of growth failure. IGF-1 has been manufactured recombinantly on a large scale using both yeast and E. coli.

Research

Contribution to aging

Signaling through the insulin/IGF-1-like receptor pathway is a significant contributor to biological aging in many organisms. Cynthia Kenyon showed that mutations in the daf-2 gene double the lifespan of the roundworm, C. elegans. Daf-2 encodes the worm's unified insulin/IGF-1-like receptor. Despite the impact of IGF1-like on C. elegans longevity, direct application to mammalian aging is not as clear as mammals lack dauer developmental stages. It is also inconsistent with evidence in humans.

There are mixed reports that IGF-1 signaling modulates the aging process in humans and about whether the direction of its effect is positive or negative.

Neuropathy

Therapeutic administration of neurotrophic proteins (IGF I) is associated with potential reversal of degeneration of spinal cord motor neuron axons in certain peripheral neuropathies.

Cancer

The IGF signaling pathway is implicated in some cancers. People with Laron syndrome have a lessened risk of developing cancer. Dietary interventions and modifications such as vegan diets shown to down regulate IGF-1 activity, has been associated with lower risk of cancer. However, despite considerable research, perturbations specific to cancer are incompletely delineated and clinical trials have been unsuccessful.

Stroke

IGF-1 has also been shown to be effective in animal models of stroke when combined with erythropoietin. Both behavioural and cellular improvements were found.

Clinical trials

Recombinant protein

Several companies have evaluated IGF-1 in clinical trials for a variety of indications, including type 1 diabetes, type 2 diabetes, amyotrophic lateral sclerosis (ALS aka "Lou Gehrig's Disease"), severe burn injury and myotonic muscular dystrophy (MMD). Results of clinical trials evaluating the efficacy of IGF-1 in type 1 diabetes and type 2 diabetes showed great promise in reducing hemoglobin A1C levels, as well as daily insulin consumption. However, the sponsor, Genentech, discontinued the program due to an exacerbation of diabetic retinopathy in patients coupled with a shift in corporate focus towards oncology. Cephalon and Chiron conducted two pivotal clinical studies of IGF-1 for ALS, and although one study demonstrated efficacy, the second was equivocal, and the product has never been approved by the FDA.

Small molecules that upregulate IGF-1

In a clinical trial of an investigational compound ibutamoren, which raises IGF-1 in patients, did not result in an improvement in patients' Alzheimer's symptoms. Another clinical demonstrated that Cephalon's IGF-1 does not slow the progression of weakness in ALS patients, but other studies shown strong beneficial effects of IGF-I replacement therapy in ALS patients, and therefore IGF-I may have the potential to be an effective and safe medicine against ALS, however other studies had conflicting results.

Society and culture

Insmed was found to infringe on patents licensed by Tercica, which then sought to get a U.S. district court judge to ban sales of Iplex. To settle patent infringement charges and resolve all litigation between the two companies, in March 2007 Insmed agreed to withdraw Iplex from the U.S. market, leaving Tercica's Increlex as the sole version of IGF-1 available in the United States.

Numerous sources have claimed that Deer Antler Spray, purportedly extracted from cervid sources, contains IGF-1. Credence to this claim comes from the fact that deer's antlers grow extremely rapidly and that the associated cellular factors can similarly aid in skeletal healing in humans. IGF-1 is currently banned by various sporting bodies. However, sprays and pills claiming to be 'deer antler velvet extracts' are freely available on the market. As IGF-1 is a protein, it cannot be absorbed orally since it is rapidly broken down in the gastrointestinal tract. In September 2013, the headquarters of SWATS, an infamous distributor of deer antler spray and other controversial products, was raided and ordered to shut down by Alabama's attorney general citing "numerous serious and willful violations of Alabama’s deceptive trade practices act".

References

Further reading

• Butler AA, Yakar S, LeRoith D (2002). "Insulin-like growth factor-I: compartmentalization within the somatotropic axis?". News Physiol. Sci. 17: 82–5. PMID 11909998. 
• Maccario M, Tassone F, Grottoli S, Rossetto R, Gauna C, Ghigo E (2002). "Neuroendocrine and metabolic determinants of the adaptation of GH/IGF-I axis to obesity". Ann. Endocrinol. (Paris) 63 (2 Pt 1): 140–4. PMID 11994678. 
• Camacho-Hübner C, Woods KA, Clark AJ, Savage MO (2003). "Insulin-like growth factor (IGF)-I gene deletion". Reviews in endocrine & metabolic disorders 3 (4): 357–61. doi:10.1023/A:1020957809082. PMID 12424437. 
• Dantzer B, Swanson EM (2012). "Mediation of vertebrate life histories via insulin-like growth factor-1". Biological Reviews 87 (2): 414–429. doi:10.1111/j.1469-185X.2011.00204.x. PMID 21981025. 
• Trojan LA, Kopinski P, Wei MX, Ly A, Glogowska A, Czarny J et al. (2004). "IGF-I: from diagnostic to triple-helix gene therapy of solid tumors". Acta Biochim. Pol. 49 (4): 979–90. PMID 12545204. 
• Winn N, Paul A, Musaró A, Rosenthal N (2003). "Insulin-like growth factor isoforms in skeletal muscle aging, regeneration, and disease". Cold Spring Harb. Symp. Quant. Biol. 67: 507–18. doi:10.1101/sqb.2002.67.507. PMID 12858577. 
• Delafontaine P, Song YH, Li Y (2005). "Expression, regulation, and function of IGF-1, IGF-1R, and IGF-1 binding proteins in blood vessels". Arterioscler. Thromb. Vasc. Biol. 24 (3): 435–44. doi:10.1161/01.ATV.0000105902.89459.09. PMID 14604834. 
• Trejo JL, Carro E, Garcia-Galloway E, Torres-Aleman I (2004). "Role of insulin-like growth factor I signaling in neurodegenerative diseases". J. Mol. Med. 82 (3): 156–62. doi:10.1007/s00109-003-0499-7. PMID 14647921. 
• Rabinovsky ED (2004). "The multifunctional role of IGF-1 in peripheral nerve regeneration". Neurol. Res. 26 (2): 204–10. doi:10.1179/016164104225013851. PMID 15072640. 
• Rincon M, Muzumdar R, Atzmon G, Barzilai N (2005). "The paradox of the insulin/IGF-1 signaling pathway in longevity". Mech. Ageing Dev. 125 (6): 397–403. doi:10.1016/j.mad.2004.03.006. PMID 15272501. 
• Conti E, Carrozza C, Capoluongo E, Volpe M, Crea F, Zuppi C et al. (2005). "Insulin-like growth factor-1 as a vascular protective factor". Circulation 110 (15): 2260–5. doi:10.1161/01.CIR.0000144309.87183.FB. PMID 15477425. 
• Wood AW, Duan C, Bern HA (2005). "Insulin-like growth factor signaling in fish". Int. Rev. Cytol. International Review of Cytology 243: 215–85. doi:10.1016/S0074-7696(05)43004-1. ISBN 9780123646477. PMID 15797461. 
• Sandhu MS (2005). "Insulin-like growth factor-I and risk of type 2 diabetes and coronary heart disease: molecular epidemiology". Endocrine development. Endocrine Development 9: 44–54. doi:10.1159/000085755. ISBN 3-8055-7926-8. PMID 15879687. 
• Ye P, D'Ercole AJ (2006). "Insulin-like growth factor actions during development of neural stem cells and progenitors in the central nervous system". J. Neurosci. Res. 83 (1): 1–6. doi:10.1002/jnr.20688. PMID 16294334. 
• Gómez JM (2006). "The role of insulin-like growth factor I components in the regulation of vitamin D". Current pharmaceutical biotechnology 7 (2): 125–32. doi:10.2174/138920106776597621. PMID 16724947. 
• Federico G, Street ME, Maghnie M, Caruso-Nicoletti M, Loche S, Bertelloni S et al. (2006). "Assessment of serum IGF-I concentrations in the diagnosis of isolated childhood-onset GH deficiency: a proposal of the Italian Society for Pediatric Endocrinology and Diabetes (SIEDP/ISPED)". J. Endocrinol. Invest. 29 (8): 732–7. doi:10.1007/bf03344184. PMID 17033263. 
• Zakula Z, Koricanac G, Putnikovic B, Markovic L, Isenovic ER (2007). "Regulation of the inducible nitric oxide synthase and sodium pump in type 1 diabetes". Med. Hypotheses 69 (2): 302–6. doi:10.1016/j.mehy.2006.11.045. PMID 17289286. 
• Trojan J, Cloix JF, Ardourel MY, Chatel M, Anthony DD (2007). "Insulin-like growth factor type I biology and targeting in malignant gliomas". Neuroscience 145 (3): 795–811. doi:10.1016/j.neuroscience.2007.01.021. PMID 17320297. 
• Venkatasubramanian G, Chittiprol S, Neelakantachar N, Naveen MN, Thirthall J, Gangadhar BN et al. (October 2007). "Insulin and insulin-like growth factor-1 abnormalities in antipsychotic-naive schizophrenia". Am J Psychiatry 164 (10): 1557–60. doi:10.1176/appi.ajp.2007.07020233. PMID 17898347. 

External links

• Insulin-Like Growth Factor I at the US National Library of Medicine Medical Subject Headings (MeSH)
• IGF-1 at Lab Tests Online
• IGF-1 recombinant GFP labeled at Protean Ltd.

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

• 1. インスリン様成長因子 Iの生理学 physiology of insulin like growth factor i
• 2. 成長ホルモン不感受性症候群 growth hormone insensitivity syndromes
• 3. 先端巨大症の診断 diagnosis of acromegaly
• 4. 思春期における多嚢胞性卵巣症候群の診断的評価 diagnostic evaluation of polycystic ovary syndrome in adolescents
• 5. 小児における成長ホルモン欠乏症の治療 treatment of growth hormone deficiency in children

English Journal

• Growth hormone (GH) increases cognition and expression of ionotropic glutamate receptors (AMPA and NMDA) in transgenic zebrafish (Danio rerio).

• Studzinski AL1, Barros DM2, Marins LF3.
• Behavioural brain research.Behav Brain Res.2015 Nov 1;294:36-42. doi: 10.1016/j.bbr.2015.07.054. Epub 2015 Jul 30.
• The growth hormone/insulin-like factor I (GH/IGF-I) somatotropic axis is responsible for somatic growth in vertebrates, and has important functions in the nervous system. Among these, learning and memory functions related to the neural expression of ionotropic glutamate receptors, mainly types AMPA
• PMID 26235327

• Role of IGF-I signaling in muscle bone interactions.

• Bikle DD1, Tahimic C1, Chang W1, Wang Y1, Philippou A2, Barton ER3.
• Bone.Bone.2015 Nov;80:79-88. doi: 10.1016/j.bone.2015.04.036.
• Skeletal muscle and bone rely on a number of growth factors to undergo development, modulate growth, and maintain physiological strength. A major player in these actions is insulin-like growth factor I (IGF-I). However, because this growth factor can directly enhance muscle mass and bone density, it
• PMID 26453498

• Role of extracellular matrix in development of skeletal muscle and postmortem aging of meat.

• Nishimura T1.
• Meat science.Meat Sci.2015 Nov;109:48-55. doi: 10.1016/j.meatsci.2015.05.015. Epub 2015 May 20.
• The integrity of skeletal muscle is maintained by the intramuscular connective tissues (IMCTs) that are composed of extracellular matrix (ECM) molecules such as collagens, proteoglycans, and glycoproteins. The ECM plays an important role not only in providing biomechanical strength of the IMCT, but
• PMID 26141816

Japanese Journal

• 先端巨大症に伴う下顎前突症に対して顎矯正手術を施行した1例 : 骨格・咬合・鼻形態の変化

• 嵐山 貴徳,宮城 尚史,福田 純一,齋藤 功,高木 律男
• 日本顎変形症学会雑誌 = The Japanese journal of jaw deformities 21(1), 18-29, 2011-04-15
• … The GH and somatomedin levels were high. … Subsequently, since the GH and somatomedin levels decreased almost to the normal ranges, preoperative orthodontic treatment was initiated, and bilateral sagittal splitting ramus osteotomy was performed 18 months after the tumor resection. …
• NAID 10030789224

• The Relation between Concentric and Eccentric Exercise and the Carbohydrate Metabolism in Healthy Individuals

• ZEBROWSKA Aleksandra
• バイオフィリア リハビリテーション研究 6(1), 27-34, 2010
• … Venous blood samples were drawn before and immediately after the test, and during 1-hour recovery for the determinations of hormonal and somatomedin concentrations. …
• NAID 130000657800

• 糖尿病関連諸検査--測定法,臨床的意義,評価法 血液検査 Insulin-like growth factor 1 (somatomedin C) (新時代の糖尿病学(2)病因・診断・治療研究の進歩) -- (糖尿病の疫学・病態・診断学の進歩 糖尿病検査学の進歩)

• 肥塚 直美
• 日本臨床 66(-) (937), 327-332, 2008-06
• NAID 40016102425

Related Links

• IGF - Tokyo Metropolitan Institute of Gerontology

SOMATOMEDIN C IGF2; INSULIN-LIKE GROWTH FACTOR II [別名] SOMATOMEDIN A IGF1R; INSULIN-LIKE GROWTH FACTOR I RECEPTOR キーワード インスリン様成長因子、成長ホルモン、IGFシグナル経路、癌 歴史と ...

• Somatomedin C - IGF1

Somatomedin C - You may be wondering just how IGF-1 and growth hormones work exactly. Without getting too technical, growth hormones are responsible for the growth of our bodies during adolescence.

---

★リンクテーブル★

リンク元	「インスリン様成長因子-I」
関連記事	「C」「Cs」「Cd」「c」

「インスリン様成長因子-I」

　　[★]

英

insulin-like growth factor I insuline-like growth factor-I IGF-I IGF-1

同

インスリン様増殖因子I、インスリン様成長因子I。ソマトメジンC somatomedin C, ソマトメジン somatomedin

性状

• ペプチド

産生組織

• 肝臓を始めとする多くの臓器

標的組織

• 血行性にホルモンとして、自己分泌的、傍分泌的に作用。

作用

• IGF-IはGH依存性に種々の組織で合成、分泌され、主にオートクリン作用によって組織の増殖を促進する。

分泌の調整

• 分泌促進：成長ホルモン、インスリン
• 分泌抑制：絶食(GH↑だが)、エストロゲン、コルチゾール

「C」

　　[★]

• 炭素 carbon
• シトシン cytosine
• システイン cysteine
• シチジン
• セルシウス度 摂氏 degrees Celsius degree C
• 産婦人科領域で「子宮外頚 子宮外頚部 exocervix」を表現するための略語

　 　 　 　

「Cs」

　　[★] セシウム, caesium, cesium 　

「Cd」

　　[★] カドミウム

関

cadmium

　

「c」

　　[★]

• 光速, speed of light