IGF type 1 receptor

• IGF-1受容体、IGF-1レセプター、IGF受容体1型

関

IGF-1 receptor、IGF-I receptor、insulin-like growth factor I receptor

WordNet

1. write by means of a keyboard with types; "type the acceptance letter, please" (同)typewrite
2. a small metal block bearing a raised character on one end; produces a printed character when inked and pressed on paper; "he dropped a case of type, so they made him pick them up"
3. (biology) the taxonomic group whose characteristics are used to define the next higher taxon
4. a subdivision of a particular kind of thing; "what type of sculpture do you prefer?"
5. all of the tokens of the same symbol; "the word `element contains five different types of character"
6. printed characters; "small type is hard to read"
7. identify as belonging to a certain type; "Such people can practically be typed" (同)typecast
8. the 9th letter of the Roman alphabet (同)i
9. a cellular structure that is postulated to exist in order to mediate between a chemical agent that acts on nervous tissue and the physiological response
10. writing done with a typewriter (同)typewriting

PrepTutorEJDIC

1. 〈C〉(…の)『型』,タイプ,類型,種類(kind)《+of+名》 / 〈C〉(その種類の特質を最もよく表している)『典型』,手本,模範《+of+名》 / 〈U〉《集合的に》活字;〈C〉(1個の)活字 / 〈U〉(印刷された)字体,活字 / 〈C〉(貨幣・メダルなどの)模様,図柄 / 〈C〉血液型(blood group) / …‘を'タイプに打つ / (…として)…‘を'分類する《+名+as+名(doing)》 / …‘の'型を決める / タイプライターを打つ
2. 『私は』私が
3. iodineの化学記号
4. =sense organ / 受信装置

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/09/18 13:45:11」(JST)

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[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, 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 region • extracellular space • insulin-like growth factor binding protein complex • platelet alpha granule lumen Biological process • skeletal system development • blood vessel remodeling • platelet degranulation • DNA replication • anti-apoptosis • 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 cascade • 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 • myoblast differentiation • positive regulation of osteoblast differentiation • positive regulation of glycogen biosynthetic process • positive regulation of DNA replication • positive regulation of DNA replication • positive regulation of glycolysis • positive regulation of mitosis • positive regulation of transcription, DNA-dependent • 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 a 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 cascade • 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 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_000618.3	NM_001111274.1
RefSeq (protein)	NP_000609.1	NP_001104744.1
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 17,066 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.

Recently, an efficient plant expression system was developed to produce biologically active recombinant human IGF-I (rhIGF-I) in transgenic rice grains.

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 AKT signaling 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.

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.

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 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 0.1x 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-2 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.

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

Contribution to ageing

It is now widely accepted that signaling through the insulin/IGF-1-like receptor pathway is a significant contributor to the biological aging process in many organisms. This avenue of research first achieved prominence with the work of Cynthia Kenyon, who showed that mutations in the daf-2 gene could double the lifespan of the roundworm C. elegans. daf-2 encodes the worm's unified insulin/IGF-1-like receptor.

Insulin/IGF-1-like signaling is conserved from worms to humans. In vitro experiments show that mutations that reduce insulin/IGF-1 signaling have been shown to decelerate the degenerative aging process and extend lifespan in a wide range of organisms, including Drosophila melanogaster, mice, and possibly humans. Reduced IGF-1 signaling is also thought to contribute to the "anti-aging" effects of Calorie restriction.

Nevertheless the situation in vivo is evidently different, Anabolic deficiency in men with chronic heart failure is prevalent and could have an associated detrimental impact on survival. Deficiency of anabolic hormones identifies groups with a higher mortality.

Factors influencing the levels in the circulation

3-d model of IGF-1

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. 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.

Neuropathy

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

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 -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.

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

IGF-I and Cancer

The IGF signaling pathway has a pathogenic role in cancer. Studies have shown that increased levels of IGF lead to increased growth of existing cancer cells. People with Laron syndrome have also recently been shown to be of much less risk to develop cancer.

Use as a diagnostic test

Reference ranges for IGF-1 (in ng/mL)
Age	Females		Males
	2.5th centile	97.5th centile	2.5th centile	97.5th centile
20	111	423	156	385
25	102	360	119	343
30	94	309	97	306
35	86	271	84	275
40	79	246	76	251
45	73	232	71	233
50	68	228	66	221
55	64	231	61	214
60	61	237	55	211
65	59	241	49	209
70	57	237	46	207
75	55	219	48	202

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.

As a therapeutic agent

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.

Several companies have evaluated IGF-1 in clinical trials for a variety of additional 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^{[citation needed]} 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.

However, in the last few years, two additional companies Tercica and Insmed compiled enough clinical trial data to seek FDA approval in the United States. In August 2005, the FDA approved Tercica's IGF-1 drug, Increlex, as replacement therapy for severe primary IGF-1 deficiency based on clinical trial data from 71 patients. In December 2005, the FDA also approved Iplex, Insmed's IGF-1/IGFBP-3 complex. The Insmed drug is injected once a day versus the twice-a-day version that Tercica sells.

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, Insmed in March 2007 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.

By delivering Iplex in a complex, patients might get the same efficacy with regard to growth rates but experience fewer side effects with less severe hypoglycemia^{[citation needed]}. This medication might emulate IGF-1's endogenous complexing, as in the human body 97–99% of IGF-1 is bound to one of six IGF binding proteins^{[citation needed]}. IGFBP-3 is the most abundant of these binding proteins, accounting for approximately 80% of IGF-1 binding.

In a clinical trial of an investigational compound MK-677, 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.

IGFBP-3 is a carrier for IGF-1, meaning that IGF-1 binds IGFBP-3, creating a complex whose combined molecular weight and binding affinity allows the growth factor to have an increased half-life in serum. Without binding to IGFBP-3, IGF-1 is cleared rapidly through the kidney, due to its low molecular weight. But when bound to IGFBP-3, IGF-1 evades renal clearance. Also, since IGFBP-3 has a lower affinity for IGF-1 than IGF-1 has for its receptor, IGFR, its binding does not interfere with IGF-1 function. For these reasons, an IGF-1/IGFBP-3 combination approach was approved for human treatment... brought forward by a small company called Insmed. However, Insmed fell afoul patent issues, and was ordered to desist in this approach.

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.

Interactions

Insulin-like growth factor 1 has been shown to bind and interact with all the IGF-1 Binding Proteins (IGFBPs), of which there are six (IGFBP1-6).

Specific references are provided for interactions with IGFBP3, IGFBP4, and IGFBP7.

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, et al. (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. 
• Trojan LA, Kopinski P, Wei MX, 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, 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. 243: 215–85. doi:10.1016/S0074-7696(05)43004-1. 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, 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. PMID 17033263. 
• Zakula Z, Koricanac G, Putnikovic B, et al. (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, et al. (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, Shetty KT (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)

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. 進行非小細胞肺癌に対する研究試験治療 investigational approaches for advanced non small cell lung cancer
• 3. 慢性腎疾患を有する小児における成長障害の病因、評価および診断 pathogenesis evaluation and diagnosis of growth impairment in children with chronic kidney disease
• 4. 先端巨大症の治療 treatment of acromegaly
• 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

• The role of the insulin-like growth factor signaling pathway in non-small cell lung cancer and other solid tumors.

• Scagliotti GV, Novello S.SourceDepartment of Clinical and Biological Sciences, Thoracic Oncology Unit, University of Turin, S. Luigi Hospital, Orbassano, Italy. giorgio.scagliotti@unito.it
• Cancer treatment reviews.Cancer Treat Rev.2012 Jun;38(4):292-302. Epub 2011 Sep 9.
• The type 1 insulin-like growth factor receptor (IGF-1R) and its downstream signaling components have become increasingly recognized as having a driving role in the development of malignancy, and consequently IGF-1R has become a potential target for cancer therapy. Several inhibitors of IGF-1R are in
• PMID 21907495

• Beneficial effects of fenofibrate in retinal pigment epithelium by the modulation of stress and survival signaling under diabetic conditions.

• Miranda S, González-Rodríguez Á, García-Ramírez M, Revuelta-Cervantes J, Hernández C, Simó R, Valverde ÁM.SourceInstituto de Investigaciones Biomédicas Alberto Sols (CSIC/UAM), Madrid, Spain.
• Journal of cellular physiology.J Cell Physiol.2012 Jun;227(6):2352-62. doi: 10.1002/jcp.22970.
• In this study, we found an imbalance between stress-mediated and survival signaling and elevated apoptotic markers in retinal pigment epithelium (RPE) from diabetic patients. Since fenofibric acid (FA) treatment reduces the progression of diabetic retinopathy (DR), we investigated the effect of hype
• PMID 21826649

Japanese Journal

• インスリン受容体異常症A型に対する19年間のIGF-1治療

• 原田 真耶,内潟 安子,片岡 菜奈子,三浦 順之助,望月 弘,柳沢 慶香,佐倉 宏,岩本 安彦
• 糖尿病 53(8), 626-630, 2010-08-30
• NAID 10026713561

• Effects of Topical Application of α-D-Glucosylglycerol on Dermal Levels of Insulin-Like Growth Factor-I in Mice and on Facial Skin Elasticity in Humans

• HARADA Naoaki,ZHAO Juan,KURIHARA Hiroki,NAKAGATA Naomi,OKAJIMA Kenji
• Bioscience, biotechnology, and biochemistry 74(4), 759-765, 2010-04-23
• … We have reported that topical application of capsaicin increases facial skin elasticity by increasing the production of dermal insulin-like growth factor-I (IGF-I) through stimulation of sensory neurons in mice and humans. … In this study, we examined whether topical application of α-D-glucosylglycerol (GG), a compound found in Japanese traditional brewed foods such as sake (Japanese rice wine), increases the dermal production of IGF-I in mice and increases the facial skin elasticity in females. …
• NAID 10027553739

Related Links

• Receptor, igf type 1 | Fundstellen im Internet | cyclopaedia.net

Der Begriff Receptor, igf type 1 ist im englisch-sprachigen Wikipedia aufgeführt. Dort heißt es dazu: The insulin-like growth factor 1 (IGF-1) receptor is a protein found on the surface of human cells. It is a transmembrane receptor that ...

• Receptor, igf type 1 | Résultats sur Internet | cyclopaedia.net

Le terme Receptor, igf type 1 est cité dans le Wikipedia de langue anglaise. Il est défini comme suit: The insulin-like growth factor 1 (IGF-1) receptor is a protein found on the surface of human cells. It is a transmembrane receptor that ...

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★リンクテーブル★

リンク元	「IGF-1受容体」「IGF-1レセプター」「IGF-1 receptor」「IGF受容体1型」
関連記事	「type」「I」「IGF」「typed」「typing」

「IGF-1受容体」

　　[★]

英

IGF-1 receptor、IGF type 1 receptor

関

IGF-1レセプター、IGF-Iレセプター、IGF受容体1型、インスリン様増殖因子I受容体

「IGF-1レセプター」

　　[★]

英

IGF-1 receptor、IGF type 1 receptor

関

IGF-1受容体、IGF-Iレセプター、IGF受容体1型、インスリン様増殖因子I受容体

「IGF-1 receptor」

　　[★]

• IGF-1受容体、IGF-1レセプター

関

IGF type 1 receptor、IGF-I receptor、insulin-like growth factor I receptor

「IGF受容体1型」

　　[★]

英

IGF type 1 receptor

関

IGF-1受容体、IGF-1レセプター

「type」

　　[★]

• n.

• 型、タイプ、(生物)タイプ標本

(windows)ファイル内容表示(linux -> cat])

ex. type report_20111118.jp.htm | php a.php > report_20111118.jp.jp.jp.html

関

form、mode、pattern、type specimen、typed

　 　 　 　 　 　 　 　

「I」

　　[★]

• イソロイシン isoleucine
• イノシン inosine
• 阻害剤 inhibitor
• iodine
• ヨード iodide
• I因子 factor I

　 　 　

「IGF」

　　[★]

• インスリン様増殖因子 インスリン様成長因子 insulin-like growth factor

「typed」

　　[★]

• adj.

• 型の

関

form、mode、pattern、type

「typing」

　　[★]

• n.

• タイプで打つこと、タイピング。分類