III型コラーゲン
- 関
- collagen III、collagen type III
WordNet
- write by means of a keyboard with types; "type the acceptance letter, please" (同)typewrite
- 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"
- (biology) the taxonomic group whose characteristics are used to define the next higher taxon
- a subdivision of a particular kind of thing; "what type of sculpture do you prefer?"
- all of the tokens of the same symbol; "the word `element contains five different types of character"
- printed characters; "small type is hard to read"
- identify as belonging to a certain type; "Such people can practically be typed" (同)typecast
- a paste-up made by sticking together pieces of paper or photographs to form an artistic image; "he used his computer to make a collage of pictures superimposed on a map" (同)montage
- any collection of diverse things; "a collage of memories"
- the 9th letter of the Roman alphabet (同)i
- a fibrous scleroprotein in bone and cartilage and tendon and other connective tissue; yields gelatin on boiling
PrepTutorEJDIC
- 〈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
- コラージュ / 〈C〉画面に絵具以外のいろいろな素材を貼り付けて耕成した絵 / 〈U〉1の絵画技法
- 『私は』私が
- iodine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）』「2017/11/13 20:42:09」(JST)
[Wiki en表示]
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This article's lead section does not adequately summarize key points of its contents. Please consider expanding the lead to provide an accessible overview of all important aspects of the article. Please discuss this issue on the article's talk page. (November 2016)
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| COL3A1 |
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| Available structures |
| PDB |
Ortholog search: PDBe RCSB |
| List of PDB id codes |
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2V53, 3DMW, 4AE2, 4AEJ, 4AK3, 4GYX
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| Identifiers |
| Aliases |
COL3A1, EDS4A, collagen type III alpha 1, collagen type III alpha 1 chain |
| External IDs |
OMIM: 120180 MGI: 88453 HomoloGene: 55433 GeneCards: COL3A1 |
| Gene location (Human) |
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| Chr. |
Chromosome 2 (human)[1] |
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| Band |
2q32.2 |
Start |
188,974,320 bp[1] |
| End |
189,012,746 bp[1] |
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| Gene location (Mouse) |
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| Chr. |
Chromosome 1 (mouse)[2] |
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| Band |
1 C1.1|1 23.67 cM |
Start |
45,311,538 bp[2] |
| End |
45,349,706 bp[2] |
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| RNA expression pattern |
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| More reference expression data |
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| Gene ontology |
| Molecular function |
• metal ion binding
• integrin binding
• protein binding
• platelet-derived growth factor binding
• SMAD binding
• extracellular matrix structural constituent
• protease binding
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| Cellular component |
• collagen trimer
• endoplasmic reticulum lumen
• proteinaceous extracellular matrix
• extracellular space
• collagen type III trimer
• extracellular matrix
• extracellular region
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| Biological process |
• positive regulation of Rho protein signal transduction
• skeletal system development
• negative regulation of neuron migration
• response to cytokine
• response to mechanical stimulus
• aging
• extracellular matrix organization
• platelet activation
• heart development
• peptide cross-linking
• negative regulation of immune response
• blood vessel development
• regulation of immune response
• cerebral cortex development
• collagen catabolic process
• cellular response to amino acid stimulus
• integrin-mediated signaling pathway
• response to radiation
• cell-matrix adhesion
• digestive tract development
• transforming growth factor beta receptor signaling pathway
• aorta smooth muscle tissue morphogenesis
• skin development
• collagen fibril organization
• wound healing
• supramolecular fiber organization
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| Sources:Amigo / QuickGO |
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| Orthologs |
| Species |
Human |
Mouse |
| Entrez |
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| Ensembl |
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| UniProt |
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| RefSeq (mRNA) |
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| RefSeq (protein) |
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| Location (UCSC) |
Chr 2: 188.97 – 189.01 Mb |
Chr 2: 45.31 – 45.35 Mb |
| PubMed search |
[3] |
[4] |
| Wikidata |
| View/Edit Human |
View/Edit Mouse |
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Collagen alpha-1(III) chain is a protein that in humans is encoded by the COL3A1 gene,[5][6] which is located on chromosome 2.
Contents
- 1 Function
- 2 Clinical significance
- 3 See also
- 4 Further reading
- 5 External links
- 6 References
Function
Collagen alpha-1(III) chain is a precursor to collagen III,[7] a protein that is found in extensible connective tissues such as skin, lung, and the vascular system, frequently in association with type I collagen. Although alternate transcripts have been detected for this gene, they are the result of mutations; these mutations alter splicing, often leading to the exclusion of multiple exons.[8]
Type-III collagen is a fibrous scleroprotein in bone, cartilage, dentin, tendon, bone marrow stroma and other connective tissue; it yields gelatin on boiling.
Scleroprotein is a simple protein found in horny and cartilaginous tissues and in the lens of the eye.
Clinical significance
Mutations in this gene are associated with type III and IV Ehlers-Danlos syndrome and with aortic and arterial aneurysms.
See also
- Collagen
- Reticular fiber
- Ehlers-Danlos syndrome
Further reading
- Kuivaniemi H, Tromp G, Prockop DJ (1991). "Genetic causes of aortic aneurysms. Unlearning at least part of what the textbooks say". J. Clin. Invest. 88 (5): 1441–4. doi:10.1172/JCI115452. PMC 295644 . PMID 1939638.
- Kuivaniemi H, Tromp G, Prockop DJ (1997). "Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels". Hum. Mutat. 9 (4): 300–15. doi:10.1002/(SICI)1098-1004(1997)9:4<300::AID-HUMU2>3.0.CO;2-9. PMID 9101290.
External links
- GeneReview/NCBI/NIH/UW entry on Ehlers-Danlos Syndrome Type IV
- Collagen type III at the US National Library of Medicine Medical Subject Headings (MeSH)
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Connective tissue
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| Physiology |
- Soft tissue
- Fibrosis
- Scarring
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| Composition |
| Cells |
| Resident |
- Fibroblast
- Fibrocyte
- Reticular cell
- Tendon cell
- Adipocyte
- Melanocyte
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| Wandering cells |
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Extracellular
matrix |
| Ground substance |
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| Fibers |
- Collagen fibers
- Reticular fibers
- Elastic fibers
- Elastin
- Fibrillin
- FBN1
- EMILIN1
- Elaunin
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| Classification |
| Proper |
| Loose |
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| Dense |
- Dense irregular connective tissue
- Dense regular connective tissue
- Ligament
- Tendon
- Aponeurosis
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| Embryonic |
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| Specialized |
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Protein: scleroproteins
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| Extracellular matrix |
| Collagen |
| Fibril forming |
- type I
- type II (COL2A1)
- type III
- type V
- COL24A1
- COL26A1
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| Other |
- FACIT: type IX
- type XII (COL12A1)
- COL14A1
- COL16A1
- COL19A1
- COL20A1
- COL21A1
- COL22A1
- basement membrane: type IV
- COL4A1
- COL4A2
- COL4A3
- COL4A4
- COL4A5
- COL4A6
- multiplexin: COL15A1
- type XVIII
- transmembrane: COL13A1
- COL17A1
- COL23A1
- COL25A1
- other: type VI
- COL6A1
- COL6A2
- COL6A3
- COL6A5
- type VII (COL7A1)
- type VIII
- type X (COL10A1)
- type XI
- COL27A1
- COL28A1
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| Enzymes |
- Prolyl hydroxylase/Lysyl hydroxylase
- Cartilage associated protein/Leprecan
- ADAMTS2
- Procollagen peptidase
- Lysyl oxidase
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| Laminin |
- alpha
- LAMA1
- LAMA2
- LAMA3
- LAMA4
- LAMA5
- beta
- gamma
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| Other |
- ALCAM
- Elastin
- Vitronectin
- FRAS1
- FREM2
- Decorin
- FAM20C
- ECM1
- Matrix gla protein
- Tectorin
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| Other |
- Keratin/Cytokeratin
- Gelatin
- Reticulin
- Cartilage oligomeric matrix protein
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References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000168542 - Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026043 - Ensembl, May 2017
- ^ "Human PubMed Reference:".
- ^ "Mouse PubMed Reference:".
- ^ Janeczko RA, Ramirez F (Oct 1989). "Nucleotide and amino acid sequences of the entire human alpha 1 (III) collagen". Nucleic Acids Res. 17 (16): 6742. doi:10.1093/nar/17.16.6742. PMC 318382 . PMID 2780304.
- ^ Superti-Furga A, Gugler E, Gitzelmann R, Steinmann B (Jun 1988). "Ehlers-Danlos syndrome type IV: a multi-exon deletion in one of the two COL3A1 alleles affecting structure, stability, and processing of type III procollagen". J Biol Chem. 263 (13): 6226–32. PMID 2834369.
- ^ Mayne, Richard; Burgeson, Robert E. Structure and Function of Collagen Types. Academic Press, Inc. ISBN 0-12-481280-5.
- ^ "Entrez Gene: COL3A1 collagen, type III, alpha 1 (Ehlers-Danlos syndrome type IV, autosomal dominant)".
UpToDate Contents
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English Journal
- Alteration of the bone tissue material properties in type 1 diabetes mellitus: A Fourier transform infrared microspectroscopy study.
- Mieczkowska A1, Mansur SA2, Irwin N3, Flatt PR3, Chappard D4, Mabilleau G5.
- Bone.Bone.2015 Jul;76:31-9. doi: 10.1016/j.bone.2015.03.010. Epub 2015 Mar 23.
- Type 1 diabetes mellitus (T1DM) is a severe disorder characterized by hyperglycemia and hypoinsulinemia. A higher occurrence of bone fractures has been reported in T1DM, and although bone mineral density is reduced in this disorder, it is also thought that bone quality may be altered in this chronic
- PMID 25813583
- Increased frequency of mitral valve prolapse in patients with deviated nasal septum.
- Arslan HH1, Aparci M, Arslan Z, Ozturk C, Isilak Z, Balta S, Celik T, Iyisoy A.
- European archives of oto-rhino-laryngology : official journal of the European Federation of Oto-Rhino-Laryngological Societies (EUFOS) : affiliated with the German Society for Oto-Rhino-Laryngology - Head and Neck Surgery.Eur Arch Otorhinolaryngol.2015 Jul;272(7):1667-71. doi: 10.1007/s00405-014-3243-8. Epub 2014 Aug 17.
- Any abnormality of collagen may affect the tissues with higher collagen content, e.g., joints, heart valves, and great arteries. Mitral valve prolapse (MVP) is a characteristic of generalized collagen abnormality. Nasal septum (NS) is constituted by osseous and cartilaginous septums that are highly
- PMID 25129374
- PLGA/gelatin hybrid nanofibrous scaffolds encapsulating EGF for skin regeneration.
- Norouzi M1, Shabani I2, Ahvaz HH3, Soleimani M4.
- Journal of biomedical materials research. Part A.J Biomed Mater Res A.2015 Jul;103(7):2225-35. doi: 10.1002/jbm.a.35355. Epub 2014 Nov 4.
- The novel strategies of skin regenerative treatment are aimed at the development of biologically responsive scaffolds capable of delivering multiple bioactive agents and cells to the target tissues. In this study, nanofibers of poly(lactic-co-glycolic acid) (PLGA) and gelatin were electrospun and th
- PMID 25345387
Japanese Journal
- SAHA Suppresses Peritoneal Fibrosis in Mice
- 癒着性イレウスにより口側腸管に多発小腸憩室を形成したEhlers-Danlos症候群の1例
- Th2-biased GATA-3 transgenic mice developed severe experimental peritoneal fibrosis compared with Th1-biased T-bet and Th17-biased RORγt transgenic mice
Related Links
- col·la·gen (kŏl′ə-jən) n. The fibrous protein constituent of bone, cartilage, tendon, and other connective tissue. It is converted into gelatin by boiling. ... The results show that the type III collagen binding assay can substitute for ...
- type III col·la·gen collagen characteristic of reticular fibers. ... The results show that the type III collagen binding assay can substitute for electrophoretic analysis of VWF multimer distribution as a part of the initial workup of VWD.
★リンクテーブル★
[★]
III型コラーゲン
- 関
- collagen III、type III collagen
[★]
- (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
[★]
[★]
[★]
- 関
- form、mode、pattern、type
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