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the 13th letter of the Roman alphabet (同)m

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Mach number / mark[s] / Monsieur

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/12/17 05:33:01」(JST)

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Collagenase 3 is an enzyme that in humans is encoded by the MMP13 gene.^[1]^[2] It is a member of the matrix metalloproteinase (MMP) family. Like most MMPs, it is secreted as an inactive pro-form. It is activated once the pro-domain is cleaved, leaving an active enzyme composed of the catalytic domain and the hemopexin-like domain PDB 1PEX. Although the actual mechanism has not been described, the hemopexin domain participates in collagen degradation, the catalytic domain alone being particularly inefficient in collagen degradation. During embryonic development, MMP13 is expressed in the skeleton as required for restructuring the collagen matrix for bone mineralization. In pathological situations it is highly overexpressed; this occurs in human carcinomas, rheumatoid arthritis and osteoarthritis.^[3]

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The protein encoded by this gene cleaves type II collagen more efficiently than types I and III. It may be involved in articular cartilage turnover and cartilage pathophysiology associated with osteoarthritis. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.^[2]

References[edit]

^ Freije JM, Diez-Itza I, Balbin M, Sanchez LM, Blasco R, Tolivia J, Lopez-Otin C (Jul 1994). "Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas". J Biol Chem 269 (24): 16766–73. PMID 8207000. Cite uses deprecated parameters (help)
^ ^a ^b "Entrez Gene: MMP13 matrix metallopeptidase 13 (collagenase 3)".
^ Johansson N, Ahonen M, Kähäri VM. (2000). "Matrix metalloproteinases in tumor invasion.". Cell Mol Life Sci. 57 (1): 5–15. PMID 10949577.

External links[edit]

The MEROPS online database for peptidases and their inhibitors: M10.013

This article on a gene on chromosome 11 is a stub. You can help Wikipedia by expanding it.

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1. 関節リウマチの病因 pathogenesis of rheumatoid arthritis
2. 変形性関節症の病因 pathogenesis of osteoarthritis
3. 頭頸部の扁平上皮癌化：分子学的および遺伝学的変化 head and neck squamous cell carcinogenesis molecular and genetic alterations
4. リウマチ性疾患におけるサイトカインの役割 role of cytokines in rheumatic diseases
5. 骨の巨大細胞腫瘍 giant cell tumor of bone

English Journal

Disruption of Sirt1 in chondrocytes causes accelerated progression of osteoarthritis under mechanical stress and during ageing in mice.

Matsuzaki T, Matsushita T, Takayama K, Matsumoto T, Nishida K, Kuroda R, Kurosaka M.
Annals of the rheumatic diseases.Ann Rheum Dis.2014 Jul;73(7):1397-404. doi: 10.1136/annrheumdis-2012-202620. Epub 2013 May 30.
OBJECTIVES: Important roles for SIRT1 are implicated in ageing and age-related diseases. The role of SIRT1 in osteoarthritis (OA), however, remains partially unknown. To investigate the role of SIRT1 in chondrocytes in vivo, cartilage-specific Sirt1-conditional knockout (CKO) mice were analysed usin
PMID 23723318

Chondroprotective and anti-inflammatory effects of S-methylisothiourea, an inducible nitric oxide synthase inhibitor in cartilage and synovial explants model of osteoarthritis.

Balaganur V1, Pathak NN, Lingaraju MC, More AS, Latief N, Kumari RR, Kumar D, Tandan SK.
The Journal of pharmacy and pharmacology.J Pharm Pharmacol.2014 Jul;66(7):1021-31. doi: 10.1111/jphp.12228. Epub 2014 Feb 20.
OBJECTIVES: To study the chondroprotective and anti-inflammatory potential of inducible nitric oxide synthase (iNOS) inhibitor S-methylisothiourea (SMT) in in-vitro model.METHODS: Rabbit cartilage explants were stimulated with recombinant human interleukin 1β (rhIL-1β), and the chondroprotective a
PMID 24697299

Protection of ginsenoside Rg1 on chondrocyte from IL-1β-induced mitochondria-activated apoptosis through PI3K/Akt signaling.

Huang Y1, Wu D, Fan W.
Molecular and cellular biochemistry.Mol Cell Biochem.2014 Jul;392(1-2):249-57. doi: 10.1007/s11010-014-2035-1. Epub 2014 Mar 27.
Chondrocyte apoptosis is closely related to the development and progression of osteoarthritis. Ginsenoside Rg1 protects cells by antagonizing apoptosis. This study aimed to investigate the protective effect of Rg1 on interleukin 1β (IL-1β)-induced chondrocyte apoptosis and the underlying molecular
PMID 24671491

Japanese Journal

P8-003　　ブレオマイシン誘発強皮症モデルマウスの線維化，血管障害および免疫異常の病態における転写因子IRF5の役割についての検討

三枝良輔,浅野善英,谷口隆志,市村洋平,高橋岳浩,遠山哲夫,吉崎歩,佐藤伸一
日本臨床免疫学会会誌 37(4), 367a-367a, 2014
… （線維化，血管障害，炎症・免疫異常）におけるIRF5の役割について検討した．Irf5−/−マウスの無刺激状態の皮膚では，野生型マウスに比べ細いcollagen線維束が目立ち，type I collagenの発現低下およびMMP-13の発現亢進がみられた．さらに，lumican, lysyl oxidase, ADAMTS2といったfibrillogenesisに関与する分子の発現低下がみられた．また，BLM投与による皮膚硬化および肺線維化がIrf5−/−マウスで抑制されていた …
NAID 130004694301

Type II collagen peptide stimulates Akt leading to nuclear factor-κB activation: Its inhibition by hyaluronan

Biomedical Research 35(3), 193-199, 2014
… While nuclear factor (NF)-κB is a critical pathway for matrix metalloproteinase (MMP)-13 inductionin chondrocytes, intracellular upstream events for NF-κB activation by the type II collagenpeptide (CB12-II) with catabolic activities remain unclear. … In monolayer cultures, pretreatmentwith HA of 2700 kDa significantly inhibited MMP-13 production by CB12-II-stimulatedchondrocytes. …
NAID 130004470867

CCN Family Member 2/Connective Tissue Growth Factor (CCN2/CTGF) Has Anti-Aging Effects That Protect Articular Cartilage from Age-Related Degenerative Changes

Itoh Shinsuke,Hattori Takako,Tomita Nao,Aoyama Eriko,Yutani Yasutaka,Yamashiro Takashi,Takigawa Masaharu
PLoS ONE 8(8), 2013-08-12
… Transgenic articular cartilage showed enhanced toluidine blue and safranin-O staining as well as chondrocyte proliferation but reduced staining for type X and I collagen and MMP-13 as compared with those parameters for WT cartilage. … CTS applied to primary cultures of mock-transfected rib chondrocytes from WT cartilage and WT epiphyseal cartilage induced expression of Col1a1, ColXa1, Mmp-13, and Mmp-9 mRNAs; …
NAID 120005345531

「matrix metalloproteinase 13」

Matrix metallopeptidase 13 (collagenase 3)
	; PDB rendering based on 1cxv.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1EUB, 1FLS, 1FM1, 1PEX, 1XUC, 1XUD, 1XUR, 1YOU, 1ZTQ, 2D1N, 2E2D, 2OW9, 2OZR, 2PJT, 2YIG, 3ELM, 3I7G, 3I7I, 3KEC, 3KEJ, 3KEK, 3KRY, 3LJZ, 3O2X, 3TVC, 3ZXH, 456C, 4A7B, 4FU4, 4FVL, 4G0D, 830C
Identifiers
Symbols	MMP13; CLG3; MANDP1
External IDs	OMIM: 600108 MGI: 1340026 HomoloGene: 20548 ChEMBL: 280 GeneCards: MMP13 Gene
EC number	3.4.24.-
Gene Ontology
Molecular function	• metalloendopeptidase activity; • calcium ion binding; • zinc ion binding;
Cellular component	• extracellular region; • proteinaceous extracellular matrix; • extracellular space;
Biological process	• proteolysis; • extracellular matrix disassembly; • extracellular matrix organization; • bone mineralization; • collagen catabolic process; • cellular protein metabolic process; • cartilage development;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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