WordNet

the chief phagocytic leukocyte; stains with either basic or acid dyes (同)neutrophile
any enzyme that catalyzes the hydrolysis of collagen and gelatin

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2012/06/24 12:12:01」(JST)

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Collagenases are enzymes that break the peptide bonds in collagen.

They assist in destroying extracellular structures in pathogenesis of bacteria such as Clostridium. They are an exotoxin (a virulence factor) and help to facilitate the spread of gas gangrene. They normally target the connective tissue in muscle cells and other body organs.^[1]

Collagen, a key component of the animal extracellular matrix, is made through cleavage of pro-collagen by collagenase once it has been secreted from the cell. This stops large structures from forming inside the cell itself.

Collagenase production can be induced during an immune response, by cytokines that stimulate cells such as fibroblasts and osteoblasts, and cause indirect tissue damage.^{[citation needed]}

Therapeutic uses

Collagenases have been approved for medical uses for

treatment of Dupuytren's contracture (Xiaflex).

Collagenases and Peyronie's disease

Collagenase remains an investigational drug for the treatment of Peyronie's disease. ^[2] It has presented a documented efficiency in reducing the size of plaques or in some cases eliminating them.^[3]

References

^ Gerard J. Tortora, Berdell R. Funke, Cristine L. Case (2007). Microbiology: an introduction. Pearson Benjamin Cummings. ISBN 0-321-39603-0.
^ http://www.peyronies.org/pages/treatment.htm
^ http://www.andrologyjournal.org/cgi/content/full/30/4/397

External links

Collagenases at the US National Library of Medicine Medical Subject Headings (MeSH)

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UpToDate Contents

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1. 運動以外の好中球機能 neutrophil functions other than movement
2. 好中球二次顆粒欠損症 neutrophil specific granule deficiency
3. 変形性関節症の病因 pathogenesis of osteoarthritis
4. 関節リウマチの病因 pathogenesis of rheumatoid arthritis
5. 慢性関節リウマチにおける滑膜異常 synovial pathology in rheumatoid arthritis

English Journal

Fetal, amniotic and maternal inflammatory responses in early stage of ascending intrauterine infection, inflammation restricted to chorio-decidua, in preterm gestation.

Park CW, Kim SM, Park JS, Jun JK, Yoon BH.SourceDepartment of Obstetrics and Gynecology, Seoul National University College of Medicine , Seoul , Korea.
The journal of maternal-fetal & neonatal medicine : the official journal of the European Association of Perinatal Medicine, the Federation of Asia and Oceania Perinatal Societies, the International Society of Perinatal Obstetricians.J Matern Fetal Neonatal Med.2014 Jan;27(1):98-105. doi: 10.3109/14767058.2013.806898. Epub 2013 Jul 11.
Abstract Objective: No data exist on the frequency and intensity of the fetal, intraamniotic and maternal inflammation in preterm-gestations with inflammation restricted to chorio-decidua, early stage of ascending intrauterine infection. The objective of the study is to examine this issue. Study Des
PMID 23691922

Opuntia humifusa Ameliorated Cerulein-Induced Acute Pancreatitis.

Choi SB, Bae GS, Park KC, Jo IJ, Seo SH, Song K, Lee DS, Oh H, Kim YC, Kim JJ, Shin YK, Park JH, Seo MJ, Song HJ, Park SJ.SourceFrom the *Department of Herbology, School of Oriental Medicine, †BK21 plus team, Professional graduate school of Oriental medicine, ‡Hanbang Body-fluid Research Center, §College of Pharmacy, and Institute of Pharmaceutical Research and Development, and ∥College of Pharmacy, Wonkwang University, Iksan, Jeonbuk; ¶ChungBuk Technopark Bio Center, Jecheon, #Foundation of industry-academy cooperation, Semyung University, ChungBuk; and **Department of Medicinal Herb, Gyeongju University, Gyeongbuk, South Korea.
Pancreas.Pancreas.2014 Jan;43(1):118-27. doi: 10.1097/MPA.0b013e318296f903.
OBJECTIVE: The aim of this study was to evaluate the effects of Opuntia humifusa (OH) on cerulein-induced acute pancreatitis (AP).METHODS: Acute pancreatitis was induced via intraperitoneal injection of cholecystokinin analog cerulein (50 μg/kg). In the OH pretreatment group, OH was administered in
PMID 24326366

The Pore-Forming Toxin Listeriolysin O Is Degraded by Neutrophil Metalloproteinase-8 and Fails To Mediate Listeria monocytogenes Intracellular Survival in Neutrophils.

Arnett E, Vadia S, Nackerman CC, Oghumu S, Satoskar AR, McLeish KR, Uriarte SM, Seveau S.SourceDepartment of Microbiology, The Ohio State University, Columbus, OH 43210;
Journal of immunology (Baltimore, Md. : 1950).J Immunol.2013 Dec 6. [Epub ahead of print]
The pore-forming toxin listeriolysin O (LLO) is a major virulence factor secreted by the facultative intracellular pathogen Listeria monocytogenes. This toxin facilitates L. monocytogenes intracellular survival in macrophages and diverse nonphagocytic cells by disrupting the internalization vesicle,
PMID 24319266

Japanese Journal

好中球コラゲナーゼ(MMP-8) : 基質特異性決定に重要な部位の検討

菊地健,HASTY KAREN A.,広瀬友彦 [他]
順天堂医学 57(5), 504-511, 2011
NAID 40019059665

骨と軟骨の発生過程におけるMMP8(Neutrophil collagenase)とMMP13(Interstitial collagenase)の遺伝子発現

笹野泰之,朱景旭,坪田真,高橋一郎,小野寺和之,溝口到,加賀山学
歯科基礎医学会雑誌 43(5), 557, 2001-08-20
NAID 110003164199

Related Pictures

★リンクテーブル★

リンク元	「matrix metalloproteinase 8」「好中球コラゲナーゼ」「fibroblast collagenase」

「matrix metalloproteinase 8」

matrix metallopeptidase 8 (neutrophil collagenase)
Identifiers
Symbol	MMP8
Entrez	4317
HUGO	7175
OMIM	120355
RefSeq	NM_002424
UniProt	P22894
Other data
EC number	3.4.24.34
Locus	Chr. 11 q21-q22

matrix metallopeptidase 1 (interstitial collagenase)
Identifiers
Symbol	MMP1
Entrez	4312
HUGO	7155
OMIM	120353
RefSeq	NM_002421
UniProt	P03956
Other data
EC number	3.4.24.7
Locus	Chr. 11 q21-q22