関: procollagen N-endopeptidase、procollagen N-proteinase

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/02/19 07:29:13」(JST)

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Procollagen peptidase is an endopeptidase involved in the processing of collagen. The proteases removes the terminal peptides of the procollagen. Deficiency of these enzymes leads to dermatosparaxis or ehlers Danlos syndrome.^[1]

The enzyme is present in the skin of rats and humans.^[2]

External links

The MEROPS online database for peptidases and their inhibitors: Procollagen C-Peptidase:M12.005, Procollagen N-Peptidase:M12.301

References

^ http://www.biology-online.org/dictionary/Procollagen_peptidase
^ Lapière, C. M.; Lenaers, A.; Kohn, L. D. (1971). "Procollagen Peptidase: An Enzyme Excising the Coordination Peptides of Procollagen". Proceedings of the National Academy of Sciences of the United States of America 68 (12): 3054–3058. doi:10.1073/pnas.68.12.3054. PMC 389589. PMID 5289249. //www.ncbi.nlm.nih.gov/pmc/articles/PMC389589/. edit

Procollagen+peptidase at the US National Library of Medicine Medical Subject Headings (MeSH)

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2. エーラス・ダンロス症候群の臨床症状および診断 clinical manifestations and diagnosis of ehlers danlos syndromes
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English Journal

A disintegrin and metalloproteinase with thrombospondin motifs 4 (ADAMTS-4) cleaves Reelin in an isoform-dependent manner.

Hisanaga A, Morishita S, Suzuki K, Sasaki K, Koie M, Kohno T, Hattori M.SourceDepartment of Biomedical Science, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan.
FEBS letters.FEBS Lett.2012 Sep 21;586(19):3349-53. doi: 10.1016/j.febslet.2012.07.017. Epub 2012 Jul 20.
Reelin is a glycoprotein essential for brain development and functions. Reelin is subject to specific proteolysis at two distinct (N-t and C-t) sites, and these cleavages significantly diminish Reelin activity. The decrease of Reelin activity is detrimental for brain function, but the protease that
PMID 22819337

MMP proteolysis of the human extracellular matrix protein aggrecan is mainly a process of normal turnover.

Struglics A, Hansson M.SourceDepartment of Orthopaedics, Clinical Sciences Lund, Lund University, Lund, Sweden. andre.struglics@med.lu.se
The Biochemical journal.Biochem J.2012 Sep 1;446(2):213-23. doi: 10.1042/BJ20120274.
Although it has been shown that aggrecanases are involved in aggrecan degradation, the role of MMP (matrix metalloproteinase) aggrecanolysis is less well studied. To investigate MMP proteolysis of human aggrecan, in the present study we used neoepitope antibodies against MMP cleavage sites and Weste
PMID 22670872

Effects of cleavage by a disintegrin and metalloproteinase with thrombospondin motifs-4 on gene expression and protein content of versican and aggrecan in the digital laminae of horses with starch gruel-induced laminitis.

Wang L, Pawlak E, Johnson PJ, Belknap JK, Alfandari D, Black SJ.SourceDepartment of Veterinary and Animal Sciences, College of Natural Sciences, University of Massachusetts, Amherst, MA 01003, USA.
American journal of veterinary research.Am J Vet Res.2012 Jul;73(7):1047-56. doi: 10.2460/ajvr.73.7.1047.
OBJECTIVE: To determine whether increased gene expression of a disintegrin and metalloproteinase with thrombospondin motifs-4 (ADAMTS-4) in laminae of horses with starch gruel-induced laminitis was accompanied by increased enzyme activity and substrate degradation.SAMPLE: Laminae from the forelimb h
PMID 22738057

Japanese Journal

Pro-gln: the procollagen peptidase cleavage site in the alpha 1 (I) chain of dermatosparatic calf skin procollagen.

HORLEIN D.
FEBS Lett 89, 279-282, 1978
NAID 80014998742

「コラーゲン」

procollagen (type III) N-endopeptidase
Identifiers
Symbol	PCOLN3
Alt. symbols	PRSM1
Entrez	5119
HUGO	8740
OMIM	164010
RefSeq	NM_002768
UniProt	Q9HD42
Other data
EC number	3.4.24.14
Locus	Chr. 16 q24.3

　　[★]

英: collagen
同: 膠原
関

first aid step1 2006 p.85,86,114,288,291,292,301,306,319,321,385,427

遺伝子

COL1A1 17q22
COL1A2 7q22.1
COL2A1 12q13
COL11A2 6p21.3

これらの遺伝子の変異による結合組織疾患はdominant negative mutationである。

臨床関連

骨形成不全

コラーゲンの種類

HIS.97 NDE.5

	場所
I型コラーゲン	狭義の結合組織、骨、歯の象牙質とセメント質に存在
II型コラーゲン	硝子軟骨、弾性軟骨
III型コラーゲン	細網線維
IV型コラーゲン	基底板の緻密板を作る
V型コラーゲン	I型コラーゲンと関連。胎盤に存在
VII型コラーゲン	基底板を細網線維に付着。anchoring fibril
XVII型コラーゲン	ヘミデスモソームと基底板を連結

生合成

first aid step1 2006 p.85
ER：ER内でOH化(Pro, Lys)：preprocollagen
Golgi：Lysの糖鎖付加：procollagen(triple helix of 3 collagen α chains)
EM：procollagen　－procollagen peptidase→　tropocollagen
：tropocollagen　－covalent lysine-hydroxylysine cross-linkage by lysyl oxidase　→　collagen fibrils