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Title: Roles of CUB and LDL receptor class A domain repeats of a transmembrane serine protease matriptase in its zymogen activation.
Authors: Inouye, Kuniyo
Tomoishi, Marie
Yasumoto, Makoto
Miyake, Yuka
Kojima, Kenji  kyouindb  KAKEN_id  orcid (unconfirmed)
Tsuzuki, Satoshi  kyouindb  KAKEN_id  orcid (unconfirmed)
Fushiki, Tohru  KAKEN_id
Author's alias: 井上, 國世
Keywords: CUB repeat
hepatocyte growth factor activator inhibitor type-1
LDLRA repeat
zymogen activation
Issue Date: Jan-2013
Publisher: Oxford University Press
Journal title: Journal of biochemistry
Volume: 153
Issue: 1
Start page: 51
End page: 61
Abstract: Matriptase is a type II transmembrane serine protease containing two complement proteases C1r/C1s-urchin embryonic growth factor-bone morphogenetic protein domains (CUB repeat) and four low-density lipoprotein receptor class A domains (LDLRA repeat). The single-chain zymogen of matriptase has been found to exhibit substantial protease activity, possibly causing its own activation (i.e. conversion to a disulfide-linked two-chain fully active form), although the activation seems to be mediated predominantly by two-chain molecules. Our aim was to assess the roles of CUB and LDLRA repeats in zymogen activation. Transient expression studies of soluble truncated constructs of recombinant matriptase in COS-1 cells showed that the CUB repeat had an inhibitory effect on zymogen activation, possibly because it facilitated the interaction of two-chain molecules with a matriptase inhibitor, hepatocyte growth factor activator inhibitor type-1. By contrast, the LDLRA repeat had a promoting effect on zymogen activation. The effect of the LDLRA repeat seems to reflect its ability to increase zymogen activity. The proteolytic activities were higher in pseudozymogen forms of recombinant matriptase containing the LDLRA repeat than in a pseudozymogen without the repeat. Our findings provide new insights into the roles of these non-catalytic domains in the generation of active matriptase.
Rights: © The Authors 2012. Published by Oxford University Press on behalf of the Japanese Biochemical Society.
This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。
DOI(Published Version): 10.1093/jb/mvs118
PubMed ID: 23038671
Appears in Collections:Journal Articles

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