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Article

The differential amino acid requirement within osteopontin in alpha4 and alpha9 integrin-mediated cell binding and migration.

Matrix biology : journal of the International Society for Matrix Biology - 1 Jan 2009

Ito Koyu, Kon Shigeyuki, Nakayama Yosuke, Kurotaki Daisuke, Saito Yoshinari, Kanayama Masashi, Kimura Chiemi, Diao Hongyan, Morimoto Junko, Matsui Yutaka, Uede Toshimitsu

Abstract excerpt

Osteopontin (OPN) contains at least two major integrin recognition domains, Arg159-Gly-Asp161 (RGD) and Ser162-Val-Val-Tyr-Gly-Leu-Arg168 (SVVYGLR), recognized by alphavbeta3 and alpha5beta1 and alpha4 and alpha9 integrins, respectively. OPN is specifically cleaved by thrombin and matrix metalloproteinase (MMP)-3 or MMP-7 at a position of Arg168/Ser169 (R/S) and Gly166/Leu167 (G/L), respectively. We in this study...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 19000758
DOI: 10.1016/j.matbio.2008.10.002

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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