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Article

Regulation of biological activity and matrix assembly of laminin-5 by COOH-terminal, LG4-5 domain of alpha3 chain.

The Journal of biological chemistry - 15 Apr 2005

Tsubota Yoshiaki, Yasuda Chie, Kariya Yoshinobu, Ogawa Takashi, Hirosaki Tomomi, Mizushima Hiroto, Miyazaki Kaoru

Abstract excerpt

The basement membrane protein laminin-5 (LN5; alpha3beta3gamma2) undergoes specific proteolytic processing of the 190-kDa alpha3 chain to the 160-kDa form after the secretion, releasing its COOH-terminal, LG4-5 domain. To clarify the biological significance of this processing, we tried to express a recombinant precursor LN5 with a 190-kDa alpha3 chain (pre-LN5), in which the cleavage sequence Gln-Asp was changed...

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PMID: 15695818
DOI: 10.1074/jbc.M413051200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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