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Article

Proteolytic processing of the laminin alpha3 G domain mediates assembly of hemidesmosomes but has no role on keratinocyte migration.

The Journal of investigative dermatology - 1 Nov 2005

Baudoin Christian, Fantin Laurence, Meneguzzi Guerrino

Abstract excerpt

Laminin-5 (Lm5), the major adhesion ligand of basal epithelial cells, undergoes complex extracellular proteolytic processing that influences cell adhesion and migration. In tumor cell lines, the proteolytic truncation of the C-terminal G domain of the Lm alpha3 chain induces assembly of hemidesmosomes and downregulates cell migration. To define the biological functions of the alpha3 G domain processing in...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 16297184
DOI: 10.1111/j.0022-202X.2005.23881.x

Provenance

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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