Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Differential regulation of cellular adhesion and migration by recombinant laminin-5 forms with partial deletion or mutation within the G3 domain of alpha3 chain.

Journal of cellular biochemistry - 15 Feb 2003

Kariya Yoshinobu, Tsubota Yoshiaki, Hirosaki Tomomi, Mizushima Hiroto, Puzon-McLaughlin Wilma, Takada Yoshikazu, Miyazaki Kaoru

Abstract excerpt

The basement membrane protein laminin-5 promotes cell adhesion and migration. The carboxyl-terminal G3 domain in the alpha3 chain is essential for the unique activity of laminin-5. To investigate the function of the G3 domain, we prepared various recombinant laminin-5 forms with a partially deleted or mutated G3 domain. The deletion of the carboxyl-terminal 28 amino acids (region III) markedly decreased the cell...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Adhesion
Share to Cell Line

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Movement

Share to Cell Size

Share to Integrins

Share to Laminin

Share to Protein Structure, Tertiary

Share to Recombinant Proteins

Source

Identifiers

PMID: 12532327
DOI: 10.1002/jcb.10350

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Differential regulation of cellular adhesion and migration by recombinant laminin-5 forms with partial deletion or mutation within the G3 domain of alpha3 chain.PMID 12532327Read ↗

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

Keratinocyte motility induced by TGF-beta1 is accompanied by dramatic changes in cellular interactions with laminin 5.Semantic proximity Read ↗

The requirement of the glutamic acid residue at the third position from the carboxyl termini of the laminin gamma chains in integrin binding by laminins.Semantic proximity Read ↗

Globular domains 4/5 of the laminin alpha3 chain mediate deposition of precursor laminin 5.Semantic proximity Read ↗

Keratinocyte migration requires alpha2beta1 integrin-mediated interaction with the laminin 5 gamma2 chain.Semantic proximity Read ↗

Functional Re-expression of laminin-5 in laminin-gamma2-deficient human keratinocytes modifies cell morphology, motility, and adhesion.Semantic proximity Read ↗

The αvβ3 Integrin Regulates α5β1-mediated Cell Migration toward FibronectinSemantic proximity Read ↗

A peptide derived from laminin-γ3 reversibly impairs spermatogenesis in rats.Semantic proximity Read ↗

N-Acetylglucosaminyltransferase III Antagonizes the Effect of N-Acetylglucosaminyltransferase V on α3β1 Integrin-mediated Cell MigrationSemantic proximity Read ↗

An N-glycosylation site on the beta-propeller domain of the integrin alpha5 subunit plays key roles in both its function and site-specific modification by beta1,4-N-acetylglucosaminyltransferase III.Semantic proximity Read ↗

Integrin engagement differentially modulates epithelial cell motility by RhoA/ROCK and PAK1.Semantic proximity Read ↗

Functional role of the cytoplasmic domain of the integrin alpha 5 subunit.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.