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Title: The PPFLMLLKGSTR motif in globular domain 3 of the human laminin-5 {alpha}3 chain is crucial for integrin {alpha}3{beta}1 binding and cell adhesion

Abstract

Laminin-5 regulates various cellular functions, including cell adhesion, spreading, and motility. Here, we expressed the five human laminin {alpha}3 chain globular (LG) domains as monomeric, soluble fusion proteins, and examined their biological functions and signaling. Recombinant LG3 (rLG3) protein, unlike rLG1, rLG2, rLG4, and rLG5, played roles in cell adhesion, spreading, and integrin {alpha}3{beta}1 binding. More significantly, we identified a novel motif (PPFLMLLKGSTR) in the LG3 domain that is crucial for these responses. Studies with the synthetic peptides delineated the PPFLMLLKGSTR peptide within LG3 domain as a major site for both integrin {alpha}3{beta}1 binding and cell adhesion. Substitution mutation experiments suggest that the Arg residue is important for these activities. rLG3 protein- and PPFLMLLKGSTR peptide-induced keratinocyte adhesion triggered cell signaling through FAK phosphorylation at tyrosine-397 and -577. To our knowledge, this is the first report demonstrating that the PPFLMLLKGSTR peptide within the LG3 domain is a novel motif that is capable of supporting integrin {alpha}3{beta}1-dependent cell adhesion and spreading.

Authors:
 [1];  [2];  [1]
  1. Department of Oral Biochemistry and Craniomaxillofacial Reconstructive Sciences, Dental Research Institute, IBEC, and BK21 HLS, Seoul National University College of Dentistry, 28 Yeonkun-Dong, Chongno-Ku, Seoul 110-749 (Korea, Republic of)
  2. Department of Textile Engineering, Chungnam National University, Daejeon 305-764 (Korea, Republic of)
Publication Date:
OSTI Identifier:
20717560
Resource Type:
Journal Article
Journal Name:
Experimental Cell Research
Additional Journal Information:
Journal Volume: 304; Journal Issue: 1; Other Information: DOI: 10.1016/j.yexcr.2004.11.009; PII: S0014-4827(04)00689-5; Copyright (c) 2004 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0014-4827
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ADHESION; ALBUMINS; BIOLOGICAL FUNCTIONS; CATTLE; ELECTROPHORESIS; GELS; GROWTH; MONOCLONAL ANTIBODIES; PEPTIDES; PHOSPHATES; PHOSPHORYLATION; TYROSINE

Citation Formats

Kim, Jin-Man, Park, Won Ho, and Min, Byung-Moo. The PPFLMLLKGSTR motif in globular domain 3 of the human laminin-5 {alpha}3 chain is crucial for integrin {alpha}3{beta}1 binding and cell adhesion. United States: N. p., 2005. Web. doi:10.1016/j.yexcr.2004.11.009.
Kim, Jin-Man, Park, Won Ho, & Min, Byung-Moo. The PPFLMLLKGSTR motif in globular domain 3 of the human laminin-5 {alpha}3 chain is crucial for integrin {alpha}3{beta}1 binding and cell adhesion. United States. https://doi.org/10.1016/j.yexcr.2004.11.009
Kim, Jin-Man, Park, Won Ho, and Min, Byung-Moo. 2005. "The PPFLMLLKGSTR motif in globular domain 3 of the human laminin-5 {alpha}3 chain is crucial for integrin {alpha}3{beta}1 binding and cell adhesion". United States. https://doi.org/10.1016/j.yexcr.2004.11.009.
@article{osti_20717560,
title = {The PPFLMLLKGSTR motif in globular domain 3 of the human laminin-5 {alpha}3 chain is crucial for integrin {alpha}3{beta}1 binding and cell adhesion},
author = {Kim, Jin-Man and Park, Won Ho and Min, Byung-Moo},
abstractNote = {Laminin-5 regulates various cellular functions, including cell adhesion, spreading, and motility. Here, we expressed the five human laminin {alpha}3 chain globular (LG) domains as monomeric, soluble fusion proteins, and examined their biological functions and signaling. Recombinant LG3 (rLG3) protein, unlike rLG1, rLG2, rLG4, and rLG5, played roles in cell adhesion, spreading, and integrin {alpha}3{beta}1 binding. More significantly, we identified a novel motif (PPFLMLLKGSTR) in the LG3 domain that is crucial for these responses. Studies with the synthetic peptides delineated the PPFLMLLKGSTR peptide within LG3 domain as a major site for both integrin {alpha}3{beta}1 binding and cell adhesion. Substitution mutation experiments suggest that the Arg residue is important for these activities. rLG3 protein- and PPFLMLLKGSTR peptide-induced keratinocyte adhesion triggered cell signaling through FAK phosphorylation at tyrosine-397 and -577. To our knowledge, this is the first report demonstrating that the PPFLMLLKGSTR peptide within the LG3 domain is a novel motif that is capable of supporting integrin {alpha}3{beta}1-dependent cell adhesion and spreading.},
doi = {10.1016/j.yexcr.2004.11.009},
url = {https://www.osti.gov/biblio/20717560}, journal = {Experimental Cell Research},
issn = {0014-4827},
number = 1,
volume = 304,
place = {United States},
year = {Thu Mar 10 00:00:00 EST 2005},
month = {Thu Mar 10 00:00:00 EST 2005}
}