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Upregulation of gamma‐2 laminin‐332 in the mouse ear vesicant wound model
Author(s) -
Chang YokeChen,
Sabourin Carol L. K.,
Lu ShouEn,
Sasaki Takako,
Svoboda Kathy K. H.,
Gordon Marion K.,
Riley David J.,
Casillas Robert P.,
Gerecke Donald R.
Publication year - 2009
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.20275
Subject(s) - laminin , wound healing , basement membrane , western blot , downregulation and upregulation , extracellular matrix , chemistry , microbiology and biotechnology , pathology , immunology , biology , biochemistry , medicine , gene
Epithelial cell migration during wound healing is regulated in part by enzymatic processing of laminin‐332 (formerly LN‐5), a heterodimer formed from α, β, and γ polypeptide chains. Under static conditions, laminin‐332 is secreted into the extracellular matrix as a proform and has two chains processed to smaller forms, allowing it to anchor epithelial cells to the basement membrane of the dermis. During incisional wounding, laminin γ2 chains in particular are processed to smaller sizes and function to promote epithelial sheet migration over the wound bed. The present study examines whether this same function occurs following chemical injury. The mouse ear vesicant model (MEVM) was used to follow the pathology in the ear and test whether processed laminin‐332 enhances epithelial cell migration. Skin biopsies of sulfur mustard (SM) exposed ears for several time points were analyzed by histology, immunohistochemistry, real‐time PCR, and Western blot analysis. SM exposure greatly increased mRNA levels for laminin‐γ2 in comparison to the other two chains. Protein production of laminin‐γ2 was upregulated, and there was an increase in the processed forms. Protein production was in excess of the amount required to form heterotrimeric laminin‐332 and was associated with the migrating epithelial sheet, suggesting a potential role in wound healing for monomeric laminin‐γ2. © 2009 Wiley Periodicals, Inc. J Biochem Mol Toxicol 23:172–184, 2009; Published online in Wiley InterScience ( www.interscience.wiley.com ). DOI 10.1002/jbt.20275