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Spatial and Temporal Similarities between Laminin‐332 and Keratin‐5 during Wound Repair
Author(s) -
Gerecke Donald R,
Gordon Marion K,
Svoboda Kathy,
Lu ShouEn,
Chang Yokechen
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.582.2
Subject(s) - laminin , keratin , western blot , keratinocyte , messenger rna , basement membrane , wound healing , microbiology and biotechnology , epidermis (zoology) , chemistry , basal (medicine) , glycoprotein , biology , pathology , immunology , cell , anatomy , biochemistry , in vitro , endocrinology , medicine , gene , insulin
A mouse ear skin vesicant model was wounded using sulfur mustard and the skin glycoprotein, laminin‐332 examined in a time‐course study. Mouse skin biopsies 6, 12, 24, 72, and 168h after SM exposure demonstrated a direct correlation in skin damage over time. Chain‐specific antibodies showed overlap of laminin‐332 and the basal keratinocyte marker, keratin‐5 in the basal cells of the epidermis and the lining of the sebaceous glands. The mRNA levels of the laminin‐332 chains declined early (within 24h), then increased to a maximum level by 72h post‐treatment. The laminin‐á3 and laminin‐â3 mRNAs returned to normal levels by 168h post‐treatment, however, the laminin‐ã2 chain mRNA levels remained about 10 fold higher than the other two chains at later timepoints (72 and 168h). The higher laminin‐ã2 mRNA level corresponded to increased amount of expressed protein (Western blot analysis). Processed forms of several different sizes for the laminin‐ã2 chain protein also increased over time. This was especially true 72h post‐exposure, when keratinocytes were undergoing hyperproliferation. Confocal microscopy demonstrated an overlap in distribution between keratin‐5 and laminin‐ã2 in the 72h samples and we speculate that the laminin‐ã2 functions to enhance epithelial cell migration.