Evaluation of the Role of Laminin 5 in Sulfur Mustard Vesication and Re-epithelialization.
Abstract
We have studied effects CEES of alkylation upon the ability of purified laminin 5 to bind keratinocytes, and to bind type VII collagen NCl domain in vitro. Alkylation of laminin 5 eliminates keratinocyte binding both when laminin 5 is treated with CEES as a solid growth substrate, and when laminin 5 is first alkylated in solution and then bound to the plastic growth surface. Alkylated laminin 5 retains its ability to bind to the type VII collagen NCl domain. Alkylation of NCl altered its solubility, and its binding to laminin 5 could not be evaluated. Purified, untreated laminin 5 promoted the adhesion rate of keratinocyte sheet grafts to wounds in nude mice. Antibodies to laminin 5 that interfere with epithelial cell binding in vitro slowed the closure of wounds made in human skin grafted to nude mice. However, the addition of exogenous laminin 5 did not significantly increase the rate of closure of wounds made to wounds in the same system. Blisters made using CEES treatment in this system resulted in wounds too irregular to allow testing of possible effects of laminin 5 treatment upon closure of the wound.
Document Details
- Document Type
- Technical Report
- Publication Date
- Oct 01, 1998
- Accession Number
- ADA377989
Entities
People
- Robert E. Burgeson
Organizations
- Massachusetts General Hospital