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Indexed/Abstracted in: EMBASE, Science Citation Index Expanded (SciSearch), Scopus
Impact Factor 0,246
Online ISSN 1827-160X
7th INTERNATIONAL CONFERENCE ON TRANSGLUTAMINASES AND PROTEIN CROSSLINKING REACTIONS
Ferrara (Italy), September 14-17, 2002
Ahvazi B., Boeshans K., Jang S.-I., Kalinin A. E., Steinert P. M.
Laboratory of Skin Biology, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland, USA
During their terminal differentiation programs, all stratified squamous epithelia assemble an elaborate insoluble barrier structure, generically termed the cornified cell envelope (CE), on the inside of their plasma membrane at the cell periphery. This structure provides a vital physical and/or biomechanical barrier for the mature tissue and organism. The CE is composed of several defined structural proteins that become cross-linked together by the action of one or more transglutaminase (TGase) enzymes. Recent studies on the complexity of the family of TGase enzymes and the initial draft of the human genome have revealed the presence of nine TGase-like genes. Of these, six active genes/enzymes are now known to be expressed in epithelial cells. This bewildering complexity strongly implies that the proper assembly of the CE is indeed vital for survival.