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Metalloproteinase 9 is the outer executioner of desmoglein 3 in apoptotic keratinocytes
Author(s) -
Cirillo N,
Femiano F,
Gombos F,
Lanza A
Publication year - 2007
Publication title -
oral diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.953
H-Index - 87
eISSN - 1601-0825
pISSN - 1354-523X
DOI - 10.1111/j.1601-0825.2006.01287.x
Subject(s) - desmoglein 3 , matrix metalloproteinase , metalloproteinase , apoptosis , keratinocyte , extracellular matrix , western blot , chemistry , microbiology and biotechnology , cancer research , immunology , medicine , cell culture , biology , biochemistry , genetics , gene , antibody , autoimmune disease
Objective: To investigate the specific matrix metalloproteinases (MMPs) targeting desmoglein 3 (Dsg3) in apoptotic keratinocytes. Method: Inhibitor studies on cultured keratinocytes and Western blot analysis. Results: Blocking of MMP‐9 activity strongly reduces shedding of Dsg3 from cell surface. MMP‐2 has a less relevant role in the cleavage of Dsg3 while other MMPs, such as MMP‐1, ‐3, and ‐8, do not target Dsg3. Conclusion: Apoptic keratinocytes impair the extracellular domain of cell surface Dsg3 by MMP‐9 activity. The discovery of a specific targeting of Dsg3 could be useful to understand the pathophysiology of diseases in which Dsg3 is affected.