Loss of proteolytically processed filaggrin caused by epidermal deletion of Matriptase/MT-SP1.
J Cell Biol
; 163(4): 901-10, 2003 Nov 24.
Article
em En
| MEDLINE
| ID: mdl-14638864
ABSTRACT
Profilaggrin is a large epidermal polyprotein that is proteolytically processed during keratinocyte differentiation to release multiple filaggrin monomer units as well as a calcium-binding regulatory NH2-terminal filaggrin S-100 protein. We show that epidermal deficiency of the transmembrane serine protease Matriptase/MT-SP1 perturbs lipid matrix formation, cornified envelope morphogenesis, and stratum corneum desquamation. Surprisingly, proteomic analysis of Matriptase/MT-SP1-deficient epidermis revealed the selective loss of both proteolytically processed filaggrin monomer units and the NH2-terminal filaggrin S-100 regulatory protein. This was associated with a profound accumulation of profilaggrin and aberrant profilaggrin-processing products in the stratum corneum. The data identify keratinocyte Matriptase/MT-SP1 as an essential component of the profilaggrin-processing pathway and a key regulator of terminal epidermal differentiation.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Serina Endopeptidases
/
Tripsina
/
Queratinócitos
/
Epiderme
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Proteínas de Filamentos Intermediários
Limite:
Animals
Idioma:
En
Ano de publicação:
2003
Tipo de documento:
Article