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Loss of Proteolytically Processed Filaggrin Caused by Epidermal Deletion of Matriptase/MT-SP1

List, Karin ; Szabo, Roman ; Wertz, Philip W. ; Segre, Julie ; Haudenschild, Christian C. ; Kim, Soo-Youl ; Bugge, Thomas H.

The Journal of cell biology, 2003-11, Vol.163 (4), p.901-910 [Periódico revisado por pares]

United States: Rockefeller University Press

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Título:
Loss of Proteolytically Processed Filaggrin Caused by Epidermal Deletion of Matriptase/MT-SP1
Autor: List, Karin ; Szabo, Roman ; Wertz, Philip W. ; Segre, Julie ; Haudenschild, Christian C. ; Kim, Soo-Youl ; Bugge, Thomas H.
Assuntos: Animals ; Antibodies ; Cell Differentiation - genetics ; Cellular biology ; Dehydration - enzymology ; Epidermis ; Epidermis - enzymology ; Epidermis - growth & development ; Epidermis - pathology ; Extracellular Matrix - genetics ; Extracellular Matrix - metabolism ; Extracellular Matrix - pathology ; filaggrin ; Ichthyosis ; Ichthyosis - enzymology ; Ichthyosis - genetics ; Ichthyosis - pathology ; Intermediate Filament Proteins - biosynthesis ; Intermediate Filament Proteins - deficiency ; Intermediate Filament Proteins - metabolism ; Keratinocytes ; Keratinocytes - enzymology ; Keratinocytes - pathology ; Keratinocytes - ultrastructure ; Lipid Metabolism ; Lipids ; Matriptase ; Membrane Proteins ; Mice ; Mice, Knockout ; Microscopy, Electron ; Monomers ; MT-SP1 protein ; Newborns ; Peptide Hydrolases - deficiency ; Peptide Hydrolases - genetics ; Permeability ; Protein Precursors - metabolism ; Proteins ; S100 Proteins - metabolism ; Serine Endopeptidases - deficiency ; Serine Endopeptidases - genetics ; Skin ; Skin Abnormalities - enzymology ; Skin Abnormalities - genetics ; Skin Abnormalities - pathology ; Skin diseases ; Trypsin - deficiency ; Trypsin - genetics
É parte de: The Journal of cell biology, 2003-11, Vol.163 (4), p.901-910
Notas: ObjectType-Article-2
SourceType-Scholarly Journals-1
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Address correspondence to Thomas H. Bugge, Proteases and Tissue Remodeling Unit, Oral and Pharyngeal Cancer Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, 30 Convent Drive, Room 211, Bethesda, MD 20892. Tel.: (301) 435-1840. Fax: (301) 402-0823. email: thomas.bugge@nih.gov
K. List and R. Szabo contributed equally to this paper.
Abbreviations used in this paper: CE, cornified envelope; E, embryonic day.
Descrição: 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.
Editor: United States: Rockefeller University Press
Idioma: Inglês

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Loss of Proteolytically Processed Filaggrin Caused by Epidermal Deletion of Matriptase/MT-SP1

List, Karin ; Szabo, Roman ; Wertz, Philip W. ; Segre, Julie ; Haudenschild, Christian C. ; Kim, Soo-Youl ; Bugge, Thomas H.

United States: Rockefeller University Press

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