Titre du document / Document title

Membrane anchored serine proteases: A rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer

Auteur(s) / Author(s)

NETZEL-ARNETT Sarah ⁽¹⁾ ; HOOPER John D. ⁽²⁾ ; SZABO Roman ⁽³⁾ ; MADISON Edwin L. ⁽⁴⁾ ; QUIGLEY James P. ⁽²⁾ ; BUGGE Thomas H. ⁽³⁾ ; ANTALIS Toni M. ;

Affiliation(s) du ou des auteurs / Author(s) Affiliation(s)

⁽¹⁾ Vascular Biology Department, Jerome H. Holland Laboratory for the Biological Sciences, American Red Cross, 15601 Crabbs Branch Way, Rockville, MD 20855, ETATS-UNIS
⁽²⁾ Department of Cell Biology, The Scripps Research Institute, La Jolla California 92093, ETATS-UNIS
⁽³⁾ Proteases and Tissue Remodeling Unit, Oral and Pharyngeal Cancer Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, 30 Convent Drive, Bethesda, MD 20892, ETATS-UNIS
⁽⁴⁾ Department of Molecular Biology, Corvas International, San Diego, California 92121, ETATS-UNIS

Résumé / Abstract

Dysregulated proteolysis is a hallmark of cancer. Malignant cells require a range of proteolytic activities to enable growth, survival, and expansion. Serine proteases of the S1 or trypsin-like family have well recognized roles in the maintenance of normal homeostasis as well as in the pathology of diseases such as cancer. Recently a rapidly expanding subgroup of S1 proteases has been recognized that are directly anchored to plasma membranes. These membrane anchored serine proteases are anchored either via a carboxy-terminal transmembrane domain (Type I), a carboxy terminal hydrophobic region that functions as a signal for membrane attachment via a glycosyl-phosphatidylinositol linkage (GPI-anchored), or via an amino terminal proximal transmembrane domain (Type II or TTSP). The TTSPs also encode multiple domains in their stem regions that may function in regulatory interactions. The serine protease catalytic domains of these enzymes show high homology but also possess features indicating unique substrate specificities. It is likely that the membrane anchored serine proteases have evolved to perform complex functions in the regulation of cellular signaling events at the plasma membrane and within the extracellular matrix. Disruption or mutation of several of the genes encoding these proteases are associated with disease. Many of the membrane anchored serine proteases show restricted tissue distribution in normal cells, but their expression is widely dysregulated during tumor growth and progression. Diagnostic or therapeutic targeting of the membrane anchored serine proteases has potential as promising new approaches for the treatment of cancer and other diseases.

Revue / Journal Title

Cancer metastasis reviews   ISSN 0167-7659   CODEN CMRED4 

Source / Source

2003, vol. 22, n^o 2-3 (162 p.)  [Document : 22 p.] (146 ref.), pp. 237-258 [22 page(s) (article)]

Langue / Language

Anglais

Editeur / Publisher

Springer, Dordrecht, PAYS-BAS  (1982) (Revue)

Mots-clés anglais / English Keywords

Genetics ; Enzyme ; Hydrolases ; Peptidases ; Human ; Review ; Metastasis ; Gene expression ; Structure ; Cell surface ; Proteolysis ; Transmembrane protein ; Serine endopeptidases ; Malignant tumor ;

Mots-clés français / French Keywords

Génétique ; Enzyme ; Hydrolases ; Peptidases ; Homme ; Article synthèse ; Métastase ; Expression génique ; Structure ; Surface cellulaire ; Protéolyse ; Protéine transmembranaire ; Serine endopeptidases ; Tumeur maligne ;

Mots-clés espagnols / Spanish Keywords

Genética ; Enzima ; Hydrolases ; Peptidases ; Hombre ; Artículo síntesis ; Metástasis ; Expresión genética ; Estructura ; Superficie celular ; Proteolisis ; Proteína transmembranar ; Serine endopeptidases ; Tumor maligno ;

Mots-clés d'auteur / Author Keywords

serine protease ; cancer ; transmembrane ; GPI anchor ; TTSP ; membrane ;

Localisation / Location

INIST-CNRS, Cote INIST : 20923, 35400011109650.0080