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ADAMTS proteases in vascular biology.
Rodríguez-Manzaneque, Juan Carlos; Fernández-Rodríguez, Rubén; Rodríguez-Baena, Francisco Javier; Iruela-Arispe, M Luisa.
Afiliación
  • Rodríguez-Manzaneque JC; GENYO, Centre for Genomics and Oncological Research, Pfizer, Universidad de Granada, Junta de Andalucía, 18016 Granada, Spain. Electronic address: juancarlos.rodriguez@genyo.es.
  • Fernández-Rodríguez R; GENYO, Centre for Genomics and Oncological Research, Pfizer, Universidad de Granada, Junta de Andalucía, 18016 Granada, Spain.
  • Rodríguez-Baena FJ; GENYO, Centre for Genomics and Oncological Research, Pfizer, Universidad de Granada, Junta de Andalucía, 18016 Granada, Spain.
  • Iruela-Arispe ML; Department of Molecular, Cell, and Developmental Biology, Molecular Biology Institute, University of California, Los Angeles, Los Angeles, CA 90095, USA. Electronic address: arispe@mcdb.ucla.edu.
Matrix Biol ; 44-46: 38-45, 2015.
Article en En | MEDLINE | ID: mdl-25698314
ABSTRACT
ADAMTS (a disintegrin and metalloprotease with thrombospondin motifs) proteases comprise the most recently discovered branch of the extracellular metalloenzymes. Research during the last 15years, uncovered their association with a variety of physiological and pathological processes including blood coagulation, tissue repair, fertility, arthritis and cancer. Importantly, a frequent feature of ADAMTS enzymes relates to their effects on vascular-related phenomena, including angiogenesis. Their specific roles in vascular biology have been clarified by information on their expression profiles and substrate specificity. Through their catalytic activity, ADAMTS proteases modify rather than degrade extracellular proteins. They predominantly target proteoglycans and glycoproteins abundant in the basement membrane, therefore their broad contributions to the vasculature should not come as a surprise. Furthermore, in addition to their proteolytic functions, non-enzymatic roles for ADAMTS have also been identified expanding our understanding on the multiple activities of these enzymes in vascular-related processes.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Neovascularización Fisiológica / Proteínas ADAM / Neovascularización Patológica Límite: Animals / Humans Idioma: En Revista: Matrix Biol Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA Año: 2015 Tipo del documento: Article

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Neovascularización Fisiológica / Proteínas ADAM / Neovascularización Patológica Límite: Animals / Humans Idioma: En Revista: Matrix Biol Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA Año: 2015 Tipo del documento: Article