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ADAM Metalloproteinases as Potential Drug Targets.
Camodeca, Caterina; Cuffaro, Doretta; Nuti, Elisa; Rossello, Armando.
Afiliação
  • Camodeca C; Department of Pharmacy, University of Pisa, Via Bonanno 6, Pisa, Italy.
  • Cuffaro D; Department of Pharmacy, University of Pisa, Via Bonanno 6, Pisa, Italy.
  • Nuti E; Department of Pharmacy, University of Pisa, Via Bonanno 6, Pisa, Italy.
  • Rossello A; Department of Pharmacy, University of Pisa, Via Bonanno 6, Pisa, Italy.
Curr Med Chem ; 26(15): 2661-2689, 2019.
Article em En | MEDLINE | ID: mdl-29589526
ABSTRACT
The ADAMs, together with ADAMTSs and snake venom metalloproteases (SVMPs), are members of the Adamalysin family. Differences in structural organization, functions and localization are known and their domains, catalytic or non-catalytic, show key roles in the substrate recognition and protease activity. Some ADAMs, as membrane-bound enzymes, show sheddase activity. Sheddases are key to modulation of functional proteins such as the tumor necrosis factor, growth factors, cytokines and their receptors, adhesion proteins, signaling molecules and stress molecules involved in immunity. These activities take part in the regulation of several physiological and pathological processes including inflammation, tumor growth, metastatic progression and infectious diseases. On these bases, some ADAMs are currently investigated as drug targets to develop new alternative therapies in many fields of medicine. This review will be focused on these aspects.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Inibidores de Proteases / Proteínas ADAM Limite: Animals / Humans Idioma: En Revista: Curr Med Chem Ano de publicação: 2019 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Inibidores de Proteases / Proteínas ADAM Limite: Animals / Humans Idioma: En Revista: Curr Med Chem Ano de publicação: 2019 Tipo de documento: Article