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Título

Derivatives of 3-sec-butyl-1-oxo-2,3-dihydroisoquinoline as inhibitors of μ-calpain

AutorChicharro, Roberto ; Alonso Giner, Mercedes; Mazo, M.ª Teresa; Arán, Vicente J. ; Herradón García, Bernardo
Palabras claveCalpain
Inhibitors
Isoquinoline
Peptide-heterocycle hybrids
Peptidomimetics
Fecha de publicación23-may-2006
EditorJohn Wiley & Sons
CitaciónChemMedChem 1(7): 710-714 (2006)
ResumenThe calpains (E.C. 3.4.22.17) are a family of cysteine proteases and consist of about 20 isoenzymes. Although most of these isoenzymes are present in only particular tissues or species, two isoenzymes, calpain I (or μ-calpain) and calpain II (or m-calpain), are ubiquitous. A distinctive mechanistic feature of calpain is that the enzyme is activated by Ca2+; the in vitro Ca2+ concentration required for half-maximal activity of μ-calpain is 2–75 μM and for m-calpain, 200–1000 μM. As these concentrations are exceptionally high for in vivo activity, several alternative mechanisms for calpain activation have been proposed.
Descripción5 pages, 3 figures, 1 table.-- PMID: 16902923 [PubMed].-- Taken in part from the ongoing PhD thesis of R.C. and the MSc thesis of M.T.M. Patents ES-P200402995 and PCT-ES2005-070171 have been filed.
Versión del editorhttp://dx.doi.org/10.1002/cmdc.200600046
URIhttp://hdl.handle.net/10261/11410
DOI10.1002/cmdc.200600046
ISSN1860-7187
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