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Matches in Nanopublications for { ?s ?p "The absence of PDE1C expression in all contractile/quiescent VSMC studied so far indicates that Ca2+ stimulated hydrolysis is unlikely to regulate cAMP levels in this VSMC phenotype. Thus, whereas PDE1C expression was markedly induced in VSMC cultured from several human arteries, no such induction was observed when rat, monkey, or bovine VSMC were similarly cultured (Rose et al., 1997; Liu and Maurice, 1998; Palmer and Maurice, 2000). PDE2 enzymes hydrolyze either cAMP or cGMP; hydrolysis is stimulated by cGMP binding to amino terminal allosteric regulatory sites known as GAF domains (Martinez et al., 2002)." ?g. }

• _4 value "The absence of PDE1C expression in all contractile/quiescent VSMC studied so far indicates that Ca2+ stimulated hydrolysis is unlikely to regulate cAMP levels in this VSMC phenotype. Thus, whereas PDE1C expression was markedly induced in VSMC cultured from several human arteries, no such induction was observed when rat, monkey, or bovine VSMC were similarly cultured (Rose et al., 1997; Liu and Maurice, 1998; Palmer and Maurice, 2000). PDE2 enzymes hydrolyze either cAMP or cGMP; hydrolysis is stimulated by cGMP binding to amino terminal allosteric regulatory sites known as GAF domains (Martinez et al., 2002)." provenance.
• _4 value "The absence of PDE1C expression in all contractile/quiescent VSMC studied so far indicates that Ca2+ stimulated hydrolysis is unlikely to regulate cAMP levels in this VSMC phenotype. Thus, whereas PDE1C expression was markedly induced in VSMC cultured from several human arteries, no such induction was observed when rat, monkey, or bovine VSMC were similarly cultured (Rose et al., 1997; Liu and Maurice, 1998; Palmer and Maurice, 2000). PDE2 enzymes hydrolyze either cAMP or cGMP; hydrolysis is stimulated by cGMP binding to amino terminal allosteric regulatory sites known as GAF domains (Martinez et al., 2002)." provenance.
• _4 value "The absence of PDE1C expression in all contractile/quiescent VSMC studied so far indicates that Ca2+ stimulated hydrolysis is unlikely to regulate cAMP levels in this VSMC phenotype. Thus, whereas PDE1C expression was markedly induced in VSMC cultured from several human arteries, no such induction was observed when rat, monkey, or bovine VSMC were similarly cultured (Rose et al., 1997; Liu and Maurice, 1998; Palmer and Maurice, 2000). PDE2 enzymes hydrolyze either cAMP or cGMP; hydrolysis is stimulated by cGMP binding to amino terminal allosteric regulatory sites known as GAF domains (Martinez et al., 2002)." provenance.