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Cyclic nucleotide phosphodiesterases (PDEs) catalyze hydrolysis of the cyclic nucleotides cAMP and cGMP to the corresponding nucleoside 5-prime-monophosphates.
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Human Polyclonal PDE1C Primary Antibody for IHC (p) - ABIN2476116
Yan, Zhao, Bentley, Beavo: The calmodulin-dependent phosphodiesterase gene PDE1C encodes several functionally different splice variants in a tissue-specific manner. in The Journal of biological chemistry 1996
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PDE1C is a proliferation-associated gene in glioblastoma multiforme cells in vitro.
PDE1C is an important regulator of SMC (show DYM Antibodies) proliferation, migration, and neointimal hyperplasia, in part through modulating endosome/lysosome-dependent PDGFRbeta protein degradation via low-density lipoprotein receptor-related protein-1 (show LRP1 Antibodies).
PDE1C levels decreased in all conditions that inhibited proliferation
PDE1C1 is expressed at high levels in human cardiac myocytes with an intracellular distribution distinct from that of PDE3A (show PDE3A Antibodies)
Cyclic nucleotide phosphodiesterases (PDEs) catalyze hydrolysis of the cyclic nucleotides cAMP and cGMP to the corresponding nucleoside 5-prime-monophosphates. Mammalian PDEs have been classified into several families based on their biochemical properties. Members of the PDE1 family, such as PDE1C, are calmodulin (see MIM 114180)-dependent PDEs (CaM-PDEs) that are stimulated by a calcium-calmodulin complex (Repaske et al., 1992
Human 3',5' cyclic nucleotide phosphodiesterase (HSPDE1C1A)
, calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
, cam-PDE 1C