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Human Polyclonal PDE1C Primary Antibody for CM, ICC - ABIN2747083
Baxendale, Fraser: Mammalian sperm phosphodiesterases and their involvement in receptor-mediated cell signaling important for capacitation. in Molecular reproduction and development 2006
Show all 13 Pubmed References
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
Show all 3 Pubmed References
Human Polyclonal PDE1C Primary Antibody for ICC, IF - ABIN152823
Ortiz-Capisano, Liao, Ortiz, Beierwaltes: Calcium-dependent phosphodiesterase 1C inhibits renin release from isolated juxtaglomerular cells. in American journal of physiology. Regulatory, integrative and comparative physiology 2009
physiological function of Pde1c in Drosophila melanogaster
The Drosophila genome encodes five novel PDE (show TWIST1 Antibodies) genes in addition to dunce (show PDE4D Antibodies). Predicted PDE (show TWIST1 Antibodies) sequences of Drosophila show highly conserved critical domains when compared with human PDEs.
Ligation injury caused a marked increa (show DYM Antibodies)se in neointimal and medial thickening in PDE1C+/+ mice. Injury-induced neointimal formation was significantly attenuated by PDE1C deficiency (knockout mice) or PDE1 inhibition in vivo.
PDE1C is expressed in isolated juxtaglomerular cells, and contributes to calcium's inhibitory modulation of renin (show REN Antibodies) release from juxtaglomerular cells.
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
, phosphodiesterase 1c
, phosphodiesterase 1C, calmodulin-dependent 70kDa
, calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
, calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C-like
, cam-PDE 1C
, cyclic nucleotide phosphodiesterase 1 C
, phosphodiesterase 1C calmodulin-dependent (70kD)
, Human 3',5' cyclic nucleotide phosphodiesterase (HSPDE1C1A)