Use your antibodies-online credentials, if available.
Il n’y a pas de produits dans votre liste de comparaison.
Votre panier est vide.
Afficher tous les synonymes
Sélectionnez vos espèces d'intérêt
physiological function of Pde1c in Drosophila melanogaster
The Drosophila genome encodes five novel PDE genes in addition to dunce. Predicted PDE sequences of Drosophila show highly conserved critical domains when compared with human PDEs.
By whole-mount immunofluorescence on postnatal day 3 mouse cochlea, we show its expression in outer (OHC) and inner (IHC) hair cells cytosol co-localizing with Lamp-1 in lysosomes. Furthermore, we provide evidence that the variant alters the PDE1C hydrolytic activity for both cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate (cGMP).
Cardiac Pde1C is a direct transcriptional target of PPARalpha.
Ligation injury caused a marked increase 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 release from juxtaglomerular cells.
By combining population-specific mutation arrays, targeted deafness genes panel, whole exome sequencing (WES), we identified PDE1C (Phosphodiesterase 1C) c.958G>T (p.A320S) as the disease-associated variant. Structural modeling insights into p.A320S strongly suggest that the sequence alteration will likely affect the substrate-binding pocket of PDE1C.
PDE1C is a proliferation-associated gene in glioblastoma multiforme cells in vitro.
PDE1C is an important regulator of SMC proliferation, migration, and neointimal hyperplasia, in part through modulating endosome/lysosome-dependent PDGFRbeta protein degradation via low-density lipoprotein receptor-related protein-1.
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
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)