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Human Polyclonal GUCA1A Primary Antibody for IHC (p), ELISA - ABIN544570
Subbaraya, Ruiz, Helekar, Zhao, Gorczyca, Pettenati, Rao, Palczewski, Baehr: Molecular characterization of human and mouse photoreceptor guanylate cyclase-activating protein (GCAP) and chromosomal localization of the human gene. in The Journal of biological chemistry 1995
Show all 3 Pubmed References
GCAP1 and GCAP2 bound to different regions on the target guanylate cyclase type 1 with submicromolar affinity (apparent KD-values of 663 +/- 121 nM and 231 +/- 63 nM for Ca(2+)-free GCAP1 and GCAP2, respectively).
Allosteric communication pathways routed by Ca(2+)/Mg(2+) exchange in GCAP1 selectively switch target regulation modes.
GUCA1A mutations could cause significant variability in maculopathies, including central areolar choroidal dystrophy, which represents a severe pattern of maculopathy.
The two novel mutations described in this study are associated with distinct phenotypes, macular dystrophy for p.Val101del and cone dystrophy for p.Asp148Glu, with no intrafamilial phenotypic heterogeneity.
GCAP1 mutation is associated with macular dystrophy.
Retinal dystrophy-associated missense mutations (L84F, I107T) in GUCA1A with distinct molecular properties result in a similar aberrant regulation of the retinal guanylate cyclase.
Dimerization domain of RETGC1 is an essential part of GCAP1 and GCAP2 binding interface.
The GCAP1 and GCAP2 binding site(s) overlaps within the kinase homology and/or dimerization domains of retinal GC1.
GUCA1A and GUCY2D mutations are both accompanied by similar pattern of generalized cone dysfunction with a tendency to less involvement of the rod photoreceptors and a less severe phenotype in patients with GUCA1A.
RetGC1 activation by GCAP1 involves establishing a tight complex through the binding patch with an additional activation step involving Met-26, Lys-85, and Trp-94.
All four mutant GCAP1 family members showed sensitivity or acuity losses relative to normal observers.
we predicted that either haploinsufficiency or dominant-negative effect accompanied by creation of a novel function for the mutant protein is a possible mechanism of the retinal degeneration due to c.250C>T and c.320T>C of the GUCA1A
Patients with autosomal dominant cone-rod dystrophy caused by a D100G mutation in GUCA1A exhibit progressive vision loss early within the first decade of life identifiable by distinct ERG.
the GUCA1A mutation only contributes to a small portion of CORD in people of Chinese descent.
Stimulation by GCAP increases the maximal velocity (Vmax) for retinal guanylyl cyclase activation up to 100-fold in HEK293 cell membranes.
The consequences of specific mutations on GCAP1 structure and GC stimulation, are described.
role in rescuing cone recovery kinetics in knockout mice
The dynamic range for recombinant photoreceptor guanylyl cyclase-1 regulation by calcium (Ca2+)/GCAP1 is determined by both the affinity of GCAP1 for Ca2+ and relative affinities of the effector enzyme for the Ca2+-free versus Ca2+-loaded GCAP1.
A novel GCAP1 mutation, I143NT, caused a form of autosomal dominant cone degeneration that destroys foveal cones by mid-life but spares some cones in the peripheral retina up to 75 years.
A novel L151F missense mutation in the EF4 high affinity Ca2+ binding site of GCAP1 is linked to adCD (autosomal dominant cone dystrophy) in a large pedigree.
EPR double electron-electron resonance and site-directed mutagenesis analysis determined an atomic resolution structural model of a GCAP1 dimer. It has intermolecular hydrophobic contacts involving the side chain atoms of H19, Y22, F73 and V77. Mutating any of these at the dimer interface abolished dimerization. Dimerization may affect compartmentalization of GCAP1 in the photoreceptors and/or affect cyclase regulation.
Data suggest that GCAP1 (Mg2+ vs. Ca2+) exhibits conformational changes in Ca2+ switch helix that are important in activation of RetGC1 (photoreceptor guanylate cyclase); myristoylation of GCAP1 is important as well in attaining activator conformation.
Data suggest that dimerization domain of GUCY2D operates as a calcium-sensitive regulatory module; GUCY2D requires correct conformation of monomer-monomer interface for interaction with guanylate cyclase activating proteins (GCAP1; GCAP2).
Presence of bound magnesium (Mg2+) in guanylate cyclase activator protein GCAP-1 is essential for its ability to stimulate retinal guanylyl cyclase.
conclude that, under normal physiological conditions, GCAP1 dominates the regulation of cGMP synthesis in mouse cones, but if its function becomes compromised, GCAP2 contributes to the regulation of phototransduction and light adaptation of cones
Direct association between RD3 and GCAP1 is important for GC1 targeting.
The wild type and mutants of GCAP1 displayed large differences in Ca(2+)-binding and regulation and preserved an intact secondary and tertiary structure with a significant rearrangement of the aromatic residues upon binding of Ca(2+).
GCAP1 is the 'first-response' sensor protein that stimulates retinal membrane guanylyl cyclase early in the rod photoresponse.
results argue that there must be a cellular mechanism that limits GCAP1 access to RetGC2 and makes RetGC1 isozyme a preferential target for the disease-causing GCAP1 mutants.
Recombinant Gcap14 protein cosedimented with pure microtubules, indicating a direct binding between the two
Calcium-myristoyl Tug is a new mechanism for intramolecular tuning of calcium sensitivity and target enzyme interaction for guanylyl cyclase-activating protein 1
Stimulation by GCAP increases the maximal velocity (Vmax) for retinal guanylyl cyclase (RetGC1) activation up to 20-fold in mouse photoreceptor outer segment.
GCAP-activated native retinal membrane (Ret)GC1 and RetGC2 are less sensitive to inhibition by calcium ions in the presence of GCAP1 than GCAP2.
Mutant GCAP1, when under normal expression control, causes both rod and cone photoreceptors to lose function and degenerate, with cone cells being more severely affected, in keeping with the human disease phenotype.
GCAP1 at near normal levels supports the generation of wild-type flash responses in the absence of GCAP2.
GCAP functions in intact photoreceptors [review]
These results provide the first direct evidence that a mutation [in GCAP1] linked to congenital blindness increases Ca2+ in the outer segment, which may trigger the apoptotic process.
Prolonged illumination up-regulates retinal arrestin and Guca1a/b: a novel mechanism for light adaptation.
This gene plays a role in the recovery of retinal photoreceptors from photobleaching. In the recovery phase, the phototransduction messeneger cGMP is replenished by retinal guanylyl cyclase-1 (GC1). GC1 is activated by decreasing Ca(2+) concentrations following photobleaching. The protein encoded by this gene, guanylyl cyclase activating protein 1 (GCAP1), mediates the sensitivity of GC1 to Ca(2+) concentrations. GCAP1 promotes activity of GC1 at low Ca(2+) concentrations and inhibits GC1 activity at high Ca(2+) concentrations. Mutations in this gene cause autosomal dominant cone dystrophy (COD3)\; a disease characterized by reduced visual acuity associated with progressive loss of color vision. Mutations in this gene prohibit the inactivation of RetGC1 at high Ca(2+) concentrations\; causing the constitutive activation of RetGC1 and, presumably, increased cell death. This gene is expressed in retina and spermatagonia.
, cone dystrophy 3
, guanylate cyclase-activating protein, photoreceptor 1
, guanylin 1, retina
, guanylyl cyclase-activating protein 1
, guanylate cyclase activator 1A (retina)