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the faster migrating Tg adduct C primarily engages the CaBP1/P5 oxidoreductase, whereas the slower migrating Tg adduct A primarily engages ERp72.
Present the NMR structure of full-length CaBP1 (show S100G Proteins) with Ca(2 (show CA2 Proteins)+) bound at the first, third, and fourth EF-hands.
Different kinetics of Ca-dependent binding step between caldendrin and calmodulin (show CALM1 Proteins) with AKAP79 (show AKAP5 Proteins) suggest their different roles in synaptic function.
We demonstrate that calmodulin (show CALM1 Proteins) and caldendrin compete for a partially overlapping binding site on AKAP79 (show AKAP5 Proteins) and that their binding is differentially dependent on calcium
CaBP1 (show S100G Proteins) regulates voltage-dependent inactivation and activation of Ca(V)1.2 (show CACNA1C Proteins) (L-type) calcium channels
Structural basis for the differential effects of CaBP1 (show S100G Proteins) and calmodulin (show CALM1 Proteins) on Ca(V)1.2 (show CACNA1C Proteins) calcium-dependent inactivation.
enhances inactivation, causes a depolarizing shift in the voltage dependence of activation, and does not support Ca2 (show CA2 Proteins)+-dependent facilitation of Ca(v)2.1 (show CACNA1A Proteins) channels
CaBP1 (show S100G Proteins) is able to specifically regulate InsP3 receptor-mediated alterations in [Ca2 (show CA2 Proteins)+]i during agonist stimulation.
We describe a new role for CaBP1 (show S100G Proteins) in regulation of Ca2 (show CA2 Proteins)+ influx through Ca(v)1.2 (show CACNA1C Proteins) (L-type) Ca2 (show CA2 Proteins)+ channels. CaBP1 (show S100G Proteins) interacts directly with the alpha1 subunit of Ca(v)1.2 (show CACNA1C Proteins) at sites that also bind Calmodulin (show CALM1 Proteins)
the NT and IQ-domains of alpha(1)1.2 mediate functionally distinct interactions with CaBP1 (show S100G Proteins) and CaM (show CALM1 Proteins) that promote conformational alterations that either stabilize or inhibit inactivation of Ca(v)1.2 (show CACNA1C Proteins).
Results show that CaBP1/caldendrin and CaBP2 are not required for normal gross retinal and synapse morphology but are necessary for the proper transmission of light responses through the retina; CaBP1/caldendrin and CaBP2 likely act by modulating presynaptic Ca(2 (show CA2 Proteins)+)-dependent signaling mechanisms.
Study provides the first report of the expression and localization of CaBP1 and caldendrin in the mouse brain
These findings suggest that expression of paracellular tight junction genes is regulated by transcellular CaBP (show S100G Proteins) proteins, suggesting that active and passive calcium transport pathways may function cooperatively
TRPV6 (show TRPV6 Proteins), NCX1 (show SLC8A1 Proteins), and CaBP (show S100G Proteins)-9k in the fetal placenta and CaBP (show S100G Proteins)-28k in the maternal placenta may play key roles in controlling calcium transport across the placenta during pregnancy.
When immature mice were treated with 17beta-estradiol or progesterone for 3 days, we found that the expressions of Bax (show BAX Proteins) and caspase 3 protein (show CASP3 Proteins) were increased by estradiol treatment in WT and CaBP (show S100G Proteins)-9k KO mice.
Regulation of calbindin-D9k (show S100G Proteins) expression by 1,25-dihydroxyvitamin D(3) and parathyroid hormone (show PTH Proteins) in mouse primary renal tubular cells
These results suggest that the mouse uterine calbindin-D9k (show S100G Proteins) gene is expressed under the control of a progesterone response element.
demonstrated that the CaBP (show S100G Proteins)-9k is distinctly regulated in the mouse placenta and extra-embryonic membrane, probably via sex steroid hormones (E2 and P4) and their receptors through a complex pathway
Progesterone and its receptor may be dominant factors in the regulation of CaBP (show S100G Proteins)-9k but estrogen and ERalpha (show ESR1 Proteins) can influence the expression of the CaBP (show S100G Proteins)-9k gene via an indirect pathway in the uterus of immature mice.
These results suggest that calcium regulates CaBP-D9k expression by modulating the circulating 1,25-dihydrxyvitamin D(3) level and that Vitamin D receptor (show VDR Proteins) is thus required for the dietary calcium-induced suppression of CaBP-D9k expression.
Calcium binding proteins are an important component of calcium mediated cellular signal transduction. This gene encodes a protein that belongs to a subfamily of calcium binding proteins which share similarity to calmodulin. The protein encoded by this gene regulates the gating of voltage-gated calcium ion channels. This protein inhibits calcium-dependent inactivation and supports calcium-dependent facilitation of ion channels containing voltage-dependent L-type calcium channel subunit alpha-1C. This protein also regulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors, P/Q-type voltage-gated calcium channels, and transient receptor potential channel TRPC5. This gene is predominantly expressed in retina and brain. Alternative splicing results in multiple transcript variants encoding disinct isoforms.
, calcium-binding protein 1
, calcium binding protein 1
, calcium binding protein 5
, calcium binding protein 1 (calbrain)
, S100 calcium-binding protein G
, calbindin 3, (vitamin D-dependent calcium binding protein)
, calbindin D9k
, calbindin-D9K major form
, cytidine 5'-triphosphate synthase 2
, protein S100-G
, vitamin D-dependent calcium-binding protein, intestinal