High impact information on LOC538603

• However, carp parvalbumin and chicken intestinal vitamin D-dependent calcium binding protein do not inhibit the phenothiazine--calmodulin interaction [1].
• These results suggest that the known amino acid sequence homology among calmodulin, troponin C, and S100b may be reflected in a similar functional domain present in these proteins but absent in parvalbumin and vitamin D-dependent protein [1].
• The primary and tertiary structural features which promote the formation of an EF hand were originally identified from the structure of parvalbumin [2].
• In the absence of MAPs, calmodulin enhances the rate and extent of polymerization of pure tubulin, probably by sequestering Ca2+ from tubulin since the effect is mimicked by ethylene glycol bis(beta-aminoethyl ether)N,N,N',N'-tetraacetic acid and parvalbumin [3].
• In order to identify the physiological regulator of calcium dependent myosin light chain kinases of cardiac, skeletal, and smooth muscles, the effects of the three homologous calciproteins, calmodulin, troponin C, and parvalbumin, on the kinases isolated from bovine myocardium, rabbit skeletal muscle, and turkey gizzard were examined [4].

Biological context of LOC538603

• From these results we conclude that Ca2+ buffers with slow kinetics, such as PV, may cause biexponential decays in [Ca2+] transients, thereby complicating the analysis of endogenous Ca2+ binding ratios (kappaS) based on time constants [5].
• Modulation of the catalytic subunit of cyclic AMP-dependent protein kinase by calmodulin, S-100 protein, parvalbumin and troponin [6].
• Little or no phosphorylation was seen with parvalbumin, the brain Ca2+-binding protein (CBP-18) and intestinal calcium-binding protein [7].

Anatomical context of LOC538603

• Only calmodulin was effective in stimulating the cardiac, skeletal, or smooth muscle kinase; troponin C and parvalbumin exhibited no activation of any of the three kinases, even when examined at concentrations as high as 10-(5) M [4].
• Kinetics of Ca2+ binding to parvalbumin in bovine chromaffin cells: implications for [Ca2+] transients of neuronal dendrites [5].
• Identification of parvalbumin alpha in bovine hypothalamus: a partial primary structure [8].
• This antibody was also shown to cross-react with bovine cardiac troponin C, barnacle (Balanus nubilus) troponin C, bovine testis calmodulin and carp parvalbumin [9].

Associations of LOC538603 with chemical compounds

• Observations on the effects of UV irradiation on the thrombic fragments of calmodulin and on related calcium binding proteins (rabbit skeletal muscle troponin C, bovine cardiac troponin C, and parvalbumin) support the interpretation that dityrosine formation in calmodulin results from the intramolecular cross-linking of Tyr-99 and Tyr-138 [10].
• The dissociation kinetics of complexes of bovine alpha-lactalbumin and cod parvalbumin with Ca(II) and Mg(II) ions induced by mixing of a Ca(II)- or MG(II)-loaded protein with a chelator of divalent cations (EDTA or EGTA) have been studied by means of the stopped-flow method with intrinsic protein fluorescence registration [11].
• Purified troponin-C, calmodulin, myosin DTNB light chain, and parvalbumin were clearly identified by this method [12].

Other interactions of LOC538603

• Inhibition of phospholipase A2 activity by calmodulin, S-100, calregulin, parvalbumin, troponin-C, or CAB-48 was not observed [13].
• The activity of the catalytic subunit of cyclic AMP-dependent protein kinase (A-PK), utilizing type II-S, III-S histone or protamine (free base) as a substrate, was augmented in the presence of regulatory protein including calmodulin, S-100 protein, parvalbumin, or troponin [6].

References