Disease relevance of ATP1B3P1

• We have previously reported the cloning of a gene that encodes a copper transporting P-type ATPase (ATP7B) which is defective in Wilson disease [1].
• Hepatic sodium-potassium-dependent ATPase in obesity [2].
• Reduced Langerhans' cell Ia antigen and ATPase activity in patients with the acquired immunodeficiency syndrome [3].
• Examination of six patients with an "AIDS-related complex" revealed significantly reduced numbers of Langerhans' cells per square millimeter; this reduction was more pronounced in staining for Ia antigen (306 +/- 69) than in staining for ATPase activity (517 +/- 101) [3].
• The putative proteasome-associated proteins Mpa (Mycobaterium proteasomal ATPase) and PafA (proteasome accessory factor A) of the human pathogen Mycobacterium tuberculosis (Mtb) are essential for virulence and resistance to nitric oxide [4].

Psychiatry related information on ATP1B3P1

• Red blood cell Na+, K+-, Mg2+-, and Ca2+-adenosine triphosphatase (ATPase) activities were studied longitudinally in eight patients with affective disorders and 12 healthy volunteers [5].
• Even though the mean Ca2+-ATPase activity was higher during manias and euthymic periods than during depressions, mood and ATPase activities did not correlate with each other in all patients [5].
• We demonstrate that the insertion of the B2 sequence reduces the motor activity of Dictyostelium myosin II, with reduction of the maximal actin-activated ATPase activity and a decrease in the affinity for actin [6].
• Erythrocyte membrane Na+-K+ ATPase and Ca++ATPase levels were investigated in 11 women treated with ECT for endogenous depression and 11 age-matched normal control subjects [7].
• Pathological lesions of Alzheimer's disease and dementia with Lewy bodies brains exhibit immunoreactivity to an ATPase that is a regulatory subunit of the 26S proteasome [8].

High impact information on ATP1B3P1

• Of the 80% of oxygen consumption coupled to ATP synthesis, approximately 25-30% is used by protein synthesis, 19-28% by the Na(+)-K(+)-ATPase, 4-8% by the Ca2(+)-ATPase, 2-8% by the actinomyosin ATPase, 7-10% by gluconeogenesis, and 3% by ureagenesis, with mRNA synthesis and substrate cycling also making significant contributions [9].
• Mutations in the gene-encoding SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+ ATPase, are associated with Brody disease [10].
• Furthermore, studies using the ATP analog, ATP gamma S, suggest either that protein phosphorylation alone is sufficient for dispersion or that transport is mediated by a unique force-generating ATPase that can use ATP gamma S for hydrolyzable energy [11].
• Sequence analysis indicated that TURF 2H3 originated by recombinations among portions of the flanking and/or coding regions of the maize mitochondrial 26S ribosomal gene, the ATPase subunit 6 gene, and the chloroplast tRNA-Arg gene [12].
• The AAA domain, a conserved Walker-type ATPase module, is a feature of members of the AAA family of proteins, which are involved in many cellular processes, including vesicular transport, organelle biogenesis, microtubule rearrangement and protein degradation [13].

Chemical compound and disease context of ATP1B3P1

• The CadA cadmium resistance ATPase of gram-positive bacteria and the CopB copper efflux system of Enterococcus hirae are homologous to P-type ATPases of animals and plants [14].
• A T-to-C transition at nucleotide (nt) 9176 in the mitochondrial adenosine triphosphatase 6 (ATPase 6) gene was detected in 2 brothers with a neurological disorder resembling Leigh syndrome [15].
• Ouabain-sensitive NaK ATPase may be useful as an indicator of state in affective illness; plasma cortisol may be continuously elevated in some individuals with affective disorder [16].
• Bafilomycin A1, a macrolide antibiotic isolated from Streptomyces species, has been used as an inhibitor of vacuolar H(+) ATPase (V-ATPase) [17].
• In the medullary collecting duct, NEM-sensitive ATPase activity was also markedly reduced in animals with acute ureteral obstruction; in the cortical collecting duct, activity fell significantly, but to a lesser degree than was observed in the medullary collecting duct [18].

Biological context of ATP1B3P1

• Fluorescence in situ hybridization with PAC DNA clones localized ATP1B3 to the q22-->23 region of Chromosome (Chr) 3, and the beta 3 pseudogene to the p13-->15 region of Chr 2 [19].
• Structural organization and chromosomal localization of the human Na,K-ATPase beta 3 subunit gene and pseudogene [19].
• Tilting of the light-chain domain of the head with respect to its actin-bound catalytic domain is thought to be coupled to the ATPase cycle [20].
• Myosin, the ATPase that interacts with actin to produce the force for muscle contraction and other forms of cell motility, is believed to be involved in cytokinesis but not in mitosis [21].
• A random hydrolysis mechanism is ruled out by the observed inhibition of ATPase in a mixed hexamer containing wt and an inactive Rho mutant [22].

Anatomical context of ATP1B3P1

• By immunofluorescence analysis using mAb P-3E10, it was found that all peripheral blood leukocytes express Na, K ATPase beta3 [23].
• Na, K ATPase beta3 subunit (CD298): association with alpha subunit and expression on peripheral blood cells [23].
• The Ca2+-stimulated ATPase which is the enzymatic expression of this pump varies in its calcium sensitivity between different preparations of erythrocyte ghosts, with activation generally occurring in a concentration range between approximately 1 and 10 microM Ca2+ (refs 2--5) [24].
• The Ca2+ + Mg2+-activated ATPase of the sarcoplasmic reticulum is responsible for the active Ca2+ transport of this membrane system, the key feature of which is the formation of an energy-rich phosphorylated transport enzyme (EP) and its conversion [25].
• DKH392, a construct containing two heads but no tails, has been shown to display both tight binding to microtubules and high ATPase rates [26].

Associations of ATP1B3P1 with chemical compounds

• Upon phytohemagglutinin or phorbol myristate acetate activation, the expression level of the Na, K ATPase beta3 subunit on activated peripheral blood mononuclear cells was not altered in comparison with those of unstimulated cells [23].
• It binds to microtubules under conditions of ATP depletion, possesses an ATPase activity and is sensitive to ultraviolet-induced, vanadate-dependent cleavage [27].
• Orthovanadate, a powerful inhibitor of the (Na+ + K+)ATPase and the Na pump, also inhibits the Ca-stimulated ATPase activity, which is the enzymatic basis for the uncoupled Ca pump, in human red cells [28].
• We localized the site of interaction to a single peptide isolated after cyanogen bromide cleavage of the ATPase [29].
• Gle1 and the phosphoinositide IP6 activate Dbp5's ATPase activity in vitro and this could provide critical spatial regulation of Dbp5 activity in vivo [30].

Physical interactions of ATP1B3P1

• hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha [31].
• On the basis of sequence homology to known genes, the WD gene (ATP7B) appears to be a copper-transporting P-type ATPase [32].
• The human Rad51 protein binds to single- and double-stranded DNA and exhibits DNA-dependent ATPase activity [33].
• The Lymn-Taylor model for the actomyosin ATPase suggests that during each cycle of ATP hydrolysis the complex of myosin subfragment 1 (S-1) with actin must dissociate into S-1.ATP plus actin before ATP hydrolysis can occur [34].
• The H+-translocating ATPase complex from the thermophilic bacterium PS3 (TF0-F1) is composed of a water-soluble part with ATP-hydrolyzing activity (TF1) and a membrane moiety with H+-conducting activity (TF0) [35].

Regulatory relationships of ATP1B3P1

• The majority of P-glycoprotein mutants containing a single cysteine residue retained substantial amounts of drug-stimulated ATPase activity and were not inhibited by dBBn [36].
• Calponin inhibits actomyosin Mg2+ ATPase and is proposed to regulate smooth muscle contraction; however, the mechanism by which it exerts its effect and the regulation of its behavior is still under investigation [37].
• The delta pH is dissipated only under conditions in which the photosystem I turns, confirming that the thioredoxin must be reduced to activate the ATPase [38].
• RESULTS: The mean Na+,K+ ATPase activity of peripheral blood mononuclear cells expressed as nanomoles per microgram protein per minute (nM/ microgram protein/ min) +/-1 standard deviation of the subjects with allergic rhinitis (n = 14) was 1.04 +/- 1.01, while that of the control subjects (n = 12) was 3.57 +/- 1.60 (P < or = .001) [39].
• The antibodies raised against human erythrocyte Dnp-SG ATPase cross-reacted with the bovine lens epithelium Dnp-SG ATPase which was identified by Western blot as a band corresponding to an approximate M(r) value of 80,000 Da [40].

Other interactions of ATP1B3P1

• The exon/intron organization of the beta 3 subunit gene is identical to that of the Na,K-ATPase beta 3 subunit gene, indicating that these two genes evolved from a common evolutionary ancestor [19].
• The ATPase activity of hMutSalpha variants carrying the Lys-->Arg mutation in hMSH2 or in hMSH6 was severely affected, but these mutants were still proficient in mismatch binding and were able to complement, albeit to different extents, mismatch repair-deficient cell extracts [31].
• (a) Serial sections were either incubated with anti-CA IV/FITC or processed for endothelial ATPase reaction [41].
• The interaction not only reduced both the ATPase and the helicase activities of XPB purified in the baculovirus system but also impaired XPB-mediated cross-complementation of the repair deficiency in rodent UV-sensitive mutants of group 3 [42].
• Mutation of lysine residue 798 in the DNA-dependent ATPase domain of BRG1 significantly reduced its ability to repress c-fos transcription [43].

Analytical, diagnostic and therapeutic context of ATP1B3P1

• We report X-ray solution scattering and electron microscopy structures of the activated, full-length nitrogen-regulatory protein C (NtrC) showing a novel mechanism for regulation of AAA+ ATPase assembly via the juxtaposition of the receiver domains and ATPase ring [44].
• Finally, recent biochemical dissection of the ATPase cycle and its coupling to protein unfolding has revealed fundamental operating principles of this important, ubiquitous family of molecular machines [45].
• Immunoblotting analysis revealed a selective decrease in the amount of phospholamban protein, without a significant change in the content for either sarcoplasmic reticulum Ca2+ ATPase or calsequestrin, in the transgenic hearts compared with controls [46].
• The immunoassay allows measurement of proton-pumping ATPase levels in human gastric biopsy specimens and may therefore be useful in studies of gastric mucosal function [47].
• Indeed, axoplasm contains actin-dependent ATPase activity, and a pan-myosin antibody recognized at least four bands in Western blots of axoplasm [48].

References