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Query: EC:3.6.3.1 (Mg2+-ATPase)
 1,484 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The phospholipid requirement for Ca2+-stimulated, Mg2+-dependent ATP hydrolysis (Ca2+/Mg2+-ATPase) and Mg2+-stimulated ATP hydrolysis (Mg2+-ATPase) in rat brain synaptosomal membranes was studied employing partial delipidation of the membranes with phospholipase A2 (Hog pancreas), phospholipase C (Bacillus cereus) and phospholipase D (cabbage). Treatment with phospholipase A2 caused an increase in the activities of both Ca2+/Mg2+-ATPase and Mg2+-ATPase whereas with phospholipase C treatment both the enzyme activities were inhibited. Phospholipase D treatment had no effect on Ca2+/Mg2+-ATPase but Mg2+-ATPase activity was inhibited. Inhibition of Mg2+-ATPase activity after phospholipase C treatment was relieved with the addition of phosphatidylinositol-4,5-bisphosphate (PIP2) and to a lesser extent with phosphatidylinositol-4-phosphate (PIP) and phosphatidylcholine (PC). Phosphatidylserine (PS), phosphatidic acid (PA), PIP and PIP2 brought about the reactivation of Ca2+/Mg2+-ATPase. Phosphatidylinositol (PI) and PA inhibited Mg2+-ATPase activity. Kms for Ca2+ (0.47 microM) and Mg2+ (60 microM) of the enzyme were found to be unaffected after treatment with the phospholipases.
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PMID:Phospholipid requirement of Ca2+-stimulated, Mg2+-dependent ATP hydrolysis in rat brain synaptic membranes. 294 70

ATPase activity and Ca2+ uptake were examined in microsomal membrane fractions isolated from guinea pig stomach smooth muscle which had been exposed to phospholipase C (PLC). Basal Mg2+-ATPase, Na+, K+-ATPase and Ca2+, Mg2+-ATP activities were inhibited in a time dependent manner by PLC treatment. There was positive correlations between each of these ATPase activities and total phospholipid content of the microsomal fraction. Phosphotidylcholine restored Ca2+, Mg2+-ATPase activity of the microsomal fraction isolated from the tissue which had been treated with PLC for 30 min but not after 60 min. Ca2+ uptake in the presence of ATP by microsomal fraction from tissue treated with PLC for 60 min was significantly decreased. The results provide a cellular basis for the inhibitory effect of PLC on contractility of stomach smooth muscle.
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PMID:ATPase activity and calcium uptake of microsomes isolated from stomach smooth muscle after exposure to phospholipase C. 622 98

Despite pronounced differences by which membrane-depolarizing or phospholipase C-activating stimuli initiate contractile responses, a rise in [Ca2+]i is considered the primary mechanism for induction of smooth muscle contractions. Subsequent to the formation of the well-characterized Ca(2+)4-calmodulin complex, interaction with the catalytic subunit of myosin light chain kinase triggers phosphorylation of 20 kDa myosin light chain and activates actin-dependent Mg2+-ATPase activity, which ultimately leads to the development of tension. The present article reviews the fundamental mechanisms leading to an increase in [Ca2+]i and discusses the biochemical processes involved in the transient and sustained phases of contraction. Moreover, the commentary summarizes current knowledge on the modulatory effect of changes in the microviscosity of the plasma membrane on the Ca2+ transient as well as the contractile response of smooth muscle. Evidence has accumulated that these changes in microviscosity alter the activity of membrane-bound enzymes and affect the generation of endogenous mediators responsible for the regulation of cytosolic Ca2+ concentrations and for the [Ca2+]i-sensitivity of myosin light chain phosphorylation.
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PMID:Ca2+ transient, cell volume, and microviscosity of the plasma membrane in smooth muscle. 925 51

The chicken T-tubule Mg2+-ATPase is an integral membrane glycoprotein that presents properties different from those of other ATPases located in skeletal muscle cells and exhibits ATP-hydrolysing activity on the extracellular side of the transverse tubule (TT) membranes. In this study we demonstrate that TT vesicles purified from chicken skeletal muscle possess ecto-ADPase and ecto-5'-nucleotidase activities that, along with ecto-ATPase, are able to sequentially degrade extracellular ATP to ADP, AMP and adenosine. Characterization studies of these TT ectonucleotidases revealed remarkable differences between ecto-ATPase and ecto-ADPase activities with respect to thermal stability, temperature dependence of the hydrolytic activity, effect of ionic strength, kinetic behaviour, divalent cation preference and responses to azide, N-ethylmaleimide, NaSCN, Triton X-100 and concanavalin A. Ecto-ATPase, but not ecto-ADPase, was inhibited by a polyclonal antibody against the chicken TT ecto-ATPase. On the basis of these results we propose that ATP and ADP hydrolysis are accomplished by two distinct enzymes and therefore the TT ecto-ATPase is not an apyrase. 5'-Nucleotidase activity was inhibited by adenosine 5'-[alpha,beta-methylene]diphosphate and concanavalin A, followed simple Michaelis-Menten kinetics and was released from the membranes by treatment with phosphatidylinositol-specific phospholipase C, indicating that AMP hydrolysis in T-tubules is catalysed by a typical ecto-5'-nucleotidase. Results obtained from electrophoresis experiments under native conditions suggest that ecto-ATPase, ecto-ADPase and 5'-nucleotidase might be associated, forming functional complexes in the T-tubule membranes. The TT ectonucleotidases constitute an enzymic cascade for the degradation of extracellular ATP that might be involved in the regulation of purinergic signalling in the muscle fibre.
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PMID:T-tubule membranes from chicken skeletal muscle possess an enzymic cascade for degradation of extracellular ATP. 958 72