Chimeric Ca2+-ATPase/Na+,K+-ATPase molecules
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چکیده
منابع مشابه
Induction of vacuolar Ca2+-ATPase and H+/Ca2+ exchange activity in yeast mutants lacking Pmr1, the Golgi Ca2+-ATPase.
We have analyzed Ca2+ transport activity in defined subcellular fractions of an isogenic set of wild-type and mutant yeast. The results, together with measurements of polypeptide expression levels and promoter::reporter gene activity, show that the Golgi Ca2+-ATPase, Pmr1, is the major Ca2+ pump under normal growth conditions. In the absence of Pmr1, we show a massive, calcineurin-dependent com...
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Mechanically sensitive hair cells of the auditory and vestibular systems use Ca2+ to control adaptation of mechanical transduction, to effect frequency tuning, to trigger neurotransmitter release, and to mediate efferent synaptic signaling. To determine the role that pumps play in regulation of Ca2+ in the hair bundle, the organelle responsible for mechanoelectrical transduction, we localized a...
متن کاملCa2’-ATPase Membrane Crystals in Sarcoplasmic Reticulum
Vanadate induces the formation of two-dimensional crystalline arrays of Ca2+-ATPase molecules in sarcoplasmic reticulum. The Ca2+-ATPase membrane crystals are evenly distributed among the terminal cisternae and longitudinal tubules of sarcoplasmic reticulum, but very few crystals were observed in the T tubules. Tryptic cleavage of the Ca2+ transport ATPase into two major fragments (A and B) did...
متن کاملTHE Ca2+-ATPase OF HEART SARCOLEMMA
THE Ca2+-ATPase OF HEART SARCOLEMMA P. Caroni and E. Carafoli, Laboratory of Biochemistry, Swiss Federal Institute of Technology (ETH), Universitiitstr. 16, 8092 Zurich, Switzerland The Ca2+-ATPase of heart sarcolema (SL) has high affinity for Ca2+ (K,,, = 0.3uM), is slightly stimulated by K ' , has a (ATP) of 30uM, a pH optimum of 7.3 and is highly sensitive to vanadate (Ki= 0.6uM). The high v...
متن کاملIn vitro effects of palmitylcarnitine on cardiac plasma membrane Na,K-ATPase, and sarcoplasmic reticulum Ca2+-ATPase and Ca2+ transport.
hkhir IUUSCle. LOW COnCeUbi~iOUS (5 t0 50 pM) Of palmitylcarnitine enhance Ca2+-ATPase activity and Ca2+ binding to sarcoplasmic reticulum and enhance [3H]ouabain binding to Na,K-ATPase above equilibrium binding levels but inhibit Na,K-ATPase hydrolytic activity. Increasing concentrations of palmitylcarnitine (50 to 200 PM) further inhibit Na,K-ATPase activity and markedly decrease the binding ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1993
ISSN: 0014-5793
DOI: 10.1016/0014-5793(93)80813-a