Zobrazeno 1 - 10
of 14
pro vyhledávání: '"B. S. Tuana"'
Publikováno v:
The Journal of biological chemistry. 272(51)
Two overlapping cDNAs encoding a novel sarcolemmal associated protein (SLAP) were isolated from a cardiac cDNA expression library by immunoscreening with anti-sarcolemmal antibodies. Further characterization of these clones showed that they belonged
Publikováno v:
The Journal of biological chemistry. 270(43)
The dihydropyridine (DHP) and ryanodine (RY) receptors play a critical role in depolarization-induced calcium release in skeletal muscle, yet the factors which govern their expression remain unknown. We investigated the roles of electrical activity a
Publikováno v:
The American journal of physiology. 267(6 Pt 1)
The subcellular localization of dystrophin was examined in adult rabbit and rat cardiac myocytes with immunofluorescence and at higher resolution with immunogold. The aim was to resolve the conflicting reports on the presence of dystrophin in the tra
Publikováno v:
The Journal of biological chemistry. 269(34)
The expression of the dihydropyridine (DHP) and ryanodine receptors in skeletal muscle was investigated during development of rat myotubes in culture as well as during embryonic and postnatal development in the rat. Through the use of specific gene p
Publikováno v:
The Journal of biological chemistry. 267(23)
Low molecular weight GTP-binding proteins and their cellular interactions were examined in cardiac muscle. Heart homogenate was separated into various subcellular fractions by differential and sucrose density gradient centrifugation. Various fraction
Publikováno v:
Molecular pharmacology. 37(2)
The dihydropyridine receptor associated with the L-type Ca2+ channel in adrenal medulla membranes has been identified and characterized. [3H]PN200-110 binds in a stereoselective, saturable manner to a single class of high affinity sites in adrenal me
Autor:
B S Tuana, D H MacLennan
Publikováno v:
Journal of Biological Chemistry. 259:6979-6983
Two specific calmodulin antagonists, compound 48/80 and calmidazolium , at concentrations of 10-20 micrograms/ml and 10-20 microM, respectively, inhibited Ca2+ uptake in skeletal muscle sarcoplasmic reticulum vesicles without affecting Ca2+-ATPase ac
Autor:
N S Dhalla, B S Tuana
Publikováno v:
Journal of Biological Chemistry. 257:14440-14445
The Ca2+-dependent ATPase was solubilized from rat heart sarcolemmal membranes upon digestion with trypsin and was found to be different from Ca2+-stimulated Mg2+-dependent ATPase (Dhalla, N. S., Anand-Srivastava, M. B., Tuana, B. S., and Khandelwal,
Publikováno v:
Canadian Journal of Physiology and Pharmacology. 59:1122-1127
The ability of prostaglandins (PG) D2, E1, E2, F2α and I2 (2.8 × 10−11 M to 2.8 × 10−7 M) to modify Ca2+, Mg2+ and (Na+ + K+)-ATPase activities of rat heart sarcolemmal membrane fractions was examined. Administration of PGE2, PGF2α, and PGI2
Publikováno v:
The Canadian journal of cardiology. 2(6)
Effects of hypothyroidism on heart sarcolemmal activities were examined by using membrane preparations obtained by two different methods from rats treated with propylthiouracil for 6 to 8 weeks. ATP-independent Ca2+ binding, sialic acid and phospholi