SEARCH · Search PubMed
Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.
Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.
Explore the source record for details and available documents.
Rabbit retinal Müller cells were isolated by means of papaine and mechanical dissociation. These cells were shown to have a well preserved morphology and to preserve viability for many hours. Intense wheat germ agglutinin binding occurs on the photoreceptor side of Müller cells, especially in the microvillous region. Rabbit retinal Müller cells have a Na+,K+-activated adenosine triphosphatase activity in the same order of magnitude as brain astroglial cells.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
The described experiments show the influence of a single dose of cadmium chloride (1.5 mg CdCl2/kg body weight applied intraperitoneally) on development of the male gonads from the 1st d of post-fetal life to 1.5 a of life. In the case of the enzymes triggering transportation processes, adenosine triphosphatase stimulated by Mg++ (Mg++-ATP-ase), alkaline phosphatase (AP), and 5'nucleotidase (5'Nt), a considerable damages begin to appear in the 15th d of life whereas in the case of acid phosphatase (AcP) already in the 1st d of life whereas in the case of acid phosphatase (AcP) already in the 1st d of life. These damages increase with age reaching their maximum in the 45th d of life.
Explore the source record for details and available documents.
Cochlear fibrocytes are the crucial component of the inner ear homeostasis and its defect by various causes; GJB2 (connexin [Cx] 26) mutation, for example, leads to hearing loss. In the present study, we investigated the potential use of human amniotic epithelial cells, proposed to possess pluripotential properties, as a source of transplantation therapy in inner ear disease. The mRNA of the gap junction protein Cx26 and Na-K-adenosine triphosphatase, the immunohistologic expression of these proteins, and the cells' intercellular communication capacity were detected in vitro. Their transplantation into the guinea pig cochlea revealed the survival and expression of the proteins even 3 weeks after transplantation. Transplanted human amniotic epithelial cells were localized at the site where the proteins function, strongly indicating their cooperation in the regional potassium ion recycling. This technology suggests the therapeutic potential for the treatment of hearing loss.
Explore the source record for details and available documents.
Prior studies indicate that the natriuretic effects of atrial natriuretic peptide (ANP) are due, in part, to an inhibition of the passive movement of sodium ions from tubular lumen through apical cation channels into renal tubular epithelium. The present work demonstrates that ANP also exerts a potent inhibitory effect on the active pumping of sodium ions by renal tubular sodium and potassium-activated adenosine triphosphatase (Na, K-ATPase). This action of ANP is relatively long lasting, is due to a change in enzyme Vmax and is specific for ouabain-sensitive activity. Enzyme modulation occurs with an EC50 for ANP of 0.1 nM, is independent of intracellular [Na+] and is associated with an increase in tissue cyclic GMP (cGMP), but not cyclic AMP (cAMP). Modulation of Na, K-ATPase by ANP is mimicked by 8-bromo-cGMP and okadaic acid (OA) and is blocked by KT 5823, a selective inhibitor of cGMP-dependent protein kinase (PKG), but not by KT 5720, a selective inhibitor of cyclic AMP-dependent protein kinase (PKA), which suggests that the action of ANP on the sodium pump involves cGMP-mediated changes in protein phosphorylation. Regulation of renal Na, K-ATPase activity also occurs with nitric oxide-generating compounds, such as nitroglycerin and sodium nitroprusside (SNP). However, the ability of ANP to modulate Na, K-ATPase does not appear to involve this latter pathway because the effects of ANP on the sodium pump cannot be blocked by either N omega-nitro-L-arginine, an inhibitor of NO synthase, or hemoglobin, which blocks NO through binding.(ABSTRACT TRUNCATED AT 250 WORDS)
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Several studies suggested that catecholamines modulate renal sodium and water excretion by direct stimulation of adrenergic receptors located on the renal proximal tubule. However, neither the mechanism nor the class of adrenoceptor involved in this effect have yet been established definitively. In the present study, we examined the effects of L-norepinephrine (NE) and selective alpha-1, alpha-2 and beta adrenergic agonists on monovalent cation transport and on Na+-K+-adenosine triphosphatase (ATPase) activity from homogenates, intact tubules and highly purified basolateral membranes prepared from superficial rabbit kidney cortex. Our results showed that neither NE nor specific alpha-1, alpha-2 and beta adrenergic agonists (10 microM) modified ouabain-sensitive uptake of 86Rb+ (a K+ analog) in intact proximal tubules. Similarly, it is demonstrated that NE and alpha and beta adrenergic agonists did not affect Na+-K+-ATPase activity from homogenates, intact tubules and basolateral membranes. The integrity of the alpha-2 adrenergic receptor system, the predominant adrenergic subtype in rabbit proximal tubule, was supported by the following findings: 1) maximal binding of [3H] rauwolscine was about 4-fold higher in basolateral membranes than in homogenates; 2) 5'-guanylimidodiphosphate induced a 27-fold increase in the Ki of NE for alpha-2 receptor in basolateral membranes; 3) NE (5 microM) inhibited by 35% parathyroid hormone-stimulated cyclic AMP production in intact tubules. In conclusion, these data fail to demonstrate that NE, as well as other adrenergic agonists, directly increases Na+-K+-ATPase in the rabbit proximal tubule. Further investigations are needed to clarify the interaction of catecholamines with the renal Na+K+ pump.
Multiple signaling pathways are known to induce apoptosis in thymocytes through mechanisms that include the loss of mitochondrial membrane potential, cell shrinkage, caspase activation, and DNA degradation but little is known about the consequences of apoptosis on the properties of the plasma membrane. We have previously shown that apoptotic signals, including survival factor withdrawal and glucocorticoids, induce plasma membrane depolarization during rat thymocyte apoptosis, but the mechanisms involved in this process are unknown. We report here that inhibition of the Na(+)/K(+)-adenosine triphosphatase (Na(+)/K(+)-ATPase) with ouabain similarly depolarized control thymocytes and enhanced glucocorticoid-induced membrane depolarization, suggesting a link between Na(+)/K(+)-ATPase and plasma membrane depolarization of thymocytes. To determine whether repression of Na(+)/K(+)-ATPase levels within cells can account for the loss of plasma membrane potential, we assessed protein levels of the Na(+)/K(+)-ATPase in apoptotic thymocytes. Spontaneously dying thymocytes had decreased levels of both catalytic and regulatory subunits of Na(+)/K(+)-ATPase, and glucocorticoid treatment enhanced the loss of Na(+)/K(+)-ATPase protein. The pan caspase inhibitor (z-VAD) blocked both cellular depolarization and repression of Na(+)/K(+)-ATPase in both spontaneously dying and glucocorticoid-treated thymocytes; however, specific inhibitors of caspase 8, 9, and caspase 3 did not. Interestingly, glucocorticoid treatment simultaneously induced cell shrinkage and depolarization. Furthermore, depolarization and the loss of Na(+)/K(+)-ATPase protein were limited to the shrunken population of cells. The data indicate an important role for Na(+)/K(+)-ATPase in both spontaneous and glucocorticoid-induced apoptosis of rat thymocytes.
A direct potential measurement of the activity of bound ATPase has been achieved with beef heart submitochondrial particles adhering to a thick phospholipidic membrane. Electric signals (90 mV amplitude) were found to be fully sensitive to ATPase inhibitors and uncouplers.
A case of infantile malignant osteopetrosis is described. The patient died from respiratory hemorrhage at 7 months of age despite treatment that included high doses of active vitamin D and administration of interferon-gamma. A postmortem examination revealed the presence of many osteoclasts in the bone, which lacked ruffled borders. This observation was consistent with the histology of bone reported in Atp6i-knockout mice, which lack the gene encoding the a3 subunit of vacuolar-type H(+)-adenosine triphosphatase (ATPase). Sequence analysis of the TCIRG1 gene encoding the a3 subunit revealed two novel mutations: a deletion/insertion mutation in exon 9 and a T-to-C transition at the splice donor site of intron 19. The former mutation caused a frame shift and premature stop codon. The latter was associated with abnormal splicing, which was confirmed by sequencing the products amplified by reverse transcription-polymerase chain reaction (RT-PCR), using total RNA from the liver specimen as template. Although several mutations in the TCIRG1 gene in infantile malignant osteopetrosis have been reported in other populations, this is the first case of a Japanese patient with a mutation identified in this gene. These results support the important role of the subunit in the function of the proton pump.
The positive inotropic action (PIA) of ouabain was analyzed kinetically using isolated perfused rabbit heart. The input function of the ouabain concentration in the perfusate (Ci) into the heart was controlled by changing the volume of the reservoir and the rate of ouabain infusion into the reservoir fixed in front of the heart. The time courses of PIA were measured continuously with different infusion rates. The relationship between Ci and PIA clearly depended on the infusion rate in isolated perfused rabbit heart. The binding kinetics of ouabain to Na+, K+-adenosine triphosphatase (ATPase) in the cardiac homogenate showed two kinds of binding sites. The association rate constant (kappa 1), the dissociation rate constant (kappa-1) and the binding capacity of each site was estimated by the simultaneous fitting method. The occupation curve of the high affinity site corresponded well with the PIA measured in the isolated perfused heart at steady state. These results indicate that ouabain binding to the high affinity site is related to the PIA, and the slow binding process of ouabain to Na+, K+-ATPase may be one of the principal reasons for the infusion-rate dependence of ouabain PIA.