Gentamicin resistance in Staphylococcus aureus.
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Drug Resistance, Microbial↗
Biomedical subjects
J Biber
Publications and source records attributed to J Biber.
The surface membrane of the small intestinal epithelial cell. I. Localization of adenyl cyclase.
The subcellular distribution of adenyl cyclase was investigated in small intestinal epithelial cells. Enterocytes were isolated, disrupted and the resulting membranes fractionated by differential and sucrose gradient centrifugation. Separation of luminal (brush border) and contra-luminal (basolateral) plasma membrane was achieved on a discontinuous sucrose gradient. The activity of adenyl cyclase was followed during fractionation in relation to other enzymes, notably those considered as markers for luminal and contraluminal plasma membrane. The luminal membrane was identified by the membrane-bound enzymes sucrase and alkaline phosphatase and the basolateral region by (Na+ + K+)-ATPase. Enrichment of the former two enzymes in purified luminal plasma membrane was 8-fold over cells and that of (Na+ + K+)-ATPase in purified bisolateral plasma membranes was 13-fold. F--activated adenyl cyclase co-purified with (Na+ + K+)-ATPase, suggesting a common localization on the plasma membrane. The distribution of K+-stimulated phosphatase and 5'-nucleotidase also followed (Na+ + K+)-ATPase during fractionation.
Adenosine Triphosphatases↗
Molecular mechanisms in proximal tubular and small intestinal phosphate reabsorption (plenary lecture).
Renal and small intestinal (re-)absorption contribute to overall phosphate(Pi)-homeostasis. In both epithelia, apical sodium (Na+)/Pi-cotransport across the luminal (brush border) membrane is rate limiting and the target for physiological/pathophysiological alterations. Three different Na/Pi-cotransporters have been identified: (i) type I cotransporter(s)--present in the proximal tubule--also show anion channel function and may play a role in secretion of organic anions; in the brain, it may serve vesicular glutamate uptake functions; (ii) type II cotransporter(s) seem to serve rather specific epithelial functions; in the renal proximal tubule (type Ila) and in the small intestine (type IIb), isoform determines Na+-dependent transcellular Pi-movements; (iii) type III cotransporters are expressed in many different cells/tissues where they could serve housekeeping functions. In the small intestine, alterations in Pi-absorption and, thus, apical expression of IIb protein are mostly in response to longer term (days) situations (altered Pi-intake, levels of 1.25 (OH2) vitamin D3, growth, etc), whereas in renal proximal tubule, in addition, hormonal effects (e.g. Parathyroid Hormone, PTH) acutely control (minutes/hours) the expression of the IIa cotransporter. The type II Na/Pi-cotransporters operate (as functional monomers) in a 3 Na+:1 Pi stoichiometry, including transfer of negatively charged (-1) empty carriers and electroneutral transfers of partially loaded carriers (1 Na+, slippage) and of the fully loaded carriers (3 Na+, 1 Pi). By a chimera (IIa/IIb) approach, and by site-directed mutagenesis (including cysteine-scanning), specific sequences have been identified contributing to either apical expression, PTH-induced membrane retrieval, Na+-interaction or specific pH-dependence of the IIa and IIIb cotransporters. For the COOH-terminal tail of the IIa Na/Pi-cotransporter, several interacting PDZ-domain proteins have been identified which may contribute to either its apical expression (NaPi-Cap1) or to its subapical/lysosomal traffic (NaPi-Cap2).
Absorption↗
Molecular characteristics of phosphate transporters and their regulation.
A key process in overall P(i)-homeostasis is renal proximal tubular reabsorption of inorganic phosphate (P(i)), which involves secondary active sodium/phosphate (Na(+)/P(i)) cotransport reabsorption at the brush border membrane. Among the two different molecularly identified Na(+)/P(i) cotransporters, the type-IIa Na(+)/P(i) cotransporter (NaPi-IIa) accounts for up to 70% of brush border membrane transport. Regulation of renal P(i) reabsorption centers around brush border membrane insertion and retrieval of transporter protein under the influence of hormonal and nonhormonal factors. Immunohistochemical and fluorescence techniques have provided new insights into the tissue distribution and the regulation processes. The intrinsic electrogenicity of NaPi-IIa, has allowed detailed studies of the transport kinetics of NaPi-IIa and, combined with mutagenesis methods, structure-function information at the protein level is emerging.
Amino Acid Sequence↗
Towards a molecular view of renal proximal tubular reabsorption of phosphate.
Apical sodium-dependent transport of inorganic phosphate (Pi) in the proximal tubule plays a crucial role in renal Pi reabsorption and consequently in the maintenance of Pi homeostasis. This transport system represents a main target for acute and long-term regulation such as by parathyroid hormone, by growth factors and dietary intake of phosphate. In this short review we briefly describe the currently established cellular mechanism of proximal tubular Pi reabsorption and its regulation via the apical Na/Pi cotransport system. In a second part we will outline recent progress made with respect to the molecular cloning of renal Na/Pi cotransport systems. Knowledge about the molecular identity of these transport systems will make it possible to resolve yet unanswered questions about the molecular mechanisms involved in the physiology of the regulation of renal Pi reabsorption.
Absorption↗
Characteristics and regulation of Na/Pi cotransport in a SV-40-transformed rabbit proximal tubular cell line.
An SV-40-transformed cell line of rabbit S2 proximal tubular origin (RKPC-2 cells) was used to characterize Na/P(i) cotransport. P(i) saturation experiments showed simple Michaelis-Menten behaviour and an apparent Km of 106 microM; Hill analysis of Na+ concentration dependence results in an apparent Km for Na+ of about 130 mM and suggests a stoichiometry exceeding unity. Exposure of confluent monolayers to low P(i) medium induced an increase in Na/P(i) cotransport. Incubation with 10(-9) M parathyroid hormone produced a 'paradoxical' stimulation of Na/P(i) cotransport, mimicked by pharmacological activation of protein kinase A or protein kinase C. The above regulatory events, observed on Na/P(i) cotransport, were not observed for Na(+)-dependent amino acid transport (L-proline and/or L-glutamic acid).
Animals↗
A molecular view of renal Na-dependent phosphate transport.
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Animals↗
Control of proximal tubular apical Na/Pi cotransport.
Two renal proximal tubular apical sodium-dependent transport systems for phosphate (Na/Pi cotransporter) have been identified. Recent studies demonstrated that the abundance of the type II Na/Pi cotransporter in the brush border is critical for the capacity of phosphate reabsorption. Evidence was obtained that a change of apical Na/Pi cotransporters may occur via endo/ exocytic processes and via protein-synthesis-dependent mechanisms involving altered transcription and/or stability of mRNA. In addition, acute control of apical Na/Pi cotransport may occur via the pH dependence and electrogenicity of the Na/Pi cotransporter.
Animals↗