A putative membrane protein, Pho88p, involved in inorganic phosphate transport inSaccharomyces cerevisiae

1996 ◽  
Vol 251 (5) ◽  
pp. 580-590 ◽  
Author(s):  
C. Yompakdee ◽  
N. Ogawa ◽  
S. Harashima ◽  
Y. Oshima
Keyword(s):  
Membrane Protein ◽  
Inorganic Phosphate ◽  
Phosphate Transport ◽  
Putative Membrane Protein

A putative membrane protein, Pho88p, involved in inorganic phosphate transport in

1996 ◽  
Vol 251 (5) ◽  
pp. 580 ◽  
Author(s):  
Chulee Yompakdee ◽  
Nobuo Ogawa ◽  
Satoshi Harashima ◽  
Y. Oshima
Keyword(s):  
Membrane Protein ◽  
Inorganic Phosphate ◽  
Phosphate Transport ◽  
Putative Membrane Protein

Sodium, potassium, and intestinal transport of glucose, l-tyrosine, phosphate, and calcium

1963 ◽  
Vol 205 (1) ◽  
pp. 107-111 ◽  
Author(s):  
Harold E. Harrison ◽  
Helen C. Harrison
Keyword(s):  
Small Intestine ◽  
Calcium Transport ◽  
Inorganic Phosphate ◽  
Choline Chloride ◽  
Sodium Concentration ◽  
Phosphate Transport ◽  
Metabolic Energy ◽  
Transport Systems ◽  
Bicarbonate Buffer ◽  
Distal Small Intestine

Everted loops of rat small intestine were incubated in media varying in their concentrations of sodium and potassium. Reduction of sodium concentration was effected by substitution of choline chloride in equimolar amounts for sodium chloride in the saline-bicarbonate buffer. Concentrative transport of glucose, l-tyrosine, inorganic phosphate, and calcium was measured by determination of the final ratio of the concentrations of the solute in serosal and mucosal fluids, and the increment of the solute in serosal fluid during incubation. Ca45 was used as an indicator of calcium distribution. The glucose, l-tyrosine, and inorganic phosphate transport systems require sodium, and at a submaximal concentration of sodium an increased concentration of potassium is inhibitory. The calcium transport system does not require sodium and in loops from the distal small intestine calcium transport is enhanced by reduction of sodium concentration in the medium. It is postulated that there is a common sodium-requiring system which is necessary for the linkage of metabolic energy to glucose, amino acid, and inorganic phosphate transport.

HOMEOSTATIC ADJUSTMENT IN THE RENAL TUBULAR TRANSPORT OF INORGANIC PHOSPHATE IN THE DOG

1955 ◽  
Vol 33 (1) ◽  
pp. 638-650 ◽  
Author(s):  
James G. Foulks
Keyword(s):  
Inorganic Phosphate ◽  
Renal Tubule ◽  
Phosphate Transport ◽  
Sodium Sulphate ◽  
Tubular Transport ◽  
Renal Tubular Transport ◽  
Transport Of Inorganic Phosphate ◽  
Renal Tubular ◽  
Filtered Load

By means of the infusion of small amounts of sodium sulphate it has been possible to elevate the filtered load of inorganic phosphate to the renal tubule in fasted dogs without the administration of exogenous phosphate. Under these circumstances, the reabsorption of phosphate remains virtually complete, even when filtered loads are reached which result in a substantial phosphaturia when phosphate has been administered. By comparing phosphate reabsorption and excretion in fasted animals, and in animals at various intervals after feeding, the existence of homeostatic adjustments in the renal tubular transport of inorganic phosphate has been demonstrated. The available evidence suggests that the intracellular disposition of phosphate itself may be an important factor in determining the rate of renal tubular phosphate transport at filtered loads in the physiological range. The limitations of the determination of the phosphate "Tm" as a device for studying homeostatic processes have been discussed.

Characterization of a Gene Coamplified with Ki-ras in Y1 Murine Adrenal Carcinoma Cells That Codes for a Putative Membrane Protein

Genomics ◽  
1994 ◽  
Vol 20 (2) ◽  
pp. 227-230 ◽  
Author(s):  
Alan F. Scott ◽  
Andrew Elizaga ◽  
James Morrell ◽  
Andrew Bergen ◽  
Margaret B. Penno
Keyword(s):  
Membrane Protein ◽  
Carcinoma Cells ◽  
Adrenal Carcinoma ◽  
Putative Membrane Protein

Does Availability of Inorganic Phosphate Regulate Cellular Oxidative Metabolism?

Physiology ◽  
1986 ◽  
Vol 1 (3) ◽  
pp. 100-103 ◽  
Author(s):  
PC Brazy ◽  
LJ Mandel
Keyword(s):  
Solute Transport ◽  
Oxidative Metabolism ◽  
Inorganic Phosphate ◽  
Phosphate Transport ◽  
Renal Tubules ◽  
Metabolic Processes

Cells require inorganic phosphate for formation of ATP and a variety of other metabolic and transport functions. Studies of renal tubules indicate that availability of phosphate does regulate rates of oxidative metabolism and solute transport, that intracellular metabolic processes compete for inorganic phosphate, and that transepithelial phosphate transport provides inorganic phosphate for use within the cell.

HOMEOSTATIC ADJUSTMENT IN THE RENAL TUBULAR TRANSPORT OF INORGANIC PHOSPHATE IN THE DOG

1955 ◽  
Vol 33 (4) ◽  
pp. 638-650 ◽  
Author(s):  
James G. Foulks
Keyword(s):  
Inorganic Phosphate ◽  
Renal Tubule ◽  
Phosphate Transport ◽  
Sodium Sulphate ◽  
Tubular Transport ◽  
Renal Tubular Transport ◽  
Transport Of Inorganic Phosphate ◽  
Renal Tubular ◽  
Filtered Load

By means of the infusion of small amounts of sodium sulphate it has been possible to elevate the filtered load of inorganic phosphate to the renal tubule in fasted dogs without the administration of exogenous phosphate. Under these circumstances, the reabsorption of phosphate remains virtually complete, even when filtered loads are reached which result in a substantial phosphaturia when phosphate has been administered. By comparing phosphate reabsorption and excretion in fasted animals, and in animals at various intervals after feeding, the existence of homeostatic adjustments in the renal tubular transport of inorganic phosphate has been demonstrated. The available evidence suggests that the intracellular disposition of phosphate itself may be an important factor in determining the rate of renal tubular phosphate transport at filtered loads in the physiological range. The limitations of the determination of the phosphate "Tm" as a device for studying homeostatic processes have been discussed.

Comparison between Ca2+-induced scrambling of various fluorescently labelled lipid analogues in red blood cells

2002 ◽  
Vol 362 (3) ◽  
pp. 741-747 ◽  
Author(s):  
David W. C. DEKKERS ◽  
Paul COMFURIUS ◽  
Edouard M. BEVERS ◽  
Robert F. A. ZWAAL
Keyword(s):  
Plasma Membrane ◽  
Membrane Protein ◽  
Red Blood Cells ◽  
Phospholipase D ◽  
Blood Cells ◽  
Amino Group ◽  
Flip Flop ◽  
Putative Membrane Protein ◽  
Kinetics Of

Treatment of red blood cells with calcium and ionomycin causes activation of the lipid scramblase, a putative membrane protein catalysing flip-flop of (phospho)lipids. Various fluorescent 1-oleoyl-2-[6(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino] caproyl (C6-NBD) analogues were tested for transbilayer movement across the plasma membrane of red blood cells. Among these phospholipid analogues were phosphatidylgalactose, phosphatidylmaltose and phosphatidylmaltotriose, which were obtained from C6-NBD-phosphatidylcholine by phospholipase D-catalysed transphosphatidylation. The inward movement after the onset of scrambling was monitored by extraction of the non-internalized probe with BSA. We demonstrate that both the amino group and the size of the headgroup determine the kinetics of lipid scrambling, and that lipids with a ceramide backbone migrate much more slowly than glycerophospholipids with the same headgroup.

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