Prostaglandin F2α and insulin stimulate phosphate uptake and (Na+, K+)ATPase activity in resting mouse fibroblast cultures

Lever, Julia E.; Clingan, Dorothie; Asúa, Luis Jiménez de

doi:10.1016/0006-291x(76)90259-x

Cited by 29 publications

(8 citation statements)

References 5 publications

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“…In 3T3 cells, prostaglandin F2a and insulin both stimulate Pi uptake (52). Prostaglandin F2a has an effect similar to that of serum in terms of both temporal and protein synthesis dependent aspects of uptake stimulation.…”

Section: Other Mitogenic Agents That Stimulate Uptakementioning

confidence: 88%

“…Prostaglandin F2a has an effect similar to that of serum in terms of both temporal and protein synthesis dependent aspects of uptake stimulation. Insulin, however, appears to be quite different from serum in both of these aspects (52). There are other agents that stimulate uptake in different types of cells.…”

Section: Other Mitogenic Agents That Stimulate Uptakementioning

confidence: 92%

“…Also, active K+ uptake decreases in 3T3 and SV4O-transformed 3T3 cells when the growth rate of both cell types decreases (85). Stimulation of DNA synthesis in 3T3 cells brings about rapid increases in K+ uptake (86) and Na+,K+-ATPase (52). All of these findings point to the importance of further investigations to determine if the changes in K+ uptake and intracellular levels of K+ are causal events in the regulation of DNA synthesis and cell division in these cases.…”

Section: Nutrients Required For Growthmentioning

confidence: 99%

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Nutrient uptake and control of animal cell proliferation

Barsh

Cunningham

1977

J Supramol Struct

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Section: Other Mitogenic Agents That Stimulate Uptakementioning

confidence: 88%

Section: Other Mitogenic Agents That Stimulate Uptakementioning

confidence: 92%

Section: Nutrients Required For Growthmentioning

confidence: 99%

See 1 more Smart Citation

Nutrient uptake and control of animal cell proliferation

Barsh

Cunningham

1977

J Supramol Struct

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“…Serum (170), as well as low doses of insulin (114,170), epidermal growth factor (170), and prostaglandins (114,170) stimulate Rb+ uptake in mouse fibroblast cells. Lelievre et al (112) were able by washing to increase ouabain sensitivity of (Na + + K +)-ATPase isolated from plasmocytoma cells grown in mice and to show that an EDT A extract able factor reversed this effect.…”

Section: Regulationmentioning

confidence: 98%

The Structure of Proteins Involved in Active Membrane Transport

Hobbs¹,

Albers²

1980

Annu. Rev. Biophys. Bioeng.

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“…1. The '"a+ pump" of nontransformed mouse fibroblast cultures is rapidly stimulated by serum (47), physiological concentrations of insulin, and prostaglandin F,, (48) which initiate cell proliferation (49), or by low, mitogenic concentrations of fibroblastic growth factor (FGF) or epidermal growth factor (EGF) (Lever JE, and Jimenez de Asua L, in preparation), by a mechanism which does not require cyclic nucleotide fluctuation or protein synthesis (48). Also, increases in Na+, KtATPase transport activity accompany viral transformation in certain cases (SO).…”

Section: Physiological Regulation Of Amino Acid Transportmentioning

confidence: 99%

Neutral amino acid transport in surface membrane vesicles isolated from mouse fibroblasts: Intrinsic and extrinsic models of regulation

Lever

1977

J Supramol Struct

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Membrane transport carrier function, its regulation and coupling t o metabolism, can be selectively investigated dissociated from metabolism and in the presence of a defined electrochemical ion gradient driving force, using the single internal compartment system provided by vesiculated surface membranes. Vesicles isolated from nontransformed and Simian virus 40-transformed mouse fibroblast cultures catalyzed carrier-mediated transport of several neutral amino acids into an osmoticallysensitive intravesicular space without detectable metabolic conversion of substrate.vesicle membranes, accumulation of several neutral amino acids achieved apparent intravesicular concentrations 6-t o 9-fold above their external concentrations. Na+-stimulated alanine transport activity accompanied plasma membrane material during subcellular fractionation procedures. Competitive interactions among several neutral amino acids for Na+-stimulated transport into vesicles and inactivation studies indicated that at least 3 separate transport systems with specificity properties previously defined for neutral amino acid transport in Ehrlich ascites cells were functional in vesicles from mouse fibroblasts: the A system, the L system and a glycine transport system. The pH profiles and apparent K m values for alanine and 2-aminoisobutyric acid transport into vesicles were those expected of components of the corresponding cellular uptake system. Several observations indicated that both a Na+ chemical concentration gradient and an electrical membrane potential contribute t o the total driving force for active amino acid transport via the A system and the glycine system. Both the initial rate and quasi-steady-state of accumulation were stimulated as a function of increasing concentrations of Na+ applied as a gradient (external > internal) across the membrane. This stimulation was independent of endogenous Na' , K+-ATPase activity in vesicles and was diminished by monensin or by preincubation of vesicles with Na+. The apparent Km for transport of alanine and 2-aminoisobutyric acid was decreased as a function of Na+ concentration. Similarly, in the presence of a standard initial Na+ gradient, quasi-steady-state alanine accumulation in vesicles increased as a function of increasing magnitudes of interior-negative membrane potential imposed across the membrane by means of Kt diffusion potentials (internal > external) in When a Na+ gradient, external Na+ > internal Na+, was artifically imposed across Abbreviations used: iso-Abu -2-aminoisobutyric acid; TPMP' -triphenylmethylphosphosphonium ion; SV 40 -Simian virus 40; FCCP -carbonyl cyanide p-trifluoromethoxyphenylhydrazone. Julia E. Lever is now at the

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Prostaglandin F2α and insulin stimulate phosphate uptake and (Na+, K+)ATPase activity in resting mouse fibroblast cultures

Cited by 29 publications

References 5 publications

Nutrient uptake and control of animal cell proliferation

Nutrient uptake and control of animal cell proliferation

The Structure of Proteins Involved in Active Membrane Transport

Neutral amino acid transport in surface membrane vesicles isolated from mouse fibroblasts: Intrinsic and extrinsic models of regulation

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