Insulin stimulates phosphate transport in opossum kidney epithelial cells

Mohan I. Abraham, James A. McAteer, Stephen A. Kempson

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Insulin is anti phosphaturic in vivo and this effect is due, in part, to increased Na+-dependent phosphate uptake across the luminal brush-border membrane of the proximal tubule. The intracellular mechanism is not understood. The present study shows that the stimulatory effect of insulin on phosphate transport can be reproduced in opossum kidney (OK) cells, suggesting that this established renal epithelial cell line may be a good model for further studies on insulin action on renal phosphate transport. The stimulation by insulin was dose related when insulin was used at concentrations within the range of 10-14 to 10-8 M. At 10-8 M, insulin had no effect on Na+-independent uptake of phosphate or on the Na+-dependent uptakes of methyl-α-D-glucopyranoside and glutamate. The onset of insulin action on phosphate uptake was detected within 15 min, and the stimulation was reversed completely within 30 min after removal of insulin from the medium. Insulin action was not blocked by protein synthesis inhibitors and was not altered by bacitracin, an inhibitor of intracellular degradation of insulin. Pretreatment with the calcium-channel blockers, nifedipine and verapamil (10-4 M), produced significant increases in the stimulatory effect of insulin, suggesting indirectly that insulin action on phosphate uptake may be influenced by Ca2+. In contrast to in vivo studies, there was no evidence that insulin interfered with parathyroid hormone action on OK cells.

Original languageEnglish
JournalAmerican Journal of Physiology - Renal Fluid and Electrolyte Physiology
Volume258
Issue number6 27-6
StatePublished - 1990

Fingerprint

Opossums
Epithelial Cells
Phosphates
Insulin
Kidney
Bacitracin
Protein Synthesis Inhibitors
Calcium Channel Blockers
Nifedipine
Microvilli
Verapamil
Parathyroid Hormone
Glutamic Acid

Keywords

  • Actinomycin D
  • Adenosine 3′,5′-cyclic monophosphate
  • Bacitracin
  • Cycloheximide
  • Glutamic acid
  • Methyl-α-D-glucoside
  • Nifedipine
  • Parathyroid hormone
  • Verapamil

ASJC Scopus subject areas

  • Physiology

Cite this

Insulin stimulates phosphate transport in opossum kidney epithelial cells. / Abraham, Mohan I.; McAteer, James A.; Kempson, Stephen A.

In: American Journal of Physiology - Renal Fluid and Electrolyte Physiology, Vol. 258, No. 6 27-6, 1990.

Research output: Contribution to journalArticle

Abraham, Mohan I. ; McAteer, James A. ; Kempson, Stephen A. / Insulin stimulates phosphate transport in opossum kidney epithelial cells. In: American Journal of Physiology - Renal Fluid and Electrolyte Physiology. 1990 ; Vol. 258, No. 6 27-6.
@article{302bcda68d90495694f0df3239f3277a,
title = "Insulin stimulates phosphate transport in opossum kidney epithelial cells",
abstract = "Insulin is anti phosphaturic in vivo and this effect is due, in part, to increased Na+-dependent phosphate uptake across the luminal brush-border membrane of the proximal tubule. The intracellular mechanism is not understood. The present study shows that the stimulatory effect of insulin on phosphate transport can be reproduced in opossum kidney (OK) cells, suggesting that this established renal epithelial cell line may be a good model for further studies on insulin action on renal phosphate transport. The stimulation by insulin was dose related when insulin was used at concentrations within the range of 10-14 to 10-8 M. At 10-8 M, insulin had no effect on Na+-independent uptake of phosphate or on the Na+-dependent uptakes of methyl-α-D-glucopyranoside and glutamate. The onset of insulin action on phosphate uptake was detected within 15 min, and the stimulation was reversed completely within 30 min after removal of insulin from the medium. Insulin action was not blocked by protein synthesis inhibitors and was not altered by bacitracin, an inhibitor of intracellular degradation of insulin. Pretreatment with the calcium-channel blockers, nifedipine and verapamil (10-4 M), produced significant increases in the stimulatory effect of insulin, suggesting indirectly that insulin action on phosphate uptake may be influenced by Ca2+. In contrast to in vivo studies, there was no evidence that insulin interfered with parathyroid hormone action on OK cells.",
keywords = "Actinomycin D, Adenosine 3′,5′-cyclic monophosphate, Bacitracin, Cycloheximide, Glutamic acid, Methyl-α-D-glucoside, Nifedipine, Parathyroid hormone, Verapamil",
author = "Abraham, {Mohan I.} and McAteer, {James A.} and Kempson, {Stephen A.}",
year = "1990",
language = "English",
volume = "258",
journal = "American Journal of Physiology",
issn = "0193-1857",
publisher = "American Physiological Society",
number = "6 27-6",

}

TY - JOUR

T1 - Insulin stimulates phosphate transport in opossum kidney epithelial cells

AU - Abraham, Mohan I.

AU - McAteer, James A.

AU - Kempson, Stephen A.

PY - 1990

Y1 - 1990

N2 - Insulin is anti phosphaturic in vivo and this effect is due, in part, to increased Na+-dependent phosphate uptake across the luminal brush-border membrane of the proximal tubule. The intracellular mechanism is not understood. The present study shows that the stimulatory effect of insulin on phosphate transport can be reproduced in opossum kidney (OK) cells, suggesting that this established renal epithelial cell line may be a good model for further studies on insulin action on renal phosphate transport. The stimulation by insulin was dose related when insulin was used at concentrations within the range of 10-14 to 10-8 M. At 10-8 M, insulin had no effect on Na+-independent uptake of phosphate or on the Na+-dependent uptakes of methyl-α-D-glucopyranoside and glutamate. The onset of insulin action on phosphate uptake was detected within 15 min, and the stimulation was reversed completely within 30 min after removal of insulin from the medium. Insulin action was not blocked by protein synthesis inhibitors and was not altered by bacitracin, an inhibitor of intracellular degradation of insulin. Pretreatment with the calcium-channel blockers, nifedipine and verapamil (10-4 M), produced significant increases in the stimulatory effect of insulin, suggesting indirectly that insulin action on phosphate uptake may be influenced by Ca2+. In contrast to in vivo studies, there was no evidence that insulin interfered with parathyroid hormone action on OK cells.

AB - Insulin is anti phosphaturic in vivo and this effect is due, in part, to increased Na+-dependent phosphate uptake across the luminal brush-border membrane of the proximal tubule. The intracellular mechanism is not understood. The present study shows that the stimulatory effect of insulin on phosphate transport can be reproduced in opossum kidney (OK) cells, suggesting that this established renal epithelial cell line may be a good model for further studies on insulin action on renal phosphate transport. The stimulation by insulin was dose related when insulin was used at concentrations within the range of 10-14 to 10-8 M. At 10-8 M, insulin had no effect on Na+-independent uptake of phosphate or on the Na+-dependent uptakes of methyl-α-D-glucopyranoside and glutamate. The onset of insulin action on phosphate uptake was detected within 15 min, and the stimulation was reversed completely within 30 min after removal of insulin from the medium. Insulin action was not blocked by protein synthesis inhibitors and was not altered by bacitracin, an inhibitor of intracellular degradation of insulin. Pretreatment with the calcium-channel blockers, nifedipine and verapamil (10-4 M), produced significant increases in the stimulatory effect of insulin, suggesting indirectly that insulin action on phosphate uptake may be influenced by Ca2+. In contrast to in vivo studies, there was no evidence that insulin interfered with parathyroid hormone action on OK cells.

KW - Actinomycin D

KW - Adenosine 3′,5′-cyclic monophosphate

KW - Bacitracin

KW - Cycloheximide

KW - Glutamic acid

KW - Methyl-α-D-glucoside

KW - Nifedipine

KW - Parathyroid hormone

KW - Verapamil

UR - http://www.scopus.com/inward/record.url?scp=0025360366&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025360366&partnerID=8YFLogxK

M3 - Article

VL - 258

JO - American Journal of Physiology

JF - American Journal of Physiology

SN - 0193-1857

IS - 6 27-6

ER -