Peptide YY receptors in the proximal tubule PKSV-PCT cell line derived from transgenic mice. Relation with cell growth

J Biol Chem. 1993 Sep 25;268(27):20547-54.

Abstract

Receptors for peptide YY (PYY) were identified in the PKSV-PCT renal proximal tubule cell line, derived from transgenic mice (SV40 large T antigen under the control of the rat L-type pyruvate kinase 5'-regulatory sequence). Binding of [125I-Tyr36]monoiodo-PYY ([125I] PYY to cell was specific, saturable, and reversible. The order of potency for peptides for inhibiting [125I]PYY binding was: PYY > neuropeptide Y (NPY) = PYY (13-36) >> pancreatic polypeptide. A single class of receptors was observed with a Kd of 0.37 +/- 0.05 nM and a Bmax of 103 +/- 10 fmol/mg protein. After cross-linking, electrophoresis of covalent [125I]PYY-receptor complexes revealed a single band of M(r) 50,000. PYY receptors were exclusively present at the basolateral membrane surface of polarized cells and were coupled negatively to adenylylcyclase by a pertussis toxin-sensitive G protein. PKSV-PCT cell growth and T antigen expression could be modulated by D-glucose in the medium. PYY receptors were exclusively expressed in proliferative cells cultured in the presence of D-glucose. PYY receptors disappeared in the absence of D-glucose and were expressed again when proliferation was activated by reintroduction of D-glucose. PYY stimulated cell growth (17-26% increase) and promoted [methyl-3H]thymidine incorporation into DNA (64% increase; ED50 = 5 nM PYY) of cells grown in D-glucose-enriched medium. This latter effect of PYY was largely reversed by pretreatment of cells with pertussis toxin. These findings suggest that PYY receptors play a role in epithelial cell growth.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenylyl Cyclases / metabolism
  • Animals
  • Antigens, Polyomavirus Transforming / genetics
  • Blotting, Western
  • Cell Division / drug effects
  • Cell Line
  • Cell Membrane / metabolism
  • Cell Membrane / ultrastructure
  • Colforsin / pharmacology
  • Cyclic AMP / metabolism
  • DNA / biosynthesis
  • GTP-Binding Proteins / isolation & purification
  • GTP-Binding Proteins / metabolism
  • Gastrointestinal Hormones / metabolism
  • Gene Expression
  • Glucose / pharmacology
  • Kidney Tubules, Proximal / cytology
  • Kidney Tubules, Proximal / metabolism*
  • Kinetics
  • Mice
  • Mice, Transgenic
  • Molecular Weight
  • Peptide YY
  • Peptides / isolation & purification
  • Peptides / metabolism
  • Peptides / pharmacology*
  • Pyruvate Kinase / genetics
  • Rats
  • Receptors, Cell Surface / genetics
  • Receptors, Cell Surface / isolation & purification
  • Receptors, Cell Surface / metabolism
  • Receptors, Gastrointestinal Hormone*
  • Regulatory Sequences, Nucleic Acid
  • Simian virus 40 / genetics
  • Thymidine / metabolism

Substances

  • Antigens, Polyomavirus Transforming
  • Gastrointestinal Hormones
  • Peptides
  • Receptors, Cell Surface
  • Receptors, Gastrointestinal Hormone
  • peptide YY receptor
  • Peptide YY
  • Colforsin
  • DNA
  • Cyclic AMP
  • Pyruvate Kinase
  • GTP-Binding Proteins
  • Adenylyl Cyclases
  • Glucose
  • Thymidine