A structure-activity analysis of the cloned rat and human Y4 receptors for pancreatic polypeptide

Peptides. 1997;18(4):609-12. doi: 10.1016/s0196-9781(97)00070-3.

Abstract

We cloned and expressed the rat Y4 receptor for pancreatic polypeptide (PP). Structure-activity profiles derived from 125I-PP binding assays and [cAMP] radioimmunoassays reveal a selective receptor interaction with rat PP vs. neuropeptide Y (NPY) or peptide YY (PYY). Rat and human Y4 receptor clones share 75% amino acid identity. Based on [cAMP] radioimmunoassay, the human Y4 receptor exhibits a less selective interaction with rat PP vs. NPY or PYY and a greater dependence on N-terminal PP residues, relative to rat Y4. Differences in sequence and structure-activity profiles suggest the rat be used with caution to model human Y4 receptor function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cloning, Molecular
  • Humans
  • In Vitro Techniques
  • Molecular Sequence Data
  • Pancreatic Polypeptide*
  • Radioligand Assay
  • Rats
  • Receptors, Gastrointestinal Hormone / chemistry
  • Receptors, Gastrointestinal Hormone / isolation & purification*
  • Receptors, Gastrointestinal Hormone / metabolism
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship

Substances

  • Receptors, Gastrointestinal Hormone
  • receptors, pancreatic polypeptide-specific
  • Pancreatic Polypeptide

Associated data

  • GENBANK/U84245