GCAP-II: isolation and characterization of the circulating form of human uroguanylin

FEBS Lett. 1995 Oct 23;374(1):34-8. doi: 10.1016/0014-5793(95)01075-p.

Abstract

The systematic isolation of circulating regulatory peptides which generate cGMP as second messenger resulted in the identification of a novel member of the guanylin family. In the present study we describe the purification and amino acid sequence of a new guanylate cyclase C activating peptide (GCAP-II). GCAP-II contains 24 amino acids in the following sequence: FKTLRTIANDDCELCVNVACTGCL. Its molecular mass is 2597.7 Da. The 16 C-terminal amino acids are identical to uroguanylin from human urine. native and synthetic GCAP-II activate GC-C, the specific guanylate cyclase receptor, of cultured human colon carcinoma (T84) cells. GCAP-II stimulates chloride secretion in isolated human intestinal mucosa mediated by intracellular cGMP increase. GCAP-II specific antibodies were used to localize the peptide by immunohistochemistry in entero-endocrine cells of the colonic mucosa.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Calcium-Binding Proteins / blood
  • Calcium-Binding Proteins / chemistry
  • Calcium-Binding Proteins / isolation & purification*
  • Calcium-Binding Proteins / physiology
  • Cyclic GMP / metabolism
  • Guanylate Cyclase-Activating Proteins
  • Humans
  • Molecular Sequence Data
  • Natriuretic Peptides
  • Peptides / chemistry
  • Sequence Homology, Amino Acid
  • Tumor Cells, Cultured

Substances

  • Calcium-Binding Proteins
  • GUCA1B protein, human
  • Guanylate Cyclase-Activating Proteins
  • Natriuretic Peptides
  • Peptides
  • uroguanylin
  • Cyclic GMP