Cholera toxin can ADP-ribosylate Gs as well as Gi in ACTH-unresponsive human adrenocortical cancer

Endocr J. 1994 Oct;41(5):593-7. doi: 10.1507/endocrj.41.593.

Abstract

It is well known that cholera toxin (CT) stimulates ADP-ribosylation of Gs and also pertussis toxin (PT) does Gi. Each GTP-binding protein has its own action in the regulation of adenylate cyclase. A human non-functioning adrenocortical cancer tissue showed an unresponsiveness in adenylate cyclase to ACTH although ACTH and CT activated adenylate cyclase in a non-functioning adrenal adenoma tissue. CT ADP-ribosylated 43 kDa protein of the plasma membrane of the cancer tissue while CT and PT could ADP-ribosylate 43 kDa and 38 kDa protein in the adenoma tissue, respectively. Immunoblotting analysis of the cancer tissue demonstrated that 40 kDa protein was detected by anti-Gs antibody as well as by anti-Gi antibody. The present experiments demonstrated that CT could ADP-ribosylate Gs which has stimulatory action on adenylate cyclase and also Gi which inhibits adenylate cyclase. Thus it is suggested that CT can activate the ADP-ribosylation of Gs and also Gi in a human adrenocortical cancer tissue, partly resulting in abnormal regulation of adenylate cyclase which may be crossly related to ACTH-unresponsiveness.

MeSH terms

  • Adenoma / metabolism*
  • Adenosine Diphosphate Ribose / metabolism*
  • Adenylate Cyclase Toxin
  • Adenylyl Cyclases / metabolism
  • Adrenal Cortex Neoplasms / metabolism*
  • Adrenocorticotropic Hormone / pharmacology
  • Cholera Toxin / pharmacology*
  • Female
  • GTP-Binding Proteins / metabolism*
  • Humans
  • Male
  • Middle Aged
  • Pertussis Toxin
  • Tumor Cells, Cultured
  • Virulence Factors, Bordetella / pharmacology

Substances

  • Adenylate Cyclase Toxin
  • Virulence Factors, Bordetella
  • Adenosine Diphosphate Ribose
  • Adrenocorticotropic Hormone
  • Cholera Toxin
  • Pertussis Toxin
  • GTP-Binding Proteins
  • Adenylyl Cyclases