Purification and partial sequencing of inhibitory factor on renal membrane adenylate cyclase in pancreatic cancer extract: identity with histones H1b or H1d

Biochem Biophys Res Commun. 1991 Apr 15;176(1):255-61. doi: 10.1016/0006-291x(91)90917-v.

Abstract

Inhibitory activity on renal membrane adenylate cyclase (AC) has previously been found in the extract of a pancreatic cancer associated with humoral hypercalcemia of malignancy (HHM). AC inhibitor was purified employing inhibition of AC activity of renal membrane stimulated by forskolin as its index. N-terminal 9 residues and a digested fragment of purified protein (14 residues) were completely consistent with that of histones H1b and H1d. Not only histone H1 but also histones H2A, H2B and H3 from calf thymus inhibited AC activity. These results indicate that the AC inhibitor in the pancreatic cancer extract is histone H1b or H1d and histones H2A, H2B and H3 also have an AC inhibitory activity.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenylyl Cyclases / isolation & purification*
  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Cell Membrane / enzymology
  • Dogs
  • Histones / genetics
  • Histones / isolation & purification
  • Histones / pharmacology*
  • Humans
  • Hypercalcemia / etiology
  • Hypercalcemia / physiopathology
  • Kidney Cortex / enzymology*
  • Molecular Sequence Data
  • Molecular Weight
  • Pancreatic Neoplasms / chemistry
  • Pancreatic Neoplasms / physiopathology*
  • Sequence Homology, Nucleic Acid

Substances

  • Histones
  • Adenylyl Cyclases