Calcium-activated neutral protease and its endogenous inhibitor in tissues of dystrophic and normal mice

Biochem Med Metab Biol. 1987 Jun;37(3):282-6. doi: 10.1016/0885-4505(87)90038-7.

Abstract

Calcium-activated neutral protease (milli-CANP) and its endogenous inhibitor are elevated in muscle tissues, primarily the skeletal muscle and heart, of dystrophic mice (C57BL/6J dy/dy) as compared to the control strain (C57BL/10J). Tissues showing relative increase of CANP also show significant loss of enzymes such as CK, LDH in comparison to plasma, where these enzymes register a significant increase. PK is lost minimally from these tissues, probably showing a "sparing effect." Absence of any significant change in CANP activity in the liver points to a specific role of CANP in the dystrophic process. In the skeletal muscle the endogenous CANP inhibitor registers a concomitant increase with CANP without altering the enzyme/inhibitor ratio.

Publication types

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

MeSH terms

  • Animals
  • Calpain / antagonists & inhibitors
  • Calpain / metabolism*
  • Creatine Kinase / metabolism
  • Glycoproteins / metabolism*
  • L-Lactate Dehydrogenase / metabolism
  • Mice
  • Mice, Inbred C57BL
  • Mice, Mutant Strains
  • Muscles / enzymology*
  • Muscular Dystrophy, Animal / enzymology*
  • Myocardium / enzymology
  • Organ Specificity
  • Pyruvate Kinase / metabolism
  • Reference Values

Substances

  • Glycoproteins
  • calpain inhibitors
  • L-Lactate Dehydrogenase
  • Pyruvate Kinase
  • Creatine Kinase
  • Calpain