Alterations of red blood cell proteolysis in favism.

Abstract

Damaged RBC drawn from favic patients during acute hemolysis showed marked alterations in their two major proteolytic systems. Cytosolic procalpain (i.e., the proenzyme species of Ca2+-activated neutral proteinase, or calpain) had considerably lower activity than in matched RBC from asymptomatic G6PD-deficient subjects. The total RBC activity of the three acid endopeptidases that are normally membrane-bound was not reduced in favism, but its subcellular distribution was mostly cytosolic, suggesting quantitative release from membranes. Changes in procalpain activity are the result of both autoxidation of divicine and of the intracellular elevation of Ca2+ that is found in favism. Changes in acid endopeptidase activity are the consequence of perturbed Ca2+ homeostasis. Overall, the picture shows a marked impairment of the RBC proteolytic machinery that in turn may worsen cellular damage.

• Authors: A De Flora, A Morelli, M Grasso, G Forteleoni, T Meloni
• Journal: Biomedica biochimica acta (Biomed Biochim Acta) Vol. 46 Issue 2-3 Pg. S184-9 ( 1987) ISSN: 0232-766X [Print] Germany
• PMID: 3036108 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Enzyme Precursors
• Pyrimidinones
• divicine
• Endopeptidases
• Peptide Hydrolases
• Calpain
• procalpain
• Calcium

Topics

• Calcium (blood)
• Calpain (blood)
• Endopeptidases (blood)
• Enzyme Precursors (blood)
• Erythrocytes (metabolism)
• Favism (blood, enzymology)
• Glucosephosphate Dehydrogenase Deficiency (enzymology)
• Hemolysis
• Humans
• Male
• Peptide Hydrolases (blood)
• Pyrimidinones (blood)