ArticleProceedings of the National Academy of Sciences of the United States of America1994
Calpain (Ca(2+)-dependent thiol protease) in erythrocytes of young and old individuals.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 55 citations in OpenAlex.
- Impact of the production method on the properties of erythrocyte-derived extracellular particles: a quantitative and qualitative evaluation.Nanotheranostics · 2025Article
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- The aging lysosome: An essential catalyst for late-onset neurodegenerative diseases.Biochimica et biophysica acta. Proteins and proteomics · 2020Review
- Membrane Aging as the Real Culprit of Alzheimer's Disease: Modification of a Hypothesis.Neuroscience bulletin · 2018Review
- Erythrocyte Aging, Protection via Vesiculation: An Analysis Methodology via Oscillatory Flow.Frontiers in physiology · 2018Article
- Membrane Repair: Mechanisms and Pathophysiology.Physiological reviews · 2015Review
- Identification of signalling cascades involved in red blood cell shrinkage and vesiculation.Bioscience reports · 2015Article
- N-ethylmaleimide activates a Cl(-)-independent component of K(+) flux in mouse erythrocytes.Blood cells, molecules & diseases · 2013Article
- Calcium in red blood cells-a perilous balance.International journal of molecular sciences · 2013Review
- Article
- Direct effect of human immunodeficiency virus protease inhibitors on neutrophil function and apoptosis via calpain inhibition.Clinical and vaccine immunology : CVI · 2007Article
- Alterations in band 3 protein and anion exchange in red blood cells of renal failure patients.Molecular and cellular biochemistry · 2005Article
- Ca2+ promotes erythrocyte band 3 tyrosine phosphorylation via dissociation of phosphotyrosine phosphatase from band 3.The Biochemical journal · 2002Article
- The pathogenic activation of calpain: a marker and mediator of cellular toxicity and disease states.International journal of experimental pathology · 2000Review
- Cytoplasmic calcium buffers in intact human red cells.The Journal of physiology · 1997Article
- Calpastatin in erythrocytes of young and old individuals.The Biochemical journal · 1994Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Limited proteolysis by calpain (Ca(2+)-activated protease; EC 3.4.22.17) is believed to regulate the function of membrane enzymes and modify the behavior of membrane structural proteins. Calpain is activated by autolysis. The degradation of band 3 protein by mu-calpain is known to be enhanced in erythrocyte membranes from human individuals > 70 years old (old) as compared with that from individuals 20-30 years old (young). In the present study, monoclonal antibody to mu-calpain was used to study the behavior of calpain in erythrocytes of young and old individuals. Less calpain was found in erythrocyte cytosol and membranes from old than in those from young. Increasing the erythrocyte Ca2+ induced translocation of calpain to the cell membrane and autolysis of the enzyme. Alkylation of erythrocyte thiols also promoted translocation of calpain to the membrane, especially in the presence of Ca2+. When calpain was added to erythrocyte membranes, initial binding was greater and subsequent autolysis faster in old than in young individuals, possibly arising from alterations in cell membranes of old individuals. The enhanced calpain autolysis was accompanied by enhanced degradation of band 3 protein in the old. The results suggest that calpain in old individuals is translocated to the cell membrane and is activated by autolysis, resulting in degradation of certain membrane proteins and loss of calpain. Enhanced calpain-induced membrane proteolysis may play a role in abnormal cell destruction (e.g., shortening the life span of erythrocytes in the aged, neuronal degeneration, etc). The erythrocyte membrane provides a convenient model for the study of age-associated alterations in cell membranes and in calpain behavior.
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