ArticleMolecular and cellular biochemistry1990
Cardiac alpha-crystallin. III. Involvement during heart ischemia.
Article in Molecular and cellular biochemistry, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 78 citations in OpenAlex.
- The role of αB-crystallin in skeletal and cardiac muscle tissues.Cell stress & chaperones · 2018Review
- O-GlcNAcylation of αB-crystallin regulates its stress-induced translocation and cytoprotection.Molecular and cellular biochemistry · 2013Article
- Phosphorylation-dependent subcellular localization of the small heat shock proteins HspB1/Hsp25 and HspB5/αB-crystallin in cultured hippocampal neurons.Histochemistry and cell biology · 2012Article
- p38 MAPK-dependent small HSP27 and αB-crystallin phosphorylation in regulation of myocardial function following cardioplegic arrest.American journal of physiology. Heart and circulatory physiology · 2011Article
- The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: a light and X-ray scattering investigation.Molecular vision · 2010Article
- Trimethylamine N-oxide alleviates the severe aggregation and ER stress caused by G98R alphaA-crystallin.Molecular vision · 2009Article
- Kinetics of the translocation and phosphorylation of alphaB-crystallin in mouse heart mitochondria during ex vivo ischemia.American journal of physiology. Heart and circulatory physiology · 2009Article
- Ischemia-induced increase of stiffness of alphaB-crystallin/HSPB2-deficient myocardium.Pflugers Archiv : European journal of physiology · 2006Article
- A pilot proteomic study of amyloid precursor interactors in Alzheimer's disease.Annals of neurology · 2005Article
- Comparison of the small heat shock proteins alphaB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle.Histochemistry and cell biology · 2004Article
- Targeted disruption of the mouse alpha A-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein alpha B-crystallin.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Modulation of the chaperone-like activity of bovine alpha-crystallin.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Self-similarity properties of alpha-crystallin supramolecular aggregates.Biophysical journal · 1995Article
- Kinetic changes of alpha B crystallin expression in neoplastic cells and syngeneic rat fibroblasts at various subculture stages.Molecular and cellular biochemistry · 1995Article
- Sense and antisense modification of glial alpha B-crystallin production results in alterations of stress fiber formation and thermoresistance.The Journal of cell biology · 1994Article
- Overexpression and abnormal modification of the stress proteins alpha B-crystallin and HSP27 in Alexander disease.The American journal of pathology · 1993Article
- Alpha B-crystallin and 27-kd heat shock protein are regulated by stress conditions in the central nervous system and accumulate in Rosenthal fibers.The American journal of pathology · 1993Article
- Determination of alpha B crystallin aggregation: a new alternative method to assess ischemic damage of the heart.Basic research in cardiologyArticle
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rat hearts were perfused in the working heart or Langendorff mode and then subjected to total normothermic ischemia. The content of alpha-crystallin in the water soluble protein fraction obtained from these hearts diminished in a time-dependent manner during ischemia. The protein was recovered in the low g pellet of the homogenate. The redistribution was dramatic, selective for alpha-crystallin and irreversible. Large crystallin clumps formed also when exposing the soluble protein fraction of control hearts to slightly acidic pH (6.5-7.0). Electron microscopic analysis showed that aggregation of the globular homo-oligomeric units of crystallin occurred. The aggregates probably represented denatured protein and were similar in appearance to lenticular alpha H-crystallin. In purified form, however, cardiac crystallin particles did not cluster at pH 6.5. Aggregation only occurred in the presence of other protein components (including, probably, cytosolic actin) of the soluble fraction. A direct and selective interaction between actin and cardiac crystallin could be demonstrated using actin-Sepharose affinity chromatography procedures. The results suggest that large aggregates of cardiac crystallin form very early during ischemia, due to acidification of the cytosol. Cardiac crystallin is highly homologous to stress proteins and is localized on the Z-disks, where it plays probably a structural or protective role. Its rapid and complete denaturation could be involved in the genesis of the irreversible structural damages occurring during ischemia.
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