caa a22 4500 475775104 CHVBK 20180406123629.0 cr unu---uuuuu 170329e20001101xx s 000 0 eng 10.1007/s00418-004-0711-z doi (NATIONALLICENCE)springer-10.1007/s00418-004-0711-z Comparison of the small heat shock proteins αB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle [Elektronische Daten] [Nikola Golenhofen, Ming Perng, Roy Quinlan, Detlev Drenckhahn] Seven members of the small heat shock protein (sHSP) family are exceptional with respect to their constitutive high abundance in muscle tissue. It has been suggested that sHSPs displaying chaperone-like properties may stabilize myofibrillar proteins during stress conditions and prevent them from loss of function. In the present study five sHSPs (αB-crystallin, MKBP, HSP25, HSP20, and cvHSP) were investigated with respect to similarities and differences of their expression in heart and skeletal muscle under normal and ischemic conditions. In ischemic heart and skeletal muscle these five sHSPs translocated from cytosol to the Z-/I-area of myofibrils. Myofibrillar binding of all sHSPs was very tight and resisted for the most part extraction with 1M NaSCN or 1M urea. MKBP and HSP20 became extracted by 1M NaSCN to a significant extent indicating that these two sHSPs may bind partially to actin-associated proteins which were completely extracted by this treatment. Ultrastructural localization of αB-crystallin showed diffuse distribution of immunogold label throughout the entire I-band in skeletal muscle fibers whereas in cardiomyocytes αB-crystallin was preferentially located at the N-line position of the I-band. These observations indicate different myofibrillar binding sites of αB-crystallin in cardiomyocytes versus skeletal muscle fibers. Further differences of the properties of sHSPs could be observed regarding fiber type distribution of sHSPs. Thus sHSPs form a complex stress-response system in striated muscle tissue with some common as well as some distinct functions in different muscle types. Springer-Verlag, 2004 Ischemia nationallicence Myofibrils nationallicence Stress proteins nationallicence Titin nationallicence Fiber type nationallicence Golenhofen Nikola Institute of Anatomy and Cell Biology, University of Würzburg, Koellikerstrasse6, 97070, Würzburg, Germany aut Perng Ming School of Biological and Biomedical Sciences, The University, South Road Science Site, DH13LE, Durham, UK aut Quinlan Roy School of Biological and Biomedical Sciences, The University, South Road Science Site, DH13LE, Durham, UK aut Drenckhahn Detlev Institute of Anatomy and Cell Biology, University of Würzburg, Koellikerstrasse6, 97070, Würzburg, Germany aut Histochemistry and Cell Biology Springer-Verlag 122/5(2000-11-01), 415-425 0948-6143 122:5<415 2000 122 418 https://doi.org/10.1007/s00418-004-0711-z text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00418-004-0711-z text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Golenhofen Nikola Institute of Anatomy and Cell Biology, University of Würzburg, Koellikerstrasse6, 97070, Würzburg, Germany aut NATIONALLICENCE 700 1- Perng Ming School of Biological and Biomedical Sciences, The University, South Road Science Site, DH13LE, Durham, UK aut NATIONALLICENCE 700 1- Quinlan Roy School of Biological and Biomedical Sciences, The University, South Road Science Site, DH13LE, Durham, UK aut NATIONALLICENCE 700 1- Drenckhahn Detlev Institute of Anatomy and Cell Biology, University of Würzburg, Koellikerstrasse6, 97070, Würzburg, Germany aut NATIONALLICENCE 773 0- Histochemistry and Cell Biology Springer-Verlag 122/5(2000-11-01), 415-425 0948-6143 122:5<415 2000 122 418 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer