(Circulation. 1997;96:3466-3476.)
© 1997 American Heart Association, Inc.
Articles |
Abundance and Location of the Small Heat Shock Proteins HSP25 and 
B-Crystallin in Rat and Human Heart
From the Max Delbrück Center for Molecular Medicine, Berlin, Germany (G.L., R.V., M.W., J.S., R.B.); the Clinic of Internal Medicine, Charité, Humboldt University Berlin, Germany (U.O., I.S.); the Department of Pathology, Philips University Marburg, Germany (H.-J.G.); and the Division of Cancer Research, Department of Pathology, University of Zürich (Switzerland) Medical School (R.K.).
Correspondence to Dr Gudrun Lutsch, Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Str 10, D-13122 Berlin, Germany. E-mail lutsch{at}mdc-berlin.de
Background In the heart, there are high constitutive
levels of the two related small heat shock proteins, HSP25 and
B-crystallin. To gain insight into their functional role, we have
analyzed abundance and location of both proteins in rat and
human hearts at different stages of development and in diseased
state.
Methods and Results Immunoblotting
analysis of rat ventricular tissue at fetal,
neonatal, and adult stages reveals the level of HSP25 to decline
strongly during development, whereas the level of B-crystallin
remains nearly constant. In parallel, the portion of
phosphorylated isoforms of HSP25 decreases as shown by
two-dimensional polyacrylamide gel electrophoresis. HSP25 is
detected in cardiomyocytes and endothelial
and vascular smooth muscle cells, whereas B-crystallin is detected
in cardiomyocytes only by
immunofluorescence and immunoelectron microscopy.
Both proteins colocalize in the I-band and M-line region of myofibrils
in cardiomyocytes. In diseased and transplanted adult human
hearts, HSP25 and B-crystallin levels are considerably elevated
compared with fetal hearts. In failing adult human hearts,
phosphorylated isoforms of HSP25 predominate, and
cardiomyocytes with a partial dislocation of HSP25 and
B-crystallin are observed.
Conclusions Differential accumulation and location of HSP25
and B-crystallin in heart tissue during development imply distinct
functions of both proteins, which seem to be involved in organization
of cytoskeletal structures. As judged by level,
phosphorylation state, and location of both small heat
shock proteins, diseased adult human hearts share features with fetal
hearts.
Key Words: ventricles • immunohistochemistry • heart failure • proteins
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