Although the small (22 Kd) heat shock protein/αB-crystallin functions as a major structural protein and molecular chaperone in the vertebrate lens, little is known about the protein's role in nonlenticular tissues such as the heart and skeletal muscle. Recent studies have demonstrated that αB- crystallin expression is uniquely regulated during myogenesis in vitro. We report here for the first time that the temporal and spatial expression of αB-crystallin is similarly regulated in vivo during mouse embryogenesis. Expression of αB-crystallin mRNA was detected by in situ hybridization in the primitive heart at 8.5 days postconception (p.c.) and in the myotome of the somites at 10.5 days p.c. This tissue-restricted pattern was corroborated by immunohistochemical studies. αB-crystallin mRNA and protein expression were uniform in the developing atria and ventricles without regional differences or gradients. αB-crystallin expression was absent in the endocardial cushion, pulmonary trunk, aorta, and endothelium. Examination of muscle precursors revealed expression throughout the dorsoventral aspect of the myotomes and in developing skeletal muscle. Our findings suggest that αB-crystallin may serve pivotal roles as a structural protein and a molecular chaperone in myofiber stabilization of metabolically active tissues during early embryogenesis. Thus, early αB-crystallin expression in myogenic lineages supports the hypothesis that the putative functions of αB- crystallin are coupled to the activation of genetic programs responsible for myogenic differentiation and cardiac morphogenesis.
|Original language||English (US)|
|Number of pages||10|
|State||Published - Jan 1997|
- in situ hybridization
- skeletal muscle