{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T10:22:59Z","timestamp":1790936579391,"version":"4.1.0"},"reference-count":85,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2007,7,27]],"date-time":"2007-07-27T00:00:00Z","timestamp":1185494400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Genesis"],"published-print":{"date-parts":[[2007,8]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The mammalian small heat shock protein (sHSPs) family is comprised of 10 members and includes HSPB1, which is proposed to play an essential role in cellular physiology, acting as a molecular chaperone to regulate diverse cellular processes. Whilst differential roles for sHSPs are suggested for specific tissues, the relative contribution of individual sHSP family members in cellular and organ physiology remains unclear. To address the function of HSPB1 in vivo and determine its tissue\u2010specific expression during development and in the adult, we generated knock\u2010in mice where the coding sequence of<jats:italic>hspb<\/jats:italic><jats:italic>1<\/jats:italic>is replaced by a<jats:italic>lacZ<\/jats:italic>reporter gene.<jats:italic>Hspb1<\/jats:italic>expression marks myogenic differentiation with specific expression first confined to developing cardiac muscles and the vascular system, and later in skeletal muscles with specific expression at advanced stages of myoblast differentiation. In the adult,<jats:italic>hspb1<\/jats:italic>expression was observed in other tissues, such as stratified squamous epithelium of skin, oronasal cavity, tongue, esophagus, and uterine cervix but its expression was most prominent in the musculature. Interestingly, in cardiac muscle<jats:italic>hsbp1<\/jats:italic>expression was down\u2010regulated during the neonatal period and maintained to a relatively low steady\u2010level throughout adulthood. Despite this widespread expression,<jats:italic>hspb1<\/jats:italic><jats:sup>\u2212\/\u2212<\/jats:sup>mice were viable and fertile with no apparent morphological abnormalities in tissues under physiological conditions. However, at the cellular level and under stress conditions (heat challenge), HSPB1 act synergistically with the stress\u2010induced HSPA1 (HSP70) in thermotolerance development, protecting cells from apoptosis. Our data thus indicate a nonessential role for HSPB1 in embryonic development and for maintenance of tissues under physiological conditions, but also shows that it plays an important role by acting synergistically with other HSPs during stress conditions to exert cytoprotection and anti\u2010apoptotic effects. genesis 45:487\u2013501, 2007. 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