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Departments of 1 Pediatrics, 2 Physiology, and 3 Anatomy and Cell Biology, University of Michigan Medical Center, Ann Arbor, Michigan 48109
Sustained smooth muscle contraction is mediated
by protein kinase C (PKC) through a signal transduction cascade leading
to contraction. Heat-shock protein 27 (HSP27) appears to
be the link between these two major events, i.e., signal transduction
and sustained smooth muscle contraction. We have investigated the involvement of HSP27 in signal transduction and HSP27 association with
contractile proteins (e.g., actin, myosin, tropomyosin, and caldesmon)
resulting in sustained smooth muscle contraction. We have carried out
confocal microscopy to investigate the cellular reorganization and
colocalization of proteins and immunoprecipitation of HSP27 with actin,
myosin, tropomyosin, and caldesmon as detected by sequential
immunoblotting. Our results indicate that
1) translocation of Raf-1 to the
membrane when stimulated with ceramide is inhibited by vasoactive
intestinal peptide (VIP), a relaxant neuropeptide; 2) PKC-
and mitogen-activated
protein kinase translocate and colocalize on the membrane in response
to ceramide, and PKC- translocation is inhibited by VIP;
3) HSP27 colocalizes with actin when
contraction occurs; and 4) HSP27
immunoprecipitates with actin and with the contractile proteins myosin,
tropomyosin, and caldesmon. We propose a model in which HSP27 is
involved in sustained smooth muscle contraction and modulates the
interaction of actin, myosin, tropomyosin, and caldesmon.
heat-shock protein 27; protein kinase C; colocalization; actin; immunoprecipitation; sustained smooth muscle contraction; Raf-1
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