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Abstract
Calponin (h1 isoform) was characterized as a smooth muscle specific, actin-, tropomyosin-,
calmodulin-binding protein and described as a factor which inhibits contraction. H2-calponin,
encoded by a different gene from h1-calponin, was identified from the smooth muscles
of mouse and pig. However, non-muscle calponin analogues have recently been reported
in rat and pig brains. Here we show the presence of calponin expressed in human skin
tissue and in cultured human keratinocytes using polyclonal antibodies to bovine aortic
smooth muscle calponin. Western blot analysis demonstrated that calponin with a molecular
weight around 36000 existed in extracts of keratinocytes. Immunofluorescence microscopy
displayed the localization of calponin in the cytoplasm of the basal cells in situ,
and along the cell-to-cell borders in cultured human keratinocytes maintained in standard
calcium medium. Furthermore, according to RT-PCR analysis using human h1- and h2-calponin-specific
primers, calponin expressed by cultured human keratinocytes was identified as the
h2 isoform. We demonstrated the presence of h2-calponin in human keratinocytes, and
it might play a role in the structural organization of actin cytoskeleton at the cytoplasmic
region of cell-to-cell junctions of keratinocytes.
Keywords
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Article info
Publication history
Accepted:
April 2,
1996
Received in revised form:
March 1,
1996
Received:
December 22,
1995
Identification
Copyright
© 1997 Published by Elsevier Inc.