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Parathyroid hormone-related protein (PTHrP) is
endoproteolytically processed to yield a family of mature secretory
forms. These include an amino-terminal, a mid-region, and a
carboxyl-terminal form. Prior studies suggested that the mid-region
form is secreted via the regulated secretory pathway, whereas the
amino- and carboxyl-terminal forms are secreted via the constitutive
pathway. Further, PTHrP is unusual in that it is produced under normal
circumstances by neuroendocrine cell types as well as by prototypical
constitutively secreting cell types. The potential for cell-specific
secretory pathway use by PTHrP has not been explored. Using
immunohistochemical and perifusion techniques, we demonstrate that all
three PTHrP daughter peptides are secreted via the regulated pathway in
neuroendocrine cells. In contrast, all three daughter peptides are
secreted in a constitutive fashion by non-neuroendocrine cells. Thus,
the secretion of PTHrP is unique in that it appears to be
cell-specific. When it is expressed in neuroendocrine cells that
contain the regulated pathway, it is secreted in a regulated fashion;
when it is expressed in non-neuroendocrine cells, it defaults to the
constitutive pathway. This phenomenon has not previously been described
for a polypeptide hormone in naturally occurring cells.
Volume 270,
Number 23,
Issue of June 9, pp. 14078-14084, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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