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(Received for publication, March 29, 1996, and in revised form, August 5, 1996)
From Connective Therapeutics, Inc.,
Palo Alto, California 94303
Relaxin is a 6-kDa peptide of the insulin family
that is present at increased levels in the circulation during
pregnancy. Its functions at that time are thought to include
maintenance of myometrial quiescence, regulation of plasma volume, and
release of neuropeptides, such as oxytocin and vasopressin. The protein
also promotes connective tissue remodeling, which allows cervical
ripening and separation of the pelvic symphysis in various mammalian
species. In this report, we provide evidence for a novel target of
relaxin, the human monocytic cell line, THP-1. Relaxin bound with high
affinity (Kd = 102 pM) to a specific
receptor on THP-1 cells. Receptor density was low (~275
receptors/cell), but binding of relaxin triggered intracelluar
signaling events. Receptor density was not modulated by pretreatment
with estrogen, progesterone, or a number of other agents known to
induce differentiation of THP-1 cells. Cross-linking studies showed
radiolabeled relaxin bound primarily to cell surface proteins with an
apparent molecular mass of >200 kDa. Other members of the insulin-like
family of proteins (insulin, insulin-like growth factors I and II, and
relaxin-like factor) were unable to displace the binding of relaxin to
THP-1 cells, suggesting that a distinct receptor for relaxin exists on
this monocyte/macrophage cell line.
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27936-27941
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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