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In sera from pregnant women, pregnancy-associated plasma
protein-A (PAPP-A) circulates as a disulfide-bound complex
(approximately 474 kDa) with the proform of eosinophil major basic
protein (proMBP) (Oxvig, C., Sand, O., Kristensen, T., Gleich, G. J.,
and Sottrup-Jensen, L. (1993) J. Biol. Chem. 268,
12243-12246). We have produced monoclonal antibodies (mAbs)
against the PAPP-A
Volume 270,
Number 23,
Issue of June 9, pp. 13645-13651, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
proMBP complex and established a
radioimmunoassay utilizing a mAb recognizing the PAPP-A subunit.
Surprisingly, serum levels of proMBP exceed those of PAPP-A four to
10-fold on a molar basis throughout pregnancy. This result prompted an
investigation of the status of proMBP in pregnancy. Using a
proMBP-specific mAb two novel proMBP complexes have been isolated by
chromatographic techniques. Based on sequence analysis, sodium dodecyl
sulfate-polyacrylamide gel electrophoresis, and reaction with specific
antibodies, one is shown to be a 2:2 disulfide-bound complex
(approximately 200 kDa) between proMBP and angiotensinogen. The other
is a 2:2:2 complex (approximately 300 kDa) between proMBP,
angiotensinogen, and complement C3dg. Circulating proMBP in pregnancy
is thus present in three types of complexes. These results suggest that
specific interactions between the complexed proteins occur in
pregnancy, and the possibility is raised that their interactions are
important in the pathophysiology of pregnancies associated with
hypertension.
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