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Claus Oxvig

Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma

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Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma. / Oxvig, Claus; Haaning, Jesper; Kristensen, Lene; Wagner, Jill M; Rubin, Inger; Stigbrand, Torgny; Gleich, Gerald J; Sottrup-Jensen, Lars.

In: Journal of Biological Chemistry, Vol. 270, No. 23, 09.06.1995, p. 13645-13651.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Oxvig, C, Haaning, J, Kristensen, L, Wagner, JM, Rubin, I, Stigbrand, T, Gleich, GJ & Sottrup-Jensen, L 1995, 'Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma', Journal of Biological Chemistry, vol. 270, no. 23, pp. 13645-13651. https://doi.org/10.1074/jbc.270.23.13645

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Author

Oxvig, Claus ; Haaning, Jesper ; Kristensen, Lene ; Wagner, Jill M ; Rubin, Inger ; Stigbrand, Torgny ; Gleich, Gerald J ; Sottrup-Jensen, Lars. / Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma. In: Journal of Biological Chemistry. 1995 ; Vol. 270, No. 23. pp. 13645-13651.

Bibtex

@article{a4a4c1676a0c4684b403652e27186656,
title = "Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma",
abstract = "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.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.",
keywords = "Amino Acid Sequence, Angiotensinogen, Animals, Blood Proteins, Complement C3b, Eosinophil Granule Proteins, Female, Humans, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Molecular Weight, Peptide Fragments, Placenta, Pregnancy, Pregnancy Proteins, Pregnancy-Associated Plasma Protein-A, Protein Precursors, Ribonucleases",
author = "Claus Oxvig and Jesper Haaning and Lene Kristensen and Wagner, {Jill M} and Inger Rubin and Torgny Stigbrand and Gleich, {Gerald J} and Lars Sottrup-Jensen",
year = "1995",
month = jun,
day = "9",
doi = "10.1074/jbc.270.23.13645",
language = "English",
volume = "270",
pages = "13645--13651",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "23",

}

RIS

TY - JOUR

T1 - Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma

AU - Oxvig, Claus

AU - Haaning, Jesper

AU - Kristensen, Lene

AU - Wagner, Jill M

AU - Rubin, Inger

AU - Stigbrand, Torgny

AU - Gleich, Gerald J

AU - Sottrup-Jensen, Lars

PY - 1995/6/9

Y1 - 1995/6/9

N2 - 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.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.

AB - 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.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.

KW - Amino Acid Sequence

KW - Angiotensinogen

KW - Animals

KW - Blood Proteins

KW - Complement C3b

KW - Eosinophil Granule Proteins

KW - Female

KW - Humans

KW - Mice

KW - Mice, Inbred BALB C

KW - Molecular Sequence Data

KW - Molecular Weight

KW - Peptide Fragments

KW - Placenta

KW - Pregnancy

KW - Pregnancy Proteins

KW - Pregnancy-Associated Plasma Protein-A

KW - Protein Precursors

KW - Ribonucleases

U2 - 10.1074/jbc.270.23.13645

DO - 10.1074/jbc.270.23.13645

M3 - Journal article

C2 - 7539791

VL - 270

SP - 13645

EP - 13651

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 23

ER -