EVIDENCE FOR BINDING OF HUMAN-PREGNANCY ZONE PROTEIN PROTEINASE COMPLEX TO ALPHA-2-MACROGLOBULIN RECEPTORS
EVIDENCE FOR BINDING OF HUMAN-PREGNANCY ZONE PROTEIN PROTEINASE COMPLEX TO ALPHA-2-MACROGLOBULIN RECEPTORS
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DOI:
10.1016/0304-4165(86)90276-x
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发表时间:
1986-10-01
期刊:
影响因子:
--
通讯作者:
SONNE, O
中科院分区:
文献类型:
--
作者:
GLIEMANN, J;MOESTRUP, S;SONNE, O
125I-labelled human pregnancy zone protein complexed with chymotrypsin was removed from the circulation with a half-time of 2.3 min after intravenous injection in rats. AFter 6 min about 67% of the label was present in the liver and about 3% was in the spleen, both in male and in female pregnant rats. The half-time of removal was more than 30 min for native pregnancy zone protein. Uptake into other organs, including placentae and feti, was negligible. 30 pM labelled pregnancy zone protein .cntdot. chymotrypsin was specifically bound to rat hepatocytes and adipocytes and to human fibroblasts and monocyte-derived macrophages at 4.degree.C. Binding was almost completely abolished by a saturating concentration of unlabelled .alpha.2-macroglobulin .cntdot. trypsin. Binding of 15 pM labelled macroglobulin complex was completely abolished by a saturating concentration of pregnancy zone protein .cntdot. chymotrypsin. In rat hepatocytes, binding of pregnancy zone protein complex was lower than that of .alpha.2-macroglobulin complex at low ligand concentrations. Half-maximal receptor occupancy was obtained with about 300 pM pregnancy zone protein complex. Unlabelled .alpha.2-macroglobulin or pregnancy zone protein complex failed to accelerate dissociation of the labelled pregnancy zone protein complex under conditions where dissociation of .alpha.2-macroglobulin was markedly enhanced. It is concluded that pregnancy zone protein and .alpha.2-macroglobulin complexes bind to the same receptors. The quantitative differences may be related to the fact that .alpha.2-macroglobulin is a tetramer whereas the functional unit of pregnancy zone protein is probably a dimer.