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. 1995 May 1;307(Pt 3):669–672. doi: 10.1042/bj3070669

Expression of haemopexin receptors by cultured human cytotrophoblast.

H P van Dijk 1, M J Kroos 1, J S Starreveld 1, H G van Eijk 1, S P Tang 1, D X Song 1, U Muller-Eberhard 1
PMCID: PMC1136703  PMID: 7741695

Abstract

The expression of cell-surface haemopexin (Hx) receptors on human cytotrophoblasts was assessed by using four different Hx species purified from plasma: human Hx isolated by wheatgerm-affinity chromatography, human Hx isolated by haem-agarose-affinity chromatography and rabbit and rat Hx, also isolated by haem-agarose-affinity chromatography. About 3500-7000 high-affinity (Kd 0.34-0.85 nM) receptors per cell were measured by Scatchard-type analysis at 4 degrees C using human (species obtained by both methods) or rabbit 125I-labelled haem-Hx. Measured simultaneously, transferrin receptor number and affinity were 40,000/cell and 0.83 nM respectively. In contrast with transferrin receptors, the number of Hx receptors did not increase during 24 h in cytotrophoblast culture. Rat Hx showed no specific binding to human Hx receptors in cytotrophoblast cultures.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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