Efficient eukaryotic expression system for authentic human sex hormone-binding globulin

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Item Type:	Article
Title:	Efficient eukaryotic expression system for authentic human sex hormone-binding globulin
Creators Name:	Hilpert, J., Vorum, H., Burmeister, R., Spoelgen, R., Grishkovskaya, I., Misselwitz, R., Nykjaer, A. and Willnow, T.E.
Abstract:	Sex hormone-binding globulin (SHBG) is the main carrier for androgens and oestrogens in humans. It mediates the transport of steroid hormones in the circulation and testicular fluid, and regulates their bioavailability to steroid-responsive tissues. In addition, the protein interacts with membrane receptors expressed in target tissues. Binding to the receptors is suspected to facilitate the uptake of steroid hormones and/or elicit cellular signal transduction. The identity of the SHBG receptor has not yet been resolved, in part due to a lack of sufficient quantities of authentic SHBG for receptor purification and molecular characterization. We have successfully addressed this problem by establishing an episomal expression system in human embryonic kidney cells that produces 5 mg of fully active human SHBG per litre. The recombinant protein resembles native SHBG in terms of structure, glycosylation pattern and steroid-binding activity. Moreover, the protein interacts with plasma membranes in steroid target tissues, an activity not observed with SHBG from other recombinant expression systems. Thus our studies have removed an important obstacle to the further elucidation of the role SHBG plays in steroid hormone action.
Keywords:	Membrane Binding, Protein Purification, Steroid Carrier, Steroid Hormone Uptake
Source:	Biochemical Journal
ISSN:	0264-6021
Publisher:	Portland Press
Volume:	360
Number:	3
Page Range:	609-615
Date:	1 January 2001
Official Publication:	https://doi.org/10.1042/bj3600609
PubMed:	View item in PubMed

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