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Thyrotropin Receptor

Characterization and Purification
  • Takashi Akamizu
  • Michele De Luca
  • Leonard D. Kohn
Part of the Receptor Purification book series (RP, volume 1)

Abstract

There is general agreement today that the TSH receptor has a high affinity TSH-binding component (Fig. 1) that is a membrane glycoprotein (Kohn et a1.,1985; Kress and Spiro, 1986). The existence of a glycolipid (Fig. 1) that can modify the binding properties of this glycoprotein, as well as act as a coupler of the high affinity binding site to G proteins related to adenylate cyclase complex, has also been argued (Kohn, 1978; Kohn et al., 1985); its role is more controversial. No consensus currently exists, however, as to the detailed structure of the thyrotropin receptor, despite the efforts of many laboratories. This results from the current unsettled state of receptor purification and characterization; hence, the present summary can only be viewed as a state of the art and procedures as they currently exist. To place them in perspective, some discussion of the various procedures used to characterize the receptor will be included. The prime focus will concentrate on the glycoprotein component and on one set of techniques and their problems as a representative picture. In addition, cloning studies will be presented that are necessary and appear to be clarifying the problem.

Keywords

Thyroid Cell Thyrotropin Receptor Thyroid Membrane Human Thyroid Carcinoma Glycoprotein Component 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Takashi Akamizu
  • Michele De Luca
  • Leonard D. Kohn

There are no affiliations available

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