REVIEW: Functional Properties of Extracellular Domains of Transducer Receptor gp130

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M. N. Kostjukova and N. N. Tupitsyn^*

Cancer Research Center, Russian Academy of Medical Sciences, Kashirskoe Shosse 24, 115478 Moscow, Russia; fax: (495) 324-1430; E-mail: nntca@yahoo.com

^* To whom correspondence should be addressed.

Received August 6, 2010; Revision received September 17, 2010

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Cytokine receptor molecules have been shown to have extracellular domains of complex structure and a multi-step activation system. Glycoprotein gp130 is a typical transducer of cytokine signal; it functions by forming multicomponent receptor complexes and transferring signals of tens of cytokines from the IL-6 family. Structural organization and basic functioning principles of gp130 are well known, as well as related signal pathways, which function during normal differentiation and are involved in pathogenesis of many tumors. The role of gp130 in IL-6-dependent tumors is best studied. In this review, based on extensive accumulated data, we examine the functional significance of certain parts of gp130 extracellular domains. Potentials of a recently developed method for estimation of receptor activation at the level of epitope structure are discussed.

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KEY WORDS: gp130 activation, cytokine, immunophenotyping, monoclonal antibodies, receptor structure, IL-6, cytokine-binding homology region

DOI: 10.1134/S000629791104002X

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