REVIEW: Structural and Functional Mapping of alpha-Fetoprotein

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A. A. Terentiev^* and N. T. Moldogazieva

Russian State Medical University, ul. Ostrovityanova 1, 117997 Moscow, Russia; fax: (7-495) 434-0588; E-mail: aaterent@mtu-net.ru

^* To whom correspondence should be addressed.

Received November 11, 2004; Revision received July 18, 2005

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alpha-Fetoprotein (AFP) is a major mammalian oncofetal protein, which is also present in small quantities in adults. It is a member of the albuminoid gene superfamily, which consists of AFP, serum albumin, vitamin D binding protein, and alpha-albumin (afamin). Although physicochemical and immunological properties of AFP have been well-studied, its biological role in embryo- and carcinogenesis and in adult organisms as well as mechanisms underlying its functioning remain unclear. During the recent decades, the biological role of AFP has been evaluated by identification of its functionally important sites. Comparison of primary structure of AFP and some physiologically active proteins revealed similarity of some polypeptide regions. This has been used for prediction of AFP functions (i.e., its multifunctionality). Localization of functionally important sites followed by determination of their amino acid composition and type of biological activity has provided valuable information for structural-functional mapping of AFP. Some peptide fragments of AFP have been synthesized and tested for biological activity. This review summarizes data on structural-functional interrelationships. We also describe functionally important AFP sites found by various groups during the last decade of structural-functional mapping of AFP with experimentally confirmed and putative biologically active sites.

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KEY WORDS: AFP, alpha-fetoprotein, peptide fragments, structural-functional mapping, multifunctionality

DOI: 10.1134/S0006297906020027

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