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Alpha-fetoprotein inhibits frog metamorphosis: implications for protein motif conservation
Authors:Butterstein G M  Mizejewski G J
Affiliation:Department of Biological Sciences, Union College, Schenectady, NY 12308-2311, USA. buttersg@union.ed
Abstract:Alpha-fetoprotein (AFP) is a tumor-associated fetal protein which has served as a marker for both oncogenic and ontogenetic growth. A growth regulatory segment on human AFP contains amino acid sequence identity and similarity with Rana and Xenopus albumin molecules. This study assessed the ability of both intact mammalian AFP and a derived peptide to influence thyroid induction of tail resorption during Rana catesbeiana metamorphosis. After AFP and other proteins/peptides were pre-incubated with triiodothyronine (T3) for 1 h, they were added to intact tadpoles in 300 ml of water. Human and/or mouse AFP, at a concentration of 70 ng/ml, completely inhibited T3-induced tail loss when measured over a 5 day period. In contrast, albumin and other proteins were without affect. A peptide (P149) with the sequence of human AFP residues # 447-480 also completely blocked the tail response at a concentration of 33 ng/ml, whereas a scrambled version of this peptide was without activity. The present peptide segment derived from mammalian AFP might represent a highly conserved serum protein motif in the vertebrate phyla since it is capable of influencing growth, differentiation and transformation phenomenon in amphibians.
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