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Male-predominant carboxylesterase expression in the reproductive system of molluscs and insects: immunochemical and biochemical similarity between Mytilus male associated polypeptide (MAP) and Drosophila sex-specific esterase S.

作者信息

Mikhailov A T, Torrado M, Korochkin L I, Kopantzeva M A, Méndez J

机构信息

Institute of Health Sciences, University of La Coruña, Spain.

出版信息

Comp Biochem Physiol B Biochem Mol Biol. 1997 Sep;118(1):197-208. doi: 10.1016/s0305-0491(97)00001-1.

Abstract

We suggested that sexual differentiation of the reproductive system in gonochoric species of invertebrates can be characterized by common molecular mechanisms in spite of high morphological divergences of reproductive tract organs in different animal groups. The present study focused on this problem and report our observations on biochemical characteristics of male-associated polypeptide (MAP) identified in the gonad tissue of bivalve molluscs, Mytilus galloprovincialis, in comparison to those of male-specific carboxylesterase (esterase S) of Drosophila virilis ejaculatory bulbs. We provide evidences for the immunochemical similarity of Mytilus MAP and Drosophila esterase S. We also show that MAP is characterized by esterase activity toward both, alpha- and beta-naphthyl acetates. Using immunofluorescence, we found MAP in the gonad (mantle) connective tissue, membranes of follicles and around gonad ducts but not in sperm cells. Nevertheless, the levels of MAP expression depend on presence or absence of ripe spermatozoa in the gonad follicles. In mature gonads before spawning, MAP is expressed at high level, while in the spent gonads only traces of this polypeptide could be detected. Using Western immunoblot, MAP was not observed in spermatozoa obtained by biopsy of gonad follicles. In contrast, we found this protein in spawned sperm cells. Thus, we suggest that spawning may be required to establish the trafficking mechanisms that control whether MAP is retained or excreted by the gonad. Taken together, the results indicate that MAP of M. galloprovincialis is structurally and functionally related to esterase S of D. virilis ejaculatory bulbs.

摘要

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