Author:
Morel L,Dufaure JP,Depeiges A
Abstract
The epididymal epithelial cells of the lizard (Lacerta vivipara) produce large amounts of specific proteins under androgenic control. Amongst them, a major protein family that binds to the head of spermatozoa, the lizard epididymal secretory protein (LESP) family, has been identified as a member of the lipocalin superfamily. LESPs are composed of 9 elements that present an identical molecular mass of 18 000 Da but have a large range of pHi (3.5 to 9). The structural analysis of this protein family was performed by the determination and comparison of both the aminoterminal sequence of each element and the complete sequence of three specific LESP cDNA clones. When not identical, LESP elements present randomly dispatched nucleotide and amino acid substitutions, indicating the existence of at least five LESP mRNA populations encoded by a multigenic family. We determined that these LESP genes are differentially expressed during the annual epididymal cycle.
Subject
Endocrinology,Molecular Biology
Cited by
13 articles.
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2. Expression, Purification, and Refolding of Human Lipocalin 6 and Production of a Monoclonal Antibody Against This Protein;Monoclonal Antibodies in Immunodiagnosis and Immunotherapy;2017-08
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4. Monotremes Provide a Key to Understanding the Evolutionary Significance of Epididymal Sperm Maturation;Journal of Andrology;2011-03-25
5. Hormones and the Sex Ducts and Sex Accessory Structures of Reptiles;Hormones and Reproduction of Vertebrates;2011