Proteome mapping of the Drosophila melanogaster male reproductive system

Abstract

The fruit fly Drosophila melanogaster is an excellent model organism for studying insect reproductive biology. Although the gene expression profiles of both male and female reproductive organs have been studied in detail, their proteomic profiles and functional characteristics largely remained to be clarified. In this study, we conducted proteome mapping of the male internal reproductive organs using 2-DE. We identified a total of 440 protein components from gels of the male reproductive organs (testis, seminal vesicle, accessory gland, ejaculatory duct, and ejaculatory bulb). A number of proteins associated with odorant/pheromone-binding, lipid metabolism, proteolysis, and antioxidation were expressed tissue specifically in the male reproductive system. Based on our proteomic data set, we constructed reference proteome maps of the reproductive organs, which will provide valuable information toward a comprehensive understanding of Drosophila reproduction.

Proteomics enhances evolutionary and functional analysis of reproductive proteins

“…For example, recent studies identified proteins from male reproductive tissues in flies and mice. (30,31,40) Many of these proteins may interact with female proteins, and others may influence the regulation or modification of interacting proteins. Others, however, could play housekeeping roles that do not relate specifically to reproduction.…”

“…A recent explosion of proteomics studies has identified many reproductive proteins in taxa ranging from crickets and honeybees to rodents and humans. (15,(26)(27)(28)(29)(30)(31)(32)(33)(34)(35)(36)(37)(38)(39)(40) Applying mass spectrometry (MS)-based proteomics to the study of reproduction has been particularly fruitful, in our view, because reproductive tissues are often specialized cell types with the discrete function of producing proteins involved in a specific biological process. Thus, biochemical isolation and purification of proteins from these tissues and cell types are straightforward, and large amounts of relatively pure protein mixtures can be analyzed by MS.…”

A Drosophila Protease Cascade Member, Seminal Metalloprotease-1, Is Activated Stepwise by Male Factors and Requires Female Factors for Full Activity

“…In D. melanogaster, ablation of the major Sfp-producing tissue, the male accessory gland (AG), results in the complete loss of male fertility (Kalb et al 1993;Gligorov et al 2013), unless Sfps are provided by a second male (Xue and Noll 2000). Over 200 Sfps are transferred (or inferred to be transferred) to females during mating in D. melanogaster (Ravi Ram and Wolfner 2007;Findlay et al 2008Findlay et al , 2009Takemori and Yamamoto 2009;Yamamoto and Takemori 2010). However, functions have been assigned to only a small proportion of Sfps in this, or any, species (Avila et al 2011).…”

“…In humans, .100 proteins in the seminal plasma are proteolysis regulators (out of 950 seminal proteins) (Utleg et al 2003;Fung et al 2004;Pilch and Mann 2006). In D. melanogaster, proteins with predicted protease or protease inhibitor domains account for at least 14% of known or inferred Sfps (Ravi Ram and Wolfner 2007;Findlay et al 2008Findlay et al , 2009Takemori and Yamamoto 2009;Yamamoto and Takemori 2010), though individual proteins in this class tend to be of low abundance (Findlay et al 2008).…”

Drosophila Genetic Resource and Stock Center; The National BioResource Project

“…Drosophila resources have been maintained in the laboratory for a very long time by inbreeding, and by using balancers and other techniques for producing homozygous populations on any scale. This homozygous constant genetic background is very valuable in proteomic analyses [41,50]. A high frequency of SNPs is convenient for mapping genes, but it causes serious problems in comprehensive proteomic profiling of specific tissues and organs.…”