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Liu F.-J.,Shandong Research Center for Stem Cell Engineering | Wang H.-Y.,Shandong Research Center for Stem Cell Engineering | Li J.-Y.,Shandong Research Center for Stem Cell Engineering
Molecular Biology Reports | Year: 2012

The testis is the male gonad responsible for spermatogenesis and steroidogenesis. Much remains to be known about the control of these events. In this study, we performed a new bioinformatic enrichment analysis of human testicular proteins selected from a protein database. Integrated function and pathway analyses were performed by Database for Annotation, Visualization and Integrated Discovery and Ingenuity Pathway Analysis programmes, and significant features were found to be clustered. Proteinmembrane organization and gene density on chromosomes were analyzed and discussed. The analysis could provide a basis for the understanding of testicular physiology and function, and facilitating biological interpretation of testicular functions in a network context. © Springer Science+Business Media B.V. 2011. Source


Liu F.,Shandong Research Center for Stem Cell Engineering | Wang H.,Shandong Research Center for Stem Cell Engineering | Li J.,Shandong Research Center for Stem Cell Engineering
BMB Reports | Year: 2011

The testis is major male gonad responsible for spermatogenesis and steroidogenesis. Much knowledge is still remained to be learned about the control of these events. In this study, we performed a comprehensive bioinformatics analysis on 1,196 mouse testis proteins screened from public protein database. Integrated function and pathway analysis were performed through Database for Annotation, Visualization and Integrated Discovery (DAVID) and ingenuity Pathway Analysis (IPA), and significant features were clustered. Protein membrane organization and gene density on chromosomes were analyzed and discussed. The enriched bioinformatics analysis could provide clues and basis to the development of diagnostic markers and therapeutic targets for infertility and male contraception. Source


Li J.,Shandong Research Center for Stem Cell Engineering | Li J.,Yantai University | Liu F.,Shandong Research Center for Stem Cell Engineering | Wang H.,Shandong Research Center for Stem Cell Engineering | And 9 more authors.
Molecular and Cellular Proteomics | Year: 2010

The mammalian spermatozoon has many cellular compartments, such as head and tail, permitting it to interact with the female reproductive tract and fertilize the egg. It acquires this fertilizing potential during transit through the epididymis, which secretes proteins that coat different sperm domains. Optimal levels of these proteins provide the spermatozoon with its ability to move to, bind to, fuse with, and penetrate the egg; otherwise male infertility results. As few human epididymal proteins have been characterized, this work was performed to generate a database of human epididymal sperm-located proteins involved in maturation. Two-dimensional gel electrophoresis of epididymal tissue and luminal fluid proteins, followed by identification using MALDI-TOF/MS or MALDI-TOF/TOF, revealed over a thousand spots in gels comprising 745 abundant nonstructural proteins, 408 in luminal fluids, of which 207 were present on spermatozoa. Antibodies raised to 619 recombinant or synthetic peptides, used in Western blots, histological sections, and washed sperm preparations to confirm antibody quality and protein expression, indicated their regional location in the epididymal epithelium and highly specific locations on washed functional spermatozoa. Sperm function tests suggested the role of some proteins in motility and protection against oxidative attack. A large database of these proteins, characterized by size, pI, chromosomal location, and function, was given a unified terminology reflecting their sperm domain location. These novel, secreted human epididymal proteins are potential targets for a posttesticular contraceptive acting to provide rapid, reversible, functional sterility in men and they are also biomarkers that could be used in noninvasive assessments of male fertility. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc. Source


Li J.,Shandong Research Center for Stem Cell Engineering | Li J.,Yantai University | Liu F.,Shandong Research Center for Stem Cell Engineering | Liu X.,Shandong Research Center for Stem Cell Engineering | And 7 more authors.
Molecular and Cellular Proteomics | Year: 2011

The testis produces male gametes in the germinal epithelium through the development of spermatogonia and spermatocytes into spermatids and immature spermatozoa with the support of Sertoli cells. The flow of spermatozoa into the epididymis is aided by testicular secretions. In the epididymal lumen, spermatozoa and testicular secretions combine with epididymal secretions that promote sperm maturation and storage. We refer to the combined secretions in the epididymis as the sperm-milieu. With two-dimensional-PAGE matrix-assisted laser desorption ionization time-of-flight MS analysis of healthy testes from fertile accident victims, 725 unique proteins were identified from 1920 two-dimensional-gel spots, and a corresponding antibody library was established. This revealed the presence of 240 proteins in the sperm-milieu by Western blotting and the localization of 167 proteins in mature spermatozoa by ICC. These proteins, and those from the epididymal proteome (Li et al. 2010), form the proteomes of the sperm-milieu and the spermatozoa, comprising 525 and 319 proteins, respectively. Individual mapping of the 319 sperm-located proteins to various testicular cell types by immunohistochemistry suggested that 47% were intrinsic sperm proteins (from their presence in spermatids) and 23% were extrinsic sperm proteins, originating from the epididymis and acquired during maturation (from their absence from the germinal epithelium and presence in the epididymal tissue and spermmilieu). Whereas 408 of 525 proteins in the sperm-milieu proteome were previously identified as abundant epididymal proteins, the remaining 22%, detected by the use of new testicular antibodies, were more likely to be minor proteins common to the testicular proteome, rather than proteins of testicular origin added to spermatozoa during maturation in the epididymis. The characterization of the sperm-milieu proteome and testicular mapping of the sperm-located proteins presented here provide the molecular basis for further studies on the production and maturation of spermatozoa. This could be the basis of development of diagnostic markers and therapeutic targets for infertility or targets for male contraception. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc. Source

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