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      Distinct Proteomic Profile of Spermatozoa from Men with Seminomatous and Non-Seminomatous Testicular Germ Cell Tumors

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          Abstract

          Testicular germ cell tumors (TGCTs) are predominant in young males (15–44 years). Seminomatous and non-seminomatous TGCTs account for about 98% of all TGCTs cases. In this study, we aimed to compare the sperm proteome of patients with seminomatous and non-seminomatous TGCTs to identify possible protein biomarkers that could help distinguish between them in a non-invasive manner. We analyzed semen samples from patients with seminomatous or non-seminomatous TGCTs ( n = 15/group) that were cryopreserved before the start of cancer treatment. Quantitative proteomic analysis was conducted on pooled samples ( n = 3/group) and a total of 258 differentially expressed proteins (DEPs) were identified. The overexpression of acrosin precursor (ACR) and chaperonin containing TCP1 subunit 6B (CCT6B) as well as the underexpression of S100 calcium-binding protein A9 (S100A9) in the spermatozoa of patients with non-seminomatous TGCTs were validated by western blotting conducted on individual samples ( n = 6 for seminomatous group and n = 6 for non-seminomatous group). Our overall results suggest an association between the higher and faster invasiveness of non-seminomatous TGCTs and the altered protein expressions, providing important information for future studies.

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          Most cited references40

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          Proteomics: Technologies and Their Applications.

          Proteomics involves the applications of technologies for the identification and quantification of overall proteins present content of a cell, tissue or an organism. It supplements the other "omics" technologies such as genomic and transcriptomics to expound the identity of proteins of an organism, and to cognize the structure and functions of a particular protein. Proteomics-based technologies are utilized in various capacities for different research settings such as detection of various diagnostic markers, candidates for vaccine production, understanding pathogenicity mechanisms, alteration of expression patterns in response to different signals and interpretation of functional protein pathways in different diseases. Proteomics is practically intricate because it includes the analysis and categorization of overall protein signatures of a genome. Mass spectrometry with LC-MS-MS and MALDI-TOF/TOF being widely used equipment is the central among current proteomics. However, utilization of proteomics facilities including the software for equipment, databases and the requirement of skilled personnel substantially increase the costs, therefore limit their wider use especially in the developing world. Furthermore, the proteome is highly dynamic because of complex regulatory systems that control the expression levels of proteins. This review efforts to describe the various proteomics approaches, the recent developments and their application in research and analysis.
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            S100A8 and S100A9: new insights into their roles in malignancy.

            Recent studies have highlighted key roles played by non-neoplastic host cells of the tumor microenvironment, and by secreted factors from tumor and host cells, in promoting malignancy. In this regard, damage-associated molecular pattern (DAMP) molecules such as S100A8 and S100A9, with well-known functions in inflammation, have been increasingly recognized not only as markers, but also as new candidates with important roles in modulating tumor growth and metastasis. This review focuses on our current understanding of the pro- and anti-tumorigenic functions of S100A8 and S100A9. Elucidating molecular pathways mediated by these proteins promises to provide potential novel targets for the development of cancer therapeutics and to establish valid biomarkers to identify early stages of tumor progression. Copyright © 2011 S. Karger AG, Basel.
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              PA200, a nuclear proteasome activator involved in DNA repair.

              We have identified a novel 200 kDa nuclear protein that activates the proteasome. The protein, which we call PA200, has been purified to homogeneity from bovine testis and has been shown to activate proteasomal hydrolysis of peptides, but not proteins. Following gamma-irradiation of HeLa cells the uniform nuclear distribution of PA200 changes to a strikingly punctate pattern, a behavior characteristic of many DNA repair proteins. Homologs of PA200 are present in worms, plants and yeast. Others have shown that mutation of yeast PA200 results in hypersensitivity to bleomycin, and exposure of yeast to DNA damaging agents induces the PA200 message. Taken together, these findings implicate PA200 in DNA repair, possibly by recruiting proteasomes to double strand breaks.
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                Author and article information

                Journal
                Int J Mol Sci
                Int J Mol Sci
                ijms
                International Journal of Molecular Sciences
                MDPI
                1422-0067
                08 July 2020
                July 2020
                : 21
                : 14
                : 4817
                Affiliations
                [1 ]American Center for Reproductive Medicine, Cleveland Clinic, Cleveland, OH 44195, USA; pannerm@ 123456ccf.org (M.K.P.S.); taniadias89@ 123456gmail.com (T.R.D.)
                [2 ]Department of Microscopy, Laboratory of Cell Biology, Institute of Biomedical Sciences Abel Salazar and Unit for Multidisciplinary Research in Biomedicine (UMIB), University of Porto, 4050-313 Porto, Portugal; alvesmarc@ 123456gmail.com
                [3 ]Faculty of Health Sciences, Universidade of Beira Interior, 6201-001 Covilhã, Portugal
                [4 ]King Abdulaziz University, Center of Excellence in Genomic Medicine, Jeddah 21589, Saudi Arabia; peter.n.pushparaj@ 123456gmail.com
                [5 ]Department of Medical Laboratory Technology, Faculty of Applied Medical Sciences, King Abdulaziz University, Jeddah 21577, Saudi Arabia
                Author notes
                [* ]Correspondence: agarwaa@ 123456ccf.org ; Tel.: +1-216-444-9485
                Author information
                https://orcid.org/0000-0002-9120-2278
                https://orcid.org/0000-0001-7635-783X
                https://orcid.org/0000-0002-2336-8006
                https://orcid.org/0000-0001-7574-1880
                https://orcid.org/0000-0003-0585-1026
                Article
                ijms-21-04817
                10.3390/ijms21144817
                7404221
                32650378
                a970df95-be31-45e6-8205-d34199f43b5a
                © 2020 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 13 May 2020
                : 01 July 2020
                Categories
                Article

                Molecular biology
                seminomatous,non-seminomatous,sperm proteomics,male fertility,diagnosis
                Molecular biology
                seminomatous, non-seminomatous, sperm proteomics, male fertility, diagnosis

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