Database: PubMedEntry: 20133968
Original site: 20133968
Guo X, Zhao C, Wang F, Zhu Y, Cui Y, Zhou Z,
Huo R, Sha J.
Investigation of human testis protein heterogeneity using 2-dimensional
J Androl. 2010 Jul-Aug;31(4):419-29. doi: 10.2164/jandrol.109.007534. Epub 2010
The testis is the male gonad responsible for spermatogenesis and male hormone
secretion. The complicated processes of spermatogenesis and steroidogenesis
determine the complexity of protein expression control in the testis. In this
study, the heterogeneity of human testis proteins was investigated using
2-dimensional gel electrophoresis. A total of 847 protein spots corresponding to
462 unique proteins were identified successfully by mass spectrometry. Notable
heterogeneity was evidenced by the presence of more than 1 spot with different
molecular weight and/or Isoelectric point values for each of 180 different
proteins. Analysis of the detected peptides of these proteins indicated that this
heterogeneity was partly the result of alternative splicing and/or proteolysis.
SP_PIR_Keywords analysis suggested that alternative initiation sites and various
forms of posttranslational modification may also contribute toward this
heterogeneity. Using Pro-Q Diamond phosphostain, 68 spots representing 52
proteins were stained, confirming the presence of phosphorylated forms of these
proteins in the human testis. These data were used to establish a proteome
reference database, which can be accessed over the Internet
(http://reprod.njmu.edu.cn/2d). This database provides an initial reference map
of the human testis and serves as a useful resource for comparative proteomics
studies of the human testis under normal and pathological states. The abundant
protein heterogeneity observed in this study and further investigation of its
biological significance will contribute toward understanding protein expression
regulation in the human testis and will generate insight into the molecular
mechanism of spermatogenesis.
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