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2013 (Vol. 5, Issue: 1)
Article Information:

Protein Profiling of Gonads of Males and Sex Reversed Males in Nemacheilus angorae

Maryam Cheraghzadeh, Ali Farazmand and Nasrin Motamed
Corresponding Author:  Maryam Cheraghzadeh 

Key words:  Nemacheilus angorae, protein profile, sex reversal, , , ,
Vol. 5 , (1): 19-25
Submitted Accepted Published
September 19, 2012 November 01, 2012 January 20, 2013
Abstract:

In the present study a proteomics approach has been taken to analyze differential protein expression between mature male and sex reversed male of Nemacheilus angorae In regard to the fruitful studies of sex reversal in mammalian species and the fact that some major sex determination molecules are conserved among vertebrates, Nemacheilus angorae (Angorae loach) seems to be a good model system in studying molecules involved in sex differentiation.N. angorae is a teleports fish exhibiting a spontaneous sex reversal (male to female) pattern. The gonads of adult individuals were dissected and used for histological investigation and protein analysis. Proteins were next analyzed using two-dimensional gel electrophoresis and the distinguished spots have been compared in two experimental samples. Among them, 23 differentially expressed proteins spots were identified by MALDI-TOF/TOF analysis. Two spots in sex reversed testis with high score showed significant similarity to Vasa (assembling of the pole plasm and the pronuclear region of the oocyte) and Proline 4-hydroxylase proteins. Vasa are involved in germ cell development both in invertebrates and vertebrates. This data could be considered as starting base for subsequent studies to identify proteins involved in sex reversal and differentiation at different stages of gonadal maturation in fish.
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  Cite this Reference:
Maryam Cheraghzadeh, Ali Farazmand and Nasrin Motamed, 2013. Protein Profiling of Gonads of Males and Sex Reversed Males in Nemacheilus angorae.  Current Research Journal of Biological Sciences, 5(1): 19-25.
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ISSN (Online):  2041-0778
ISSN (Print):   2041-076X
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