Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/11103
Title: Lens proteome map and <img src='/image/spc_char/alpha.gif' border=0>-crystallin profile of the catfish <i style="">Rita rita</i>
Authors: Mohanty, Bimal Prasanna
Bhattacharjee, Soma
Das, Manas Kumar
Keywords: <img src='/image/spc_char/alpha.gif' border=0>-Crystallin
Biomarker
Cataract
Crystallin proteome map
Lens proteins
<i style="">Rita rita</i>
Issue Date: Feb-2011
Publisher: NISCAIR-CSIR, India
Abstract: Crystallins are a diverse group of proteins that constitute nearly 90% of the total soluble proteins of the vertebrate eye lens and these tightly packed crystallins are responsible for transparency of the lens. These proteins have been studied in different model and non-model species for understanding the modifications they undergo with ageing that lead to cataract, a disease of protein aggregation. In the present investigation, we studied the lens crystallin profile of the tropical freshwater catfish <i style="">Rita rita</i>. Profiles of lens crystallins were analyzed and crystallin proteome maps of <i style="">Rita rita</i> were generated for the first time. <img src='/image/spc_char/alpha.gif' border=0>A-crystallins, member of the <img src='/image/spc_char/alpha.gif' border=0>-crystallin family, which are molecular chaperons and play crucial role in maintaining lens transparency were identified by 1-and 2-D immunoblot analysis with anti-<img src='/image/spc_char/alpha.gif' border=0>A-crystallin antibody. Two protein bands of 19-20 kDa were identified as <img src='/image/spc_char/alpha.gif' border=0>A-crystallins on 1-D immunoblots and these bands separated into 10 discrete spots on 2-D immunoblot. However, anti-<img src='/image/spc_char/alpha.gif' border=0>B-crystallin and antiphospho-<img src='/image/spc_char/alpha.gif' border=0>B-crystallin antibodies were not able to detect any immunoreactive bands on 1- and 2-D immunoblots, indicating <img src='/image/spc_char/alpha.gif' border=0>B-crystallin was either absent or present in extremely low concentration in <i style="">Rita rita </i>lens. Thus, <i style="">Rita rita</i> <img src='/image/spc_char/alpha.gif' border=0> -crystallins are more like that of the catfish <i style="">Clarias batrachus</i> and the mammal kangaroo in its <img src='/image/spc_char/alpha.gif' border=0> A- and <img src='/image/spc_char/alpha.gif' border=0>B-crystallin content (contain low amount from 5-9% of aB-crystallin) and unlike the dogfish, zebrafish, human, bovine and mouse <img src='/image/spc_char/alpha.gif' border=0>-crystallins (contain higher amount of <img src='/image/spc_char/alpha.gif' border=0>B-crystallin from 25% in mouse and bovine to 85% in dogfish). Results of the present study can be the baseline information for stimulating further investigation on <i style="">Rita rita</i> lens crystallins for comparative lens proteomics. Comparing and contrasting the <img src='/image/spc_char/alpha.gif' border=0>-crystallins of the dogfish and <i style="">Rita rita</i> may provide valuable information on the functional attributes of <img src='/image/spc_char/alpha.gif' border=0>A- and <img src='/image/spc_char/alpha.gif' border=0>B-isoforms, as they are at the two extremes in terms of <img src='/image/spc_char/alpha.gif' border=0>A-and <img src='/image/spc_char/alpha.gif' border=0>B-crystallin content.
Description: 35-41
URI: http://hdl.handle.net/123456789/11103
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.48(1) [February 2011]

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