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Lens proteome map and <img src='/image/spc_char/alpha.gif' border=0>-crystallin profile of the catfish <i style="">Rita rita</i>

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Title Lens proteome map and -crystallin profile of the catfish Rita rita
 
Creator Mohanty, Bimal Prasanna
Bhattacharjee, Soma
Das, Manas Kumar
 
Subject -Crystallin
Biomarker
Cataract
Crystallin proteome map
Lens proteins
Rita rita
 
Description 35-41
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 Rita rita. Profiles of lens
crystallins were analyzed and crystallin proteome maps of Rita rita were generated for the first
time. A-crystallins, member of the -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-A-crystallin
antibody. Two protein bands of 19-20 kDa were identified as A-crystallins on
1-D immunoblots and these bands separated into 10 discrete spots on 2-D
immunoblot. However, anti-B-crystallin and antiphospho-B-crystallin
antibodies were not able to detect any immunoreactive bands on 1- and 2-D
immunoblots, indicating B-crystallin was either absent or present in extremely
low concentration in Rita rita lens.
Thus, Rita rita -crystallins are
more like that of the catfish Clarias
batrachus and the mammal kangaroo in its A- and B-crystallin
content (contain low amount from 5-9% of aB-crystallin) and unlike
the dogfish, zebrafish, human, bovine and mouse -crystallins (contain
higher amount of 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 Rita rita
lens crystallins for comparative lens proteomics. Comparing and contrasting the
-crystallins
of the dogfish and Rita rita may
provide valuable information on the functional attributes of A- and B-isoforms, as
they are at the two extremes in terms of A-and B-crystallin
content.
 
Date 2011-02-25T04:17:03Z
2011-02-25T04:17:03Z
2011-02
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/11103
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.48(1) [February 2011]