Primary structural documentation of the major urinary protein of the Indian commensal rat (Rattus rattus) using a proteomics platform
Purpose: A number of proteome studies have been performed recently to identify pheromone-related protein expression and their molecular function using genetically modified rodents' urine. However, no such studies have used Indian commensal rodents; interestingly, in a previous investigation, we...
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ftindianacasci:oai:repository.ias.ac.in:61232 2023-05-15T18:05:44+02:00 Primary structural documentation of the major urinary protein of the Indian commensal rat (Rattus rattus) using a proteomics platform Rajkumar, Ramalingam Prakash, Subramanya Archunan Ramanathan, Govindaraju 2010-04 http://repository.ias.ac.in/61232/ http://www.benthamscience.com/contents-JCode-PPL-Vol-00000017-Iss-00000004.htm#3158528 unknown Bentham Science Publishers Rajkumar, Ramalingam Prakash, Subramanya Archunan Ramanathan, Govindaraju (2010) Primary structural documentation of the major urinary protein of the Indian commensal rat (Rattus rattus) using a proteomics platform Protein and Peptide Letters, 17 (4). pp. 449-457. ISSN 0929-8665 QH301 Biology Article PeerReviewed 2010 ftindianacasci 2013-01-20T12:16:11Z Purpose: A number of proteome studies have been performed recently to identify pheromone-related protein expression and their molecular function using genetically modified rodents' urine. However, no such studies have used Indian commensal rodents; interestingly, in a previous investigation, we confirmed the presence of volatile molecules in commensal rodents urine and these molecules seem to be actively involved in pheromonal communication. Therefore, the present study aims to identify the major urinary protein [MUP] present in commensal rat urine, which will help us to understand the protein's expression pattern and intrinsic properties among the rodents globally. Experimental Design: Initially, the total urinary proteins were separated by 1-D and 2-D electrophoresis and then subsequently analyzed by Matrix Assisted Laser Desorption Ionization-Time of Flight and Mass Spectrometer (MALDITOF/ MS). Furthermore, they were then fragmented with the aid of a Tandem Mass Spectrometer (TOF/TOF) and the identified sequences aligned and confirmed using similarity with the deduced primary structures of members of the lipocalin superfamily. Results: The SDS-PAGE protein profiles showed distinct proteins with molecular masses of 15, 22.4, 25, 28, 42, 50, 55, 68, and 91 kDa. Of these proteins, the 22.4 kDa protein was considered to be target candidate. When 2D electrophoresis was carried out, about ~50 spots were detected with different masses and various pI ranges. The 22.4 kDa protein was found to have a pI of about 4.9. This 22.4 kDa protein spot was digested and subjected to mass spectrometry; it was identified as rat MUP. The fragmented peptides from the rat MUP at 935, 1026, 1192, and 1303 m/z were further fragmented with the aid of MS/MS and generated de novo sequence and this confirmed this protein to be the MUP present in the urine of commensal rats. Conclusion: The present investigation confirms the presence of MUP with a molecular mass of 22.4 kDa in the urine of commensal rats. This protein may be involved in the binding of volatile molecules and opens up a discussion about how volatile and non-volatile molecules in the commensal rats' urine may contribute chemo-communic. Article in Journal/Newspaper Rattus rattus Indian Academy of Sciences: Publication of Fellows Indian |
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Indian Academy of Sciences: Publication of Fellows |
op_collection_id |
ftindianacasci |
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unknown |
topic |
QH301 Biology |
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QH301 Biology Rajkumar, Ramalingam Prakash, Subramanya Archunan Ramanathan, Govindaraju Primary structural documentation of the major urinary protein of the Indian commensal rat (Rattus rattus) using a proteomics platform |
topic_facet |
QH301 Biology |
description |
Purpose: A number of proteome studies have been performed recently to identify pheromone-related protein expression and their molecular function using genetically modified rodents' urine. However, no such studies have used Indian commensal rodents; interestingly, in a previous investigation, we confirmed the presence of volatile molecules in commensal rodents urine and these molecules seem to be actively involved in pheromonal communication. Therefore, the present study aims to identify the major urinary protein [MUP] present in commensal rat urine, which will help us to understand the protein's expression pattern and intrinsic properties among the rodents globally. Experimental Design: Initially, the total urinary proteins were separated by 1-D and 2-D electrophoresis and then subsequently analyzed by Matrix Assisted Laser Desorption Ionization-Time of Flight and Mass Spectrometer (MALDITOF/ MS). Furthermore, they were then fragmented with the aid of a Tandem Mass Spectrometer (TOF/TOF) and the identified sequences aligned and confirmed using similarity with the deduced primary structures of members of the lipocalin superfamily. Results: The SDS-PAGE protein profiles showed distinct proteins with molecular masses of 15, 22.4, 25, 28, 42, 50, 55, 68, and 91 kDa. Of these proteins, the 22.4 kDa protein was considered to be target candidate. When 2D electrophoresis was carried out, about ~50 spots were detected with different masses and various pI ranges. The 22.4 kDa protein was found to have a pI of about 4.9. This 22.4 kDa protein spot was digested and subjected to mass spectrometry; it was identified as rat MUP. The fragmented peptides from the rat MUP at 935, 1026, 1192, and 1303 m/z were further fragmented with the aid of MS/MS and generated de novo sequence and this confirmed this protein to be the MUP present in the urine of commensal rats. Conclusion: The present investigation confirms the presence of MUP with a molecular mass of 22.4 kDa in the urine of commensal rats. This protein may be involved in the binding of volatile molecules and opens up a discussion about how volatile and non-volatile molecules in the commensal rats' urine may contribute chemo-communic. |
format |
Article in Journal/Newspaper |
author |
Rajkumar, Ramalingam Prakash, Subramanya Archunan Ramanathan, Govindaraju |
author_facet |
Rajkumar, Ramalingam Prakash, Subramanya Archunan Ramanathan, Govindaraju |
author_sort |
Rajkumar, Ramalingam |
title |
Primary structural documentation of the major urinary protein of the Indian commensal rat (Rattus rattus) using a proteomics platform |
title_short |
Primary structural documentation of the major urinary protein of the Indian commensal rat (Rattus rattus) using a proteomics platform |
title_full |
Primary structural documentation of the major urinary protein of the Indian commensal rat (Rattus rattus) using a proteomics platform |
title_fullStr |
Primary structural documentation of the major urinary protein of the Indian commensal rat (Rattus rattus) using a proteomics platform |
title_full_unstemmed |
Primary structural documentation of the major urinary protein of the Indian commensal rat (Rattus rattus) using a proteomics platform |
title_sort |
primary structural documentation of the major urinary protein of the indian commensal rat (rattus rattus) using a proteomics platform |
publisher |
Bentham Science Publishers |
publishDate |
2010 |
url |
http://repository.ias.ac.in/61232/ http://www.benthamscience.com/contents-JCode-PPL-Vol-00000017-Iss-00000004.htm#3158528 |
geographic |
Indian |
geographic_facet |
Indian |
genre |
Rattus rattus |
genre_facet |
Rattus rattus |
op_relation |
Rajkumar, Ramalingam Prakash, Subramanya Archunan Ramanathan, Govindaraju (2010) Primary structural documentation of the major urinary protein of the Indian commensal rat (Rattus rattus) using a proteomics platform Protein and Peptide Letters, 17 (4). pp. 449-457. ISSN 0929-8665 |
_version_ |
1766177248660946944 |