Sperm specific expression of temperature-sensitive ion channel TRPM8 correlates with vertebrate evolution

, , , , , , , , ,
1 Biological Sciences, National Institute of Science Education and Research, Institute of Physics Campus,, Bhubaneswar, Orissa, India
2 School of Biotechnology, KIIT University, Bhubaneswar, Orissa, India
3 School of Biotechnology,, KIIT University, Bhubaneswar, Orissa, India
4 Department of Zoology, Government Science College, Chatrapur, Ganjam, Odisha, India
5 Department of Veterinary Biochemistry,, CVSc&AH, Orissa University of Agriculture & Technology, Bhubaneswar, Orissa, India
6 Biological Sciences, National Institute of Science Education and Research, Institute of Physics Campus, Bhubaneswar, Orissa, India
7 Department of Genetics & Molecular Biology in Botany, Institute of Botany, University of Kiel (CAU), Kiel, Schleswig-Holstein, Germany
DOI
10.7287/peerj.preprints.440v1
Published
Accepted
Subject Areas
Cell Biology, Evolutionary Studies, Genetics, Genomics, Medical Genetics
Keywords
sperm cells, TRP ion channel, Cold-sensitivity, molecular evolution, Ca2+-signaling, vertebrate evolution
Copyright
© 2014 Kumar Majhi et al.
Licence
This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ PrePrints) and either DOI or URL of the article must be cited.
Cite this article
Kumar Majhi R, Saha S, Kumar A, Swain N, Goswami L, Mohapatra P, Maity AA, Kumar Sahoo V, Kumar A, Goswami C. 2014. Sperm specific expression of temperature-sensitive ion channel TRPM8 correlates with vertebrate evolution. PeerJ PrePrints 2:e440v1

Abstract

Transient Receptor Potential subfamily Melastatin member 8 (TRPM8) is involved in detection of cold temperature and different noxious compounds, execute thermo- as well as chemo-sensitive responses at cellular levels. Here we explored the molecular evolution of TRPM8 by analyzing sequences from different species. We elucidate that different regions of TRPM8 had different levels of selection pressure and the 4-5th transmembrane regions remain highly conserved. Synteny analysis suggests that since vertebrate origin, TRPM8 gene is linked with SPP2, a bone morphogen. We found 16656 TRPM8 variants in 1092 human genomes with top variations are SNPs, insertions and deletions. 692 missense mutations are also mapped to human TRPM8 protein. TRPM8 expresses endogenously in sperm cells of different vertebrates ranging from fish to human. We conclude that TRPM8 has emerged during vertebrate evolution (ca 450 MYA) and sperm-specific expression has guided its molecular evolution. These understandings may have medical importance as well.

Supplemental Information