Differential expression of heat shock proteins in tissues of riverine buffaloes

MONIKA SODHI; A KISHORE; A SHARMA; U K SHANDILYA; P KUMARI; MANISHI MUKESH

doi:10.56093/ijans.v85i4.47850

Authors

MONIKA SODHI Animal Biotechnology Division, National Bureau of Animal Genetic Resources, Karnal, Haryana 132 001 India
A KISHORE Animal Biotechnology Division, National Bureau of Animal Genetic Resources, Karnal, Haryana 132 001 India
A SHARMA Animal Biotechnology Division, National Bureau of Animal Genetic Resources, Karnal, Haryana 132 001 India
U K SHANDILYA Animal Biotechnology Division, National Bureau of Animal Genetic Resources, Karnal, Haryana 132 001 India
P KUMARI Animal Biotechnology Division, National Bureau of Animal Genetic Resources, Karnal, Haryana 132 001 India
MANISHI MUKESH Animal Biotechnology Division, National Bureau of Animal Genetic Resources, Karnal, Haryana 132 001 India

https://doi.org/10.56093/ijans.v85i4.47850

Keywords:

Buffalo, Gene expression, Heat shock protein, Real-time PCR, Tissues

Abstract

In this study, an effort was made to study tissue-specific expression of some of the major heat shock protein (HSP) genes in riverine buffaloes. Samples (30) comprising 5 each of kidney, liver, muscle, heart, mammary gland and PBMCs were utilized for expression analysis under no heat shock condition. Amongst HSPs, HSP27 mRNA showed maximum expression in all the analyzed 5 tissues, viz. heart, kidney, liver, muscle and mammary gland, indicating this to be the most abundant form. However, in comparisons to tissues, HSP27 expression was low in PBMCs. On the other hand, HSP40 transcript was expressed at higher level in PBMCs while HSP60 and HSP90 transcripts were found highly expressed in mammary gland. The expression of HSP70 mRNA was highest in muscle, however HSP70 mRNA level was prominently high in all other tissues. The study helped to generate base line expression data on major HSP genes in different buffalo tissues. In future, the information presented here would be useful in evaluating the tissue specific response to any physiological and thermal stressors in buffaloes.

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References

Arrigo A P. 1990a. Tumor necrosis factor alpha induces the rapid phosphorylation of the mammalian low molecular weight heat shock protein HSP28. Molecular and Cellular Biology 10: 1276–80. DOI: https://doi.org/10.1128/mcb.10.3.1276-1280.1990

Arrigo A P. 1990b. The monovalent ionophore monensin maintains the nuclear localization of the human stress protein HSP28 during heat shock recovery. Journal of Cell Science 96: 419– 27. DOI: https://doi.org/10.1242/jcs.96.3.419

Benndorf R and Welsh M J. 2004. Shocking degeneration. Nature Genetics 36: 547–48. DOI: https://doi.org/10.1038/ng0604-547

Blechinger S R, Evans T G, Tang P T, Kuwada J Y, Warren J T and Jr Krone P H. 2002. The heat-inducible zebrafish HSP70 gene is expressed during normal lens development under nonstress conditions. Mechanisms of Development 112: 213–15. DOI: https://doi.org/10.1016/S0925-4773(01)00652-9

Brown M A, Zhu L, Schmidt C and Tucker P W. 2007. From signal transduction to cell transformation. Biochemical and Biophysical Research Communications 363: 241–46. DOI: https://doi.org/10.1016/j.bbrc.2007.08.054

Christians E S, Zhou Q, Renard J and Benjamin I J. 2003. Heat shock proteins in mammalian development. Seminars in Cell and Developmental Biology 14: 283–90. DOI: https://doi.org/10.1016/j.semcdb.2003.09.021

Collier R J, Collier J L, Rhoads R P and Baumgard L H. 2008. Genes involved in the bovine heat stress response. Journal of Dairy Science 91: 445–54. DOI: https://doi.org/10.3168/jds.2007-0540

Concannon C G, Gorman A M and Samali A. 2003. On the role of Hsp27 in regulating apoptosis. Apoptosis 8: 61–70. DOI: https://doi.org/10.1023/A:1021601103096

Dillmann W H. 1999. Heat shock proteins and protection against ischemic injury. Infectious Diseases in Obstetrics and Gynecology 7: 55–57. DOI: https://doi.org/10.1155/S1064744999000113

Foster J and Brown I. 1996. Basal expression of stress-inducible HSP70 mRNA detected in hippocampal and cortical neurons of normal rabbit brain. Brain Research 724: 73–83. DOI: https://doi.org/10.1016/0006-8993(96)00266-1

Georgopoulos C and Welch W J. 1993. Role of the major heat shock proteins as molecular chaperones. Annual Review of Cell and Developmental Biology 9: 601–34. DOI: https://doi.org/10.1146/annurev.cb.09.110193.003125

Habich C and Burkart V. 2007. Heat shock protein 60: regulatory role on innate immune cells. Cellular and Molecular Life Sciences 64: 742–51. DOI: https://doi.org/10.1007/s00018-007-6413-7

Hartl F U and Hayer-Hartl M. 2002. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 29: 1852–58. DOI: https://doi.org/10.1126/science.1068408

Hickey E, Brandon S E, Potter R, Stein G, Stein J and Weber L A. 1986. Sequence and organization of genes encoding the human 27 kDa heat shock protein. Nucleic Acids Research 14: 4127– 45. DOI: https://doi.org/10.1093/nar/14.10.4127

Kregel K C. 2002. Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance. Journal of Applied Physiology 92: 2177–86. DOI: https://doi.org/10.1152/japplphysiol.01267.2001

Lacetera N, Bernabucci U, Scalia D, Basirico P and Nardone A. 2006. Heat stress elicits different responses in peripheral blood mononuclear cells from Brown Swiss and Holstein cows. Journal of Dairy Science 89: 4606–12. DOI: https://doi.org/10.3168/jds.S0022-0302(06)72510-3

Li Z and Srivastava P. 2004. Heat-shock proteins. Current Protocol in Immunology. Appendix 1: Appendix 1T. doi: 10.1002/ 0471142735.ima01ts58. DOI: https://doi.org/10.1002/0471142735.ima01ts58

Lindquist S and Craig E A. 1988. The heat-shock proteins. Annual Review of Genetics 22: 631–77. DOI: https://doi.org/10.1146/annurev.ge.22.120188.003215

Mao L, Bryantsev A L, Chechenova M B and Shelden E A. 2005. Cloning, characterization, and heat stress-induced redistribution of a protein homologous to human HSP27 in the zebrafish Danio rerio. Experimental Cell Research 306: 230–41. DOI: https://doi.org/10.1016/j.yexcr.2005.02.007

Marvin M, O’Rourke D, Kurihara T, Juliano C E, Harrison K L and Hutson L D. 2008. Developmental expression patterns of the zebrafish small heat shock proteins. Developmental Dynamics 237: 454–63. DOI: https://doi.org/10.1002/dvdy.21414

McComb M A and Spurlock M E. 1997. Expression of stress proteins in porcine tissues: developmental changes and effect of immunological challenge. Journal of Animal Science 75: 195–201. DOI: https://doi.org/10.2527/1997.751195x

Meistertzheim A L, Lejart M, Le Goïc N and Thébault M T. 2009. Sex-, gametogenesis, and tidal height-related differences in levels of HSP70 and metallothioneins in the Pacific oyster Crassostrea gigas. Comparative biochemistry and physiology Part A: Molecular and Integrative Physiology 152: 234–39. DOI: https://doi.org/10.1016/j.cbpa.2008.10.004

Moran D S, Eli-Berchoer L, Heled Y, Mendel L, Schocina M and Horowitz M. 2006. Heat tolerance: Does gene transcription contribute? Journal of Applied Physiology 100: 1370–76. DOI: https://doi.org/10.1152/japplphysiol.01261.2005

Morimoto R I. 1998. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes and Development 12: 3788–96. DOI: https://doi.org/10.1101/gad.12.24.3788

Multhoff G. 2007. Heat shock protein 70 (Hsp70): membrane location, export and immunological relevance. Methods 43 (3): 229–37. DOI: https://doi.org/10.1016/j.ymeth.2007.06.006

Oksala N K J, Laaksonen D E, Lappalainen J, Khanna S, Nakao C, Hänninen O, Sen C K and Atalay M. 2006. Heat shock protein 60 response to exercise in diabetes. Effects of α-lipoic acid supplementation. Journal of Diabetes Complications 20: 257–61. DOI: https://doi.org/10.1016/j.jdiacomp.2005.07.008

Poltronieri C, Maccatrozzo L, Simontacchi C, Bertotto D, Funkenstein B, Patruno M and Radaelli G. 2007. Quantitative RT-PCR analysis and immunohistochemical localization of HSP70 in sea bass Dicentrarchus labrax exposed to transport stress. European Journal of Histochemistry 51: 125–35.

Pratt W B and Toft D O. 2003. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Experimental Biology and Medicine 228: 111–33. DOI: https://doi.org/10.1177/153537020322800201

Preville X, Mehlen Ñ, Fabre-Jonca Í, Chaufour S, Kretz-Remy C, Michel μ R and Arrigo A P. 1996. Biochemical and immunofluorescence analysis of the constitutively expressed HSP27 stress protein in monkey CV-1 cells. Journal of Biosciences 21: 221–34. DOI: https://doi.org/10.1007/BF02703110

Rane M J, Pan Y, Singh S, Powell DW, Wu R, Cummins T, Chen Q, McLeish K.R and Klein J B 2003. Heat shock protein 27 controls apoptosis by regulating Akt activation. Journal of Biological Chemistry 278: 27828–35. DOI: https://doi.org/10.1074/jbc.M303417200

Sarge K D and Culle K E. 1997. Regulation of hsp expression during rodent spermatogenesis. Cellular and Molecular Life Sciences 53: 191–97. DOI: https://doi.org/10.1007/PL00000591

Scott M A, Locke M, Buck L T. 2003. Tissue-specific expression of inducible and constitutive Hsp70 isoforms in the western painted turtle. Journal of Experimental Biology 206: 303–11. DOI: https://doi.org/10.1242/jeb.00107

Srivastava P. 2002. Roles of heat-shock proteins in innate and adaptive immunity. Nature Reviews Immunology 2: 185–41. DOI: https://doi.org/10.1038/nri749

Tucker N R, Ustyugov A, Bryantsev A L, Konkel M E and Shelden E A. 2009. Hsp27 is persistently expressed in zebrafish skeletal and cardiac muscle tissues but dispensable for their morphogenesis. Cell Stress Chaperones 14: 521–33. Tukaj S, Kotlarz A, Jozwik A, Smolenska Z, Bryl E, Witkowski J M and Lipinska B. 2010. Hsp40 proteins modulate humoral and cellular immune response in rheumatoid arthritis patients. Cell Stress Chaperones 15: 555–66. DOI: https://doi.org/10.1007/s12192-009-0105-1

Velázquez M M, Alfaro N S, Salvetti N R, Stangaferro M L, Rey F, Panzani C G and Ortega H H. 2011. Levels of heat shock protein transcripts in normal follicles and ovarian follicular cysts. Reproductive Biology 11: 276–83. DOI: https://doi.org/10.1016/S1642-431X(12)60072-2

Vidyasagar A, Reese S, Acun Z, Hullett D and Djamal A. 2008. HSP27 is involved in the pathogenesis of kidney tubulointerstitial fibrosis. American Journal of Physiology - Renal Physiology 295: F707–F716. DOI: https://doi.org/10.1152/ajprenal.90240.2008

Vidyasagar A, Wilson N A and Djamali A. 2012. Heat shock protein 27 (HSP27): biomarker of disease and therapeutic target. Fibrogenesis Tissue Repair 5, 7. doi: 10.1186/1755- 1536–5–7. DOI: https://doi.org/10.1186/1755-1536-5-7

Watanabe A, Miyamoto T, Katoh N and Takahashi Y. 1997. Effect of stages of lactation on the concentration of a 90-kilodalton heat shock protein in bovine mammary tissue. Journal of Dairy Science 80: 2372–79. DOI: https://doi.org/10.3168/jds.S0022-0302(97)76188-5

Welch W J. 1990. The mammalian stress response: cell physiology and biochemistry of stress proteins. Stress Proteins in Biology and Medicine. pp. 223–78. (Eds) Morimoto R I, Tissieres A and Georgopoulos C. 1, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.

Yang Y X, Sun X F, Cheng A L, Zhang G Y, Yi H, Sun Y, Hu H D, Hu P, Ye F, Chen Z C and Xiao Z Q. 2009. Increased expression of HSP27 linked to vincristine resistance in human gastric cancer cell line. Journal of Cancer Research and Clinical Oncology 135: 181–89. DOI: https://doi.org/10.1007/s00432-008-0460-9

Zhang D, Ke L, Mackovicova K, Van Der Want J J, Sibon O C, Tanguay R M, Morrow G, Henning R H, Kampinga H H and Brundel B J. 2011. Effects of different small HSPB members on contractile dysfunction and structural changes in a Drosophila melanogaster model for Atrial Fibrillation. Journal of Molecular and Cellular Cardiology 51: 381–89. DOI: https://doi.org/10.1016/j.yjmcc.2011.06.008

Zhang H and Burrows F. 2004. Targeting multiple signal transduction pathways through inhibition of Hsp90. Journal of Molecular Medicine 82: 488–99. DOI: https://doi.org/10.1007/s00109-004-0549-9

Zhao Q, Wang J, Levichkin I V, Stasinopoulos S, Ryan M T and Hoogenraad N J. 2002. A mitochondrial specific stress response in mammalian cells. EMBO Journal 21: 4411–19. DOI: https://doi.org/10.1093/emboj/cdf445