Factors Influencing the Chaperone-Like Activity of Major Proteins of Mammalian Seminal Plasma, Equine HSP-1/2 and Bovine PDC-109: Effect of Membrane Binding, pH and Ionic Strength
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HSP-1/2 and PDC-109 belong to a family of fibronectin type II proteins, present in high concentrations in bovine and equine seminal plasma, respectively. These proteins act as extracellular small heat shock proteins and protect target/client proteins against various kinds of stress. They also exhibit characteristic binding to choline phospholipids present on the sperm plasma membrane and cause efflux of choline phospholipids and cholesterol, resulting in sperm capacitation. The current study demonstrates that hypersaline conditions decrease the chaperone-like activity (CLA) of HSP-1/2. On the other hand, lipoprotein aggregates formed by the binding of choline phospholipids to this protein exhibit higher CLA than HSP-1/2 alone in vitro; the increased CLA can be correlated to the increased surface hydrophobicity of the lipoprotein aggregates. Presence of cholesterol in the membrane was found to decrease such enhancement in the CLA. We have also observed that salinity of the medium affects the chaperone activity by altering the polydisperse nature of the HSP-1/2. Together these results indicate that hydrophobicity and polydispersity are important for the chaperone-like activity of HSP-1/2 and factors that can alter these properties of HSP-1/2 can modulate its CLA. Further, studies on PDC-109 show that the chaperone-like and membrane-destabilizing activities of this protein are differentially affected by change in pH.
KeywordsSeminal plasma protein Molecular chaperone Fluorescence spectroscopy Circular dichroism Aggregation assay pH switch Capacitation Membrane destabilization Hydrophobicity
This work was supported by a research grant from the Department of Science and Technology to MJS. CSK and BPS were supported by Senior Research Fellowships from the CSIR (India) and UGC (India), respectively. We thank Dr. G. Vinu (Lam Farm, Guntur, Andhra Pradesh) for providing samples of bovine semen and Dr. Sanjay K. Ravi (ICAR-National Research Centre on Equines, Bikaner, India) for providing samples of horse semen. Financial and infrastructural support from the University Grants Commission, New Delhi (through the UPE-II and CAS programmes), and the Department of Science and Technology, New Delhi (through the PURSE and FIST programmes), are gratefully acknowledged.
- Leemans B, Gadella BM, Sostaric E, Neils H, Stout TA, Hoogewijis M, Van Soom A (2014) Oviduct binding and elevated pH induce protein tyrosine phosphorylation in stallion spermatozoa. Biol Reprod 91(13):1–12Google Scholar
- Sheluho D, Ackerman SH (2001) An accessible hydrophobic surface is a key element of molecular chaperone action of Atp11p. J Biol Chem 276(43):39945–39949Google Scholar
- Swamy MJ (2004) Interaction of bovine seminal plasma proteins with model membranes and sperm plasma membranes. Curr Sci 87:203–211Google Scholar
- Voellmy R, Boellmann F (2007) Chaperone regulation of heat shock protein response. Adv Exp Med Biol 594:88–99Google Scholar