Spermine and spermidine act as chemical chaperones and enhance chaperone-like and membranolytic activities of major bovine seminal plasma protein, PDC-109

• Published in: Biochemical and biophysical research communications Vol. 493; no. 4; pp. 1418 - 1424
• Main Authors: Singh, Bhanu Pratap, Saha, Ishita, Nandi, Indrani, Swamy, Musti J.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 02.12.2017
• Subjects: Animals; Atomic force microscopy; BSP-A1/A2; Capacitation; Cattle; Cell Membrane - metabolism; Chemical chaperone; Erythrocyte Membrane - metabolism; Fructose-Bisphosphate Aldolase - antagonists & inhibitors; Fructose-Bisphosphate Aldolase - chemistry; Fructose-Bisphosphate Aldolase - metabolism; Hot Temperature - adverse effects; Humans; In Vitro Techniques; L-Lactate Dehydrogenase - antagonists & inhibitors; L-Lactate Dehydrogenase - chemistry; L-Lactate Dehydrogenase - metabolism; Male; Membrane Lipids - metabolism; Membranes, Artificial; Molecular chaperone; Molecular Chaperones - metabolism; Molecular Chaperones - pharmacology; Oxidative Stress; Polyamine; Protein Aggregates - drug effects; Protein Denaturation - drug effects; Semen - metabolism; Seminal Vesicle Secretory Proteins - metabolism; Spermidine - metabolism; Spermidine - pharmacology; Spermine - metabolism; Spermine - pharmacology; Stress, Physiological; Capacitation; Chemical chaperone; Atomic force microscopy; Polyamine; Molecular chaperone; BSP-A1/A2
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2017.09.148

The major bovine seminal plasma protein, PDC-109, binds to choline phospholipids of the sperm plasma membrane and induces an efflux of cholesterol and choline phospholipids (cholesterol efflux), which is crucial for sperm capacitation. PDC-109 also exhibits chaperone-like activity and protects target proteins against various kinds of stress. Here we show that the polyamines spermine and spermidine, present in high concentration in the seminal plasma of various mammals, increase the ability of PDC-109 to perturb membrane structure as well as its chaperone-like activity. Interestingly, spermine/spermidine alone did not perturb membrane structure but exhibited chaperone-like activity by protecting target proteins against thermal and oxidative stress. When spermine/spermidine was used along with PDC-109, the observed chaperone-like activity was considerably higher than that expected for a simple additive effect, suggesting that PDC-109 and the polyamines act in a synergistic fashion. These results indicate that at the high concentrations present in the seminal plasma spermine/spermidine exhibit a positive modulatory effect on the chaperone-like activity of PDC-109 and may also function as chemical chaperones and protect other seminal plasma proteins from various kinds of stress. [Display omitted] •Spermine (Spm) and spermidine (Spd) enhance membrane disruption by PDC-109.•Both Spm and Spd act as chemical chaperones at physiological concentration.•Spm/Spd and PDC-109 act synergistically in their chaperone-like activity (CLA).•Spm is better than Spd in enhancing membrane destabilizing and CLA of PDC-109.