Fluorescence studies on the interaction of choline-binding domain B of the major bovine seminal plasma protein, PDC-109 with phospholipid membranes

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 12, 2009, Pages 1725-1733

  Damai, Rajani S ^a   Anbazhagan, V ^a   Rao, K Babu ^b   Swamy, Musti J ^a  

^a UNIVERSITY OF HYDERABAD   (India)

^b SRI VENKATESWARA VETERINARY UNIVERSITY   (India)

Author keywords

BSP A1 A2; Capacitation; Cholesterol efflux; Fluorescence quenching; Major protein; Red edge excitation shift

Indexed keywords

CHOLINE; DIMYRISTOYLPHOSPHATIDYLCHOLINE; LYSOPHOSPHATIDYLCHOLINE; PDC 109 PROTEIN; PHOSPHOLIPID; SEMINAL PLASMA PROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; EXCITATION; FLUORESCENCE; HYDROPHOBICITY; LIGAND BINDING; MEMBRANE BINDING; MICELLE; PHOSPHOLIPID MEMBRANE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CATTLE; CHOLINE; KINETICS; LIGANDS; LIPOSOMES; MALE; MEMBRANE LIPIDS; MICELLES; MOLECULAR SEQUENCE DATA; PHOSPHOLIPIDS; PROTEIN STRUCTURE, TERTIARY; SEMINAL VESICLE SECRETORY PROTEINS; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

BOVINAE;

EID: 73049087977     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.08.010     Document Type: Article

References (33)

1. Shivaji S., Scheit K.-H., and Bhargava P.M. Proteins of Seminal Plasma (1990), Wiley, New York
2. Yanagimachi R. Mammalian fertilization. In: Knobil E., and Neill J.D. (Eds). The Physiology of Reproduction. 2nd ed. (1994), Raven Press, New York 189-317
3. Chang M.C. Fertilizing capacity of spermatozoa deposited into the fallopian tubes. Nature 168 (1951) 697-698
4. Austin C.R. The capacitation of the mammalian sperm. Nature 170 (1952) 326
5. Harrison R.A.P. Capacitation mechanisms, and the role of capacitation as seen in eutherian mammals. Reprod. Fertil. Dev. 8 (1996) 581-596
6. Visconti P.E., Calantino-Hormer H., Moore G.D., Bailey J.L., Ning X., Fornes M., and Kopf G.S. The molecular basis of sperm capacitation. J. Androl. 19 (1998) 242-248
7. Desnoyers L., and Manjunath P. Major proteins of bovine seminal plasma exhibit novel interaction with phospholipids. J. Biol. Chem. 267 (1992) 10149-10155
8. Esch F.S., Ling N.C., Böhlen P., Ying S.Y., and Guillemin R. Primary structure of PDC-109, a major protein constituent of bovine seminal plasma. Biochem. Biophys. Res. Commun. 113 (1983) 861-867
9. Seidah N.G., Manjunath P., Rochemont J., Sairam M.R., and Cheretian M. Complete amino acid sequence of BSP-A3 from bovine seminal plasma. Homology to PDC-109 and to the collagen-binding domain of fibronectin. Biochem. J. 243 (1987) 195-203
10. Scheit K.-H., Kemme M., Aümuller G., Seitz J., Hagendorff G., and Zimmer M. The major protein of bull seminal plasma: biosynthesis and biological function. Biosci. Rep. 8 (1988) 589-608
11. Baker M.E. The PDC-109 protein from bovine seminal plasma is similar to the gelatin-binding domain of bovine fibronectin and a kringle domain of human tissue-type plasminogen activator. Biochem. Biophys. Res. Commun. 130 (1985) 1010-1014
12. Thérien I., Moreau R., and Manjunath P. Major proteins of bovine seminal plasma and high-density lipoprotein induce cholesterol efflux from epididymal sperm. Biol. Reprod. 59 (1998) 768-776
13. Moreau R., Thérien I., Lazure C., and Manjunath P. Type II domains of BSP-A1/A2 proteins: binding properties, lipid efflux, and sperm capacitation potential. Biochem. Biophys. Res. Commun. 246 (1998) 148-154
14. Wah D.A., Fernández-Tornero C., Sanz L., Romero A., and Calvete J.J. Sperm coating mechanism from the 1.8 Å crystal structure of PDC-109-phosphorylcholine complex. Structure 10 (2002) 505-514
15. Ramakrishnan M., Anbazhagan V., Pratap T.V., Marsh D., and Swamy M.J. Membrane insertion and lipid-protein interaction of bovine seminal plasma protein PDC-109 investigated by spin-label electron spin resonance spectroscopy. Biophys. J. 81 (2001) 2215-2225
16. Swamy M.J., Marsh D., Anbazhagan V., and Ramakrishnan M. Effect of cholesterol on the interaction of seminal plasma protein, PDC-109 with phosphatidylcholine membranes. FEBS Lett. 528 (2002) 230-234
17. Greube A., Müller K., Töpfer-Petersen E., Herrmann A., and Müller P. Influence of the bovine seminal plasma protein PDC-109 on the physical state of membranes. Biochemistry 40 (2001) 8326-8334
18. Müller P., Greube A., Töpfer-Petersen E., and Herrmann A. Influence of the bovine seminal plasma protein PDC-109 on cholesterol in the presence of phospholipids. Eur. Biophys. J. 31 (2002) 438-447
19. Thomas C.J., Anbazhagan V., Ramakrishnan M., Sultan N., Surolia I., and Swamy M.J. Mechanism of membrane binding by the bovine seminal plasma protein, PDC-109. A surface plasmon resonance study. Biophys. J. 84 (2003) 3037-3044
20. Anbazhagan V., and Swamy M.J. Thermodynamics of phosphorylcholine and lysophosphatidylcholine binding to the major protein of bovine seminal plasma, PDC-109. FEBS Lett. 579 (2005) 2933-2938
21. Tannert A., Kurz A., Erlemann K.-R., Müller K., Herrmann A., Schiller J., Töpfer-Petersen E., Manjunath P., and Müller P. The bovine seminal plasma protein PDC-109 extracts phosphorylcholine-containing lipids from the outer membrane. Eur. Biophys. J. 36 (2007) 461-475
22. Gasset M., Magdaleno M., and Calvete J.J. Biophysical study of the perturbation of model membrane structure caused by seminal plasma protein PDC-109. Arch. Biochem. Biophys. 250 (2000) 735-744
23. Swamy M.J. Interaction of bovine seminal plasma proteins with model membranes and sperm plasma membranes. Curr. Sci. 87 (2004) 203-211
24. Anbazhagan V., Damai R.S., Paul A., and Swamy M.J. Interaction of PDC-109, the major protein from bovine seminal plasma, with phospholipid membranes and soluble ligands investigated by fluorescence approaches. Biochim. Biophys. Acta 1784 (2008) 891-899
25. Calvette J.J., Varela P.F., Sanz L., Romero A., Mann K., and Töpfer-Petersen E. A procedure for the large-scale isolation of bovine seminal plasma proteins. Protein Expr. Purif. 8 (1996) 48-56
26. Bányai L., Trexler M., Koncz S., Gyenes M., Sipos G., and Patthy L. The collagen-binding site of type-II units of bovine seminal fluid protein PDC-109 and fibronectin. Eur. J. Biochem. 193 (1990) 801-806
27. Constantine K.L., Madrid M., Bányai L., Trexler M., Patthy L., and Llinás M. Refined solution structure and ligand-binding properties of PDC-109 domain b. A collagen-binding type II domain. J. Mol. Biol. 223 (1992) 281-298
28. Lakowicz J.R. Principles of Fluorescence Spectroscopy. 2nd ed. (1999), Kluwer Academic Publishers, New York 698 pp.
29. Lehrer S.S. Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10 (1971) 3254-3263
30. Sillen A., and Engelboroughs Y. The correct use of "average" fluorescence parameters. Photochem. Photobiol. 67 (1998) 475-486
31. Müller P., Erlemann K.R., Müller K., Calvette J.J., Töpfer-Petersen E., Marienfeld K., and Herrmann A. Biophysical characterization of the interaction of bovine seminal plasma protein PDC-109 with phospholipid vesicles. Eur. Biophys. J. 27 (1998) 33-41
32. Chattopadhyay A., and Mukherjee S. Red edge excitation of a deeply embedded membrane probe: implications in water penetration. J. Phys. Chem. B. 103 (1999) 8180-8185
33. Chattopadhyay A., and Mukherjee S. Depth-dependent solvent relaxation in membranes: wavelength-selective fluorescence as a membrane dipstick. Langmuir 15 (1999) 2142-2148