title: Influence of the bovine seminal plasma protein PDC-109 on the physical state of membranes.
abstract: PDC-109 is the main component of bovine seminal plasma and has been suggested to play an important role in the genesis of bovine sperm cells. Here, the effect of binding of PDC-109 to membranes on the structure and physical properties of the lipid phase was investigated. For that, ESR measurements were undertaken on model membranes (lipid vesicles) and on biological membranes (epididymal spermatozoa) by employing various spin-labeled phospholipids. We found that PDC-109 alters the membrane structure of lipid vesicles as well as of bovine epididymal spermatozoa in that the mobility of spin-labeled phospholipids was reduced in the presence of the protein. This immobilizing effect of the protein was not restricted to analogues of phosphatidylcholine but was also detected with spin-labeled phosphatidylethanolamine. However, the extent of immobilization was lower for phosphatidylethanolamine compared with phosphatidylcholine, supporting the lipid headgroup specificity of the protein. Besides phospholipid headgroups, the physical state of membrane lipids is also important for the interaction of PDC-109 with membranes, in that, e.g., the immobilizing effect of the protein on labeled lipids was larger in membranes above the phase transition temperature compared with the effect below this temperature. The results are of relevance for understanding the physiological role of PDC-109 in the genesis of sperm cells.
authors.affiliation: Mathematisch-Naturwissenschaftliche Fakultät I, Institut für Biologie, Humboldt-Universität zu Berlin, Invalidenstrasse 43, D-10115 Berlin, Germany.
authors.forename: A
authors.initials: A
authors.lastname: Greube
authors.forename: K
authors.initials: K
authors.lastname: Müller
authors.forename: E
authors.initials: E
authors.lastname: Töpfer-Petersen
authors.forename: A
authors.initials: A
authors.lastname: Herrmann
authors.forename: P
authors.initials: P
authors.lastname: Müller
mesh_terms: D000818:Animals; D002417:Cattle; D002462:Cell Membrane / Q000737:chemistry / Q000502:physiology; D004578:Electron Spin Resonance Spectroscopy; D004822:Epididymis / Q000737:chemistry / Q000166:cytology / Q000502:physiology; D007700:Kinetics; D008081:Liposomes / Q000737:chemistry; D008297:Male; D008567:Membranes, Artificial; D010063:Ovum / Q000737:chemistry; D010713:Phosphatidylcholines / Q000737:chemistry; D010714:Phosphatidylethanolamines / Q000737:chemistry; D010743:Phospholipids / Q000737:chemistry; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000502:physiology; D029589:Seminal Plasma Proteins; D013075:Sperm Capacitation / Q000502:physiology; D013094:Spermatozoa / Q000737:chemistry / Q000502:physiology; D013113:Spin Labels; D013329:Structure-Activity Relationship
chemical_list: D008081:Liposomes; D008567:Membranes, Artificial; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; D010743:Phospholipids; D011506:Proteins; D029589:Seminal Plasma Proteins; D013113:Spin Labels