Interaction of Fibronectin Type II Proteins with Membranes:  The Stallion Seminal Plasma Protein SP-1/2

Seminal plasma of mammalians contains, among others, proteins that are characterized by the fibronectin (Fn) type II module. Our knowledge about the structure and the physiological function of seminal Fn type II proteins mainly originates from studies on PDC-109, the bovine representative of this pr...

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Veröffentlicht in:Biochemistry (Easton) 2004-01, Vol.43 (2), p.464-472
Hauptverfasser: Greube, Alexa, Müller, Karin, Töpfer-Petersen, Edda, Herrmann, Andreas, Müller, Peter
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container_issue 2
container_start_page 464
container_title Biochemistry (Easton)
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creator Greube, Alexa
Müller, Karin
Töpfer-Petersen, Edda
Herrmann, Andreas
Müller, Peter
description Seminal plasma of mammalians contains, among others, proteins that are characterized by the fibronectin (Fn) type II module. Our knowledge about the structure and the physiological function of seminal Fn type II proteins mainly originates from studies on PDC-109, the bovine representative of this protein family. The present work focuses on the equine protein SP-1/2 (also named HSP-1/2) with particular emphasis on its interaction with lipid membranes by employing the intrinsic protein fluorescence and a number of spin-labeled and fluorescent lipid analogues. The results indicate that the interaction of SP-1/2 with (lipid) membranes is similar to that of PDC-109 which can be explained by homologous amino acid sequences of both proteins. Like PDC-109, SP-1/2 has a specificity for phospholipids with the phosphocholine headgroup. Upon binding to lipid vesicles, the protein intercalates into the hydrophobic membrane core, resulting in a rigidification of the lipid phase and, at higher concentration, in a perturbation of membrane structure. However, compared with PDC-109, the impact of SP-1/2 on membranes is less intense in that the degree of protein-mediated immobilization of lipids was lower. Furthermore, different to PDC-109, SP-1/2 was not able to extract lipids from human red blood cells. The data are discussed with regard to similarities and species-specific differences of the function of seminal Fn type II proteins in the genesis of sperm cells.
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subjects Amino Acid Motifs
Androstanes - chemistry
Animals
Cattle
Cholestanes - chemistry
Cholesterol - chemistry
Electron Spin Resonance Spectroscopy
Erythrocyte Membrane - chemistry
Fibronectins - chemistry
Fibronectins - metabolism
Fluorescence Resonance Energy Transfer
Horses
Humans
Liposomes
Male
Membrane Lipids - chemistry
Membrane Lipids - metabolism
Phosphatidylcholines - chemistry
Seminal Plasma Proteins - chemistry
Seminal Plasma Proteins - metabolism
Seminal Vesicle Secretory Proteins - chemistry
Spin Labels
title Interaction of Fibronectin Type II Proteins with Membranes:  The Stallion Seminal Plasma Protein SP-1/2
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