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Interaction of fibronectin type II proteins with membranes: the stallion seminal plasma protein SP-1/2.
Abstract: 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.
Publication Date: 2004-01-14 PubMed ID: 14717601DOI: 10.1021/bi035647lGoogle Scholar: Lookup The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This research article investigates the interaction between a specific protein found in stallion seminal plasma, known as SP-1/2, and lipid membranes. The findings suggest that SP-1/2 behaves similarly to its bovine counterpart PDC-109, but with a lesser impact on membranes.
Background of the Research
- The study revolves around proteins that are characterized by the fibronectin (Fn) type II module, which are present in the seminal plasma of mammals.
- Earlier knowledge about these proteins primarily comes from studies on PDC-109, a bovine protein equivalent.
- The current work focusses on the equine protein SP-1/2 and its interaction with lipid membranes.
Methods and Techniques
- Fluorescence techniques using the intrinsic protein fluorescence and a number of spin-labeled and fluorescent lipid analogues were used to study the interaction of SP-1/2 with lipid membranes.
Findings of the Research
- The study found that the interaction of SP-1/2 with lipid membranes akin to that of PDC-109, which could be attributed to the homologous amino acid sequences of both proteins.
- SP-1/2, like PDC-109, shows selectivity for phospholipids with a phosphocholine headgroup.
- Upon binding to lipid vesicles, SP-1/2 penetrates into the hydrophobic core of the membrane, leading to a stiffening of the lipid phase and disturbing the membrane structure at higher concentrations.
Comparisons and Differences with PDC-109
- Compared to PDC-109, SP-1/2’s impact on membranes is less intense, causing a lower degree of lipid immobilization.
- Another key difference is that SP-1/2 could not extract lipids from human red blood cells, unlike PDC-109.
Conclusions of the Study
- The research concludes with a discussion of the similarities and species-specific differences between the function of seminal Fn type II proteins in the development of sperm cells.
- The study enhances our understanding of the role of seminal Fn type II proteins and their interaction with lipid membranes in reproduction.
Cite This Article
APA
Greube A, Müller K, Töpfer-Petersen E, Herrmann A, Müller P.
(2004).
Interaction of fibronectin type II proteins with membranes: the stallion seminal plasma protein SP-1/2.
Biochemistry, 43(2), 464-472.
https://doi.org/10.1021/bi035647l Publication
Researcher Affiliations
- Institut für Biologie, Mathematisch-Naturwissenschaftliche Fakultät I, Humboldt-Universität zu Berlin, Invalidenstrasse 43, D-10115 Berlin, Germany.
MeSH Terms
- 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
Citations
This article has been cited 2 times.- Sudheer Kumar C, Swamy MJ. Modulation of chaperone-like and membranolytic activities of major horse seminal plasma protein HSP-1/2 by L-carnitine. J Biosci 2017 Sep;42(3):469-479.
- Tannert A, Kurz A, Erlemann KR, Müller K, Herrmann A, Schiller J, Töpfer-Petersen E, Manjunath P, Müller P. The bovine seminal plasma protein PDC-109 extracts phosphorylcholine-containing lipids from the outer membrane leaflet. Eur Biophys J 2007 Apr;36(4-5):461-75.
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