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 |
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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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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.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi035647l</identifier><identifier>PMID: 14717601</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>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</subject><ispartof>Biochemistry (Easton), 2004-01, Vol.43 (2), p.464-472</ispartof><rights>Copyright © 2004 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a349t-93867f7a09218ed9aa2d9e0c17aaa2e6688ed2cc7ec7d30d6bc3d6928af29a973</citedby><cites>FETCH-LOGICAL-a349t-93867f7a09218ed9aa2d9e0c17aaa2e6688ed2cc7ec7d30d6bc3d6928af29a973</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi035647l$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi035647l$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14717601$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Greube, Alexa</creatorcontrib><creatorcontrib>Müller, Karin</creatorcontrib><creatorcontrib>Töpfer-Petersen, Edda</creatorcontrib><creatorcontrib>Herrmann, Andreas</creatorcontrib><creatorcontrib>Müller, Peter</creatorcontrib><title>Interaction of Fibronectin Type II Proteins with Membranes: The Stallion Seminal Plasma Protein SP-1/2</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><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.</description><subject>Amino Acid Motifs</subject><subject>Androstanes - chemistry</subject><subject>Animals</subject><subject>Cattle</subject><subject>Cholestanes - chemistry</subject><subject>Cholesterol - chemistry</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Erythrocyte Membrane - chemistry</subject><subject>Fibronectins - chemistry</subject><subject>Fibronectins - metabolism</subject><subject>Fluorescence Resonance Energy Transfer</subject><subject>Horses</subject><subject>Humans</subject><subject>Liposomes</subject><subject>Male</subject><subject>Membrane Lipids - chemistry</subject><subject>Membrane Lipids - metabolism</subject><subject>Phosphatidylcholines - chemistry</subject><subject>Seminal Plasma Proteins - chemistry</subject><subject>Seminal Plasma Proteins - metabolism</subject><subject>Seminal Vesicle Secretory Proteins - chemistry</subject><subject>Spin Labels</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkE1PGzEQhq2qVQnQA38A-VIkDlts78Ze91YBIZGICEqaqzXrnRWm-5HaG0FuXPs3-0swSoALp_l65p3RS8gRZz84E_yscCwdykzVn8iADwVLMq2Hn8mAMSYToSXbI_sh3McyYyr7SvZ4priSjA-Im7Q9erC961raVXTkCt-1GOuWLjYrpJMJnfmuR9cG-uD6OzrFpvDQYvj5_-kfXdwhnfdQ1y_7c2xcCzWd1RAaeN2j81nCz8Qh-VJBHfDbLh6Q36PLxfk4ub65mpz_uk4gzXSf6DSXqlLAtOA5lhpAlBqZ5QpiilLmsSusVWhVmbJSFjYtpRY5VEKDVukBOdnqrnz3d42hN40LFus6_tytg8kZ0yrjeQRPt6D1XQgeK7PyrgG_MZyZF1_Nm6-RPd6JrosGy3dyZ2QEki3gQo-Pb3Pwf4xUqRqaxWxuLpZjNb5dTs048t-3PNhg7ru1j76FDw4_AwHgjrk</recordid><startdate>20040120</startdate><enddate>20040120</enddate><creator>Greube, Alexa</creator><creator>Müller, Karin</creator><creator>Töpfer-Petersen, Edda</creator><creator>Herrmann, Andreas</creator><creator>Müller, Peter</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20040120</creationdate><title>Interaction of Fibronectin Type II Proteins with Membranes: The Stallion Seminal Plasma Protein SP-1/2</title><author>Greube, Alexa ; 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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.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>14717601</pmid><doi>10.1021/bi035647l</doi><tpages>9</tpages></addata></record> |
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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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