Purification and characterization of a human follicular fluid lipid transfer protein that stimulates human sperm capacitation
Identification of the mechanisms responsible for sperm capacitation has been an active area of research for nearly four decades. Changes in the lipid composition of the sperm membrane is one of the biochemical events that occurs during sperm capacitation. We have been studying physiological effector...
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| Veröffentlicht in: | Biology of reproduction 1992-12, Vol.47 (6), p.1126-1133 |
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| container_title | Biology of reproduction |
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| creator | RAVNIK, S. E ZARUTSKIE, P. W MULLER, C. H |
| description | Identification of the mechanisms responsible for sperm capacitation has been an active area of research for nearly four decades.
Changes in the lipid composition of the sperm membrane is one of the biochemical events that occurs during sperm capacitation.
We have been studying physiological effectors of some of these changes and have identified lipid transfer activity in fractions
of human follicular fluid that stimulates sperm penetration of zona-free hamster oocytes. We report here the purification
of a lipid transfer protein by sequential chromatography from human follicular fluid. This protein was purified greater than
20,000-fold for lipid transfer activity and greater than 28,000-fold for sperm penetration-inducing activity. This 64,000
molecular weight protein has a pI of approximately 5.0 and shares physicochemical characteristics with the plasma lipid transfer
protein, LTP-I. Antibodies to LTP-I also recognize this protein and depletion of LTP-I from human follicular fluid by immunoaffinity
chromatography renders the follicular fluid incapable of stimulating sperm penetration. We conclude that purified LTP-I is
able to stimulate human sperm capacitation and that LTP-I is a molecule responsible for this stimulation in follicular fluid. |
| doi_str_mv | 10.1095/biolreprod47.6.1126 |
| format | Article |
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Changes in the lipid composition of the sperm membrane is one of the biochemical events that occurs during sperm capacitation.
We have been studying physiological effectors of some of these changes and have identified lipid transfer activity in fractions
of human follicular fluid that stimulates sperm penetration of zona-free hamster oocytes. We report here the purification
of a lipid transfer protein by sequential chromatography from human follicular fluid. This protein was purified greater than
20,000-fold for lipid transfer activity and greater than 28,000-fold for sperm penetration-inducing activity. This 64,000
molecular weight protein has a pI of approximately 5.0 and shares physicochemical characteristics with the plasma lipid transfer
protein, LTP-I. Antibodies to LTP-I also recognize this protein and depletion of LTP-I from human follicular fluid by immunoaffinity
chromatography renders the follicular fluid incapable of stimulating sperm penetration. We conclude that purified LTP-I is
able to stimulate human sperm capacitation and that LTP-I is a molecule responsible for this stimulation in follicular fluid.</description><identifier>ISSN: 0006-3363</identifier><identifier>EISSN: 1529-7268</identifier><identifier>DOI: 10.1095/biolreprod47.6.1126</identifier><identifier>PMID: 1493178</identifier><identifier>CODEN: BIREBV</identifier><language>eng</language><publisher>Madison, WI: Society for the Study of Reproduction</publisher><subject>Antibodies, Monoclonal - pharmacology ; Biological and medical sciences ; Carrier Proteins - biosynthesis ; Carrier Proteins - immunology ; Carrier Proteins - pharmacology ; Chromatography ; Electrophoresis, Polyacrylamide Gel ; Female ; Follicular Fluid - chemistry ; Fundamental and applied biological sciences. Psychology ; Humans ; Immunoblotting ; Male ; Mammalian male genital system ; Morphology. Physiology ; Sperm Capacitation - physiology ; Vertebrates: reproduction</subject><ispartof>Biology of reproduction, 1992-12, Vol.47 (6), p.1126-1133</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4460970$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1493178$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>RAVNIK, S. E</creatorcontrib><creatorcontrib>ZARUTSKIE, P. W</creatorcontrib><creatorcontrib>MULLER, C. H</creatorcontrib><title>Purification and characterization of a human follicular fluid lipid transfer protein that stimulates human sperm capacitation</title><title>Biology of reproduction</title><addtitle>Biol Reprod</addtitle><description>Identification of the mechanisms responsible for sperm capacitation has been an active area of research for nearly four decades.
Changes in the lipid composition of the sperm membrane is one of the biochemical events that occurs during sperm capacitation.
We have been studying physiological effectors of some of these changes and have identified lipid transfer activity in fractions
of human follicular fluid that stimulates sperm penetration of zona-free hamster oocytes. We report here the purification
of a lipid transfer protein by sequential chromatography from human follicular fluid. This protein was purified greater than
20,000-fold for lipid transfer activity and greater than 28,000-fold for sperm penetration-inducing activity. This 64,000
molecular weight protein has a pI of approximately 5.0 and shares physicochemical characteristics with the plasma lipid transfer
protein, LTP-I. Antibodies to LTP-I also recognize this protein and depletion of LTP-I from human follicular fluid by immunoaffinity
chromatography renders the follicular fluid incapable of stimulating sperm penetration. We conclude that purified LTP-I is
able to stimulate human sperm capacitation and that LTP-I is a molecule responsible for this stimulation in follicular fluid.</description><subject>Antibodies, Monoclonal - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - biosynthesis</subject><subject>Carrier Proteins - immunology</subject><subject>Carrier Proteins - pharmacology</subject><subject>Chromatography</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Female</subject><subject>Follicular Fluid - chemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>Male</subject><subject>Mammalian male genital system</subject><subject>Morphology. Physiology</subject><subject>Sperm Capacitation - physiology</subject><subject>Vertebrates: reproduction</subject><issn>0006-3363</issn><issn>1529-7268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFUctuFTEMjRCovbT9AlQpC9TdXJLJa2aJqhaQKsEC1iPnxaTKPJpkdAUS_06gI9jYln18fGwj9IaSIyW9eKfDEpNb02K5Osojpa18gQ5UtH2jWtm9RAdCiGwYk-wcvc75kRDKWcvO0BnlPaOqO6BfX7YUfDBQwjJjmC02IyQwxaXw8zm5eAx43CaYsV9iDGaLkLCPW7A4hrXakmDO3iVctRQXZlxGKDiXMFVocXnvzqtLEzawggnlL_cleuUhZne1-wv07f7u6-3H5uHzh0-37x-asZWyNFJ4TpTQXHbKt14L6nvb6Z7pVlheYy41b3kvrBdcE0ls7zkjzoJUuusUu0A3z7xV4NPmchmmkI2LEWa3bHlQjAsuqKzA6x246cnZYU1hgvRj2O9V62_3OmQD0dfFTcj_YJxL0ivyf94Yvo-nkNyQJ4ixkrLhdDpxNcjhz7vYbwVsjBc</recordid><startdate>19921201</startdate><enddate>19921201</enddate><creator>RAVNIK, S. E</creator><creator>ZARUTSKIE, P. W</creator><creator>MULLER, C. H</creator><general>Society for the Study of Reproduction</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19921201</creationdate><title>Purification and characterization of a human follicular fluid lipid transfer protein that stimulates human sperm capacitation</title><author>RAVNIK, S. E ; ZARUTSKIE, P. W ; MULLER, C. H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h266t-65f4075b4687f2fb51f9d8b93b25d4f9d46b42495df54b060d9f430eda67b8873</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Antibodies, Monoclonal - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Carrier Proteins - biosynthesis</topic><topic>Carrier Proteins - immunology</topic><topic>Carrier Proteins - pharmacology</topic><topic>Chromatography</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Female</topic><topic>Follicular Fluid - chemistry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Immunoblotting</topic><topic>Male</topic><topic>Mammalian male genital system</topic><topic>Morphology. Physiology</topic><topic>Sperm Capacitation - physiology</topic><topic>Vertebrates: reproduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>RAVNIK, S. E</creatorcontrib><creatorcontrib>ZARUTSKIE, P. W</creatorcontrib><creatorcontrib>MULLER, C. H</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Biology of reproduction</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>RAVNIK, S. E</au><au>ZARUTSKIE, P. W</au><au>MULLER, C. H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of a human follicular fluid lipid transfer protein that stimulates human sperm capacitation</atitle><jtitle>Biology of reproduction</jtitle><addtitle>Biol Reprod</addtitle><date>1992-12-01</date><risdate>1992</risdate><volume>47</volume><issue>6</issue><spage>1126</spage><epage>1133</epage><pages>1126-1133</pages><issn>0006-3363</issn><eissn>1529-7268</eissn><coden>BIREBV</coden><abstract>Identification of the mechanisms responsible for sperm capacitation has been an active area of research for nearly four decades.
Changes in the lipid composition of the sperm membrane is one of the biochemical events that occurs during sperm capacitation.
We have been studying physiological effectors of some of these changes and have identified lipid transfer activity in fractions
of human follicular fluid that stimulates sperm penetration of zona-free hamster oocytes. We report here the purification
of a lipid transfer protein by sequential chromatography from human follicular fluid. This protein was purified greater than
20,000-fold for lipid transfer activity and greater than 28,000-fold for sperm penetration-inducing activity. This 64,000
molecular weight protein has a pI of approximately 5.0 and shares physicochemical characteristics with the plasma lipid transfer
protein, LTP-I. Antibodies to LTP-I also recognize this protein and depletion of LTP-I from human follicular fluid by immunoaffinity
chromatography renders the follicular fluid incapable of stimulating sperm penetration. We conclude that purified LTP-I is
able to stimulate human sperm capacitation and that LTP-I is a molecule responsible for this stimulation in follicular fluid.</abstract><cop>Madison, WI</cop><pub>Society for the Study of Reproduction</pub><pmid>1493178</pmid><doi>10.1095/biolreprod47.6.1126</doi><tpages>8</tpages></addata></record> |
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| ispartof | Biology of reproduction, 1992-12, Vol.47 (6), p.1126-1133 |
| issn | 0006-3363 1529-7268 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals |
| subjects | Antibodies, Monoclonal - pharmacology Biological and medical sciences Carrier Proteins - biosynthesis Carrier Proteins - immunology Carrier Proteins - pharmacology Chromatography Electrophoresis, Polyacrylamide Gel Female Follicular Fluid - chemistry Fundamental and applied biological sciences. Psychology Humans Immunoblotting Male Mammalian male genital system Morphology. Physiology Sperm Capacitation - physiology Vertebrates: reproduction |
| title | Purification and characterization of a human follicular fluid lipid transfer protein that stimulates human sperm capacitation |
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