Characterization of the Pharmacological-Sensitivity Profile of Neoglycoprotein-Induced Acrosome Reaction in Mouse Spermatozoa
Mammalian spermatozoa undergo the acrosome reaction (AR) in response to the interaction of a carbohydrate-recognizing molecule(s) on the sperm plasma membrane (sperm surface receptor) and its complementary glycan (ligand) moiety(ies) on the zona pellucida (ZP). Previously, we demonstrated that a hex...
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Veröffentlicht in: | Biology of reproduction 1999-09, Vol.61 (3), p.629-634 |
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creator | LOESER, C. R LYNCH, C. II TULSIANI, D. R. P |
description | Mammalian spermatozoa undergo the acrosome reaction (AR) in response to the interaction of a carbohydrate-recognizing molecule(s)
on the sperm plasma membrane (sperm surface receptor) and its complementary glycan (ligand) moiety(ies) on the zona pellucida
(ZP). Previously, we demonstrated that a hexose (mannose) or two amino sugars (glucosaminyl or galactosaminyl residues) when
covalently conjugated to a protein backbone (neoglycoproteins) mimicked the mouse ZP3 glycoprotein and induced the AR in capacitated
mouse spermatozoa (Loeser and Tulsiani, Biol Reprod 1999; 60:94â101). To elucidate the mechanism underlying sperm-neoglycoprotein
interaction and the induction of the AR, we have examined the effect of several AR blockers on neoglycoprotein-induced AR.
Our data demonstrate that two known L-type Ca 2+ channel blockers prevented the induction of the AR by three neoglycoproteins (mannose-BSA, N -acetylglucosamine-BSA, and N -acetylgalactosamine-BSA). The fact that the L-type Ca 2+ channel blockers (verapamil, diltiazem) had no inhibitory effect on sperm surface galactosyltransferase or α- d -mannosidase, two carbohydrate-recognizing enzymes thought to be sperm surface receptors, suggests that the reagents block
the AR by a mechanism other than binding to the active site of the enzymes. |
doi_str_mv | 10.1095/biolreprod61.3.629 |
format | Article |
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on the sperm plasma membrane (sperm surface receptor) and its complementary glycan (ligand) moiety(ies) on the zona pellucida
(ZP). Previously, we demonstrated that a hexose (mannose) or two amino sugars (glucosaminyl or galactosaminyl residues) when
covalently conjugated to a protein backbone (neoglycoproteins) mimicked the mouse ZP3 glycoprotein and induced the AR in capacitated
mouse spermatozoa (Loeser and Tulsiani, Biol Reprod 1999; 60:94â101). To elucidate the mechanism underlying sperm-neoglycoprotein
interaction and the induction of the AR, we have examined the effect of several AR blockers on neoglycoprotein-induced AR.
Our data demonstrate that two known L-type Ca 2+ channel blockers prevented the induction of the AR by three neoglycoproteins (mannose-BSA, N -acetylglucosamine-BSA, and N -acetylgalactosamine-BSA). The fact that the L-type Ca 2+ channel blockers (verapamil, diltiazem) had no inhibitory effect on sperm surface galactosyltransferase or α- d -mannosidase, two carbohydrate-recognizing enzymes thought to be sperm surface receptors, suggests that the reagents block
the AR by a mechanism other than binding to the active site of the enzymes.</description><identifier>ISSN: 0006-3363</identifier><identifier>EISSN: 1529-7268</identifier><identifier>DOI: 10.1095/biolreprod61.3.629</identifier><identifier>PMID: 10456838</identifier><identifier>CODEN: BIREBV</identifier><language>eng</language><publisher>Madison, WI: Society for the Study of Reproduction</publisher><subject>Acrosome Reaction - drug effects ; alpha-Mannosidase ; Animals ; Biological and medical sciences ; Calcimycin - pharmacology ; Calcium Channel Blockers - pharmacology ; Cell Membrane - enzymology ; Diltiazem - pharmacology ; Fundamental and applied biological sciences. Psychology ; Glucosyltransferases - metabolism ; Glycoproteins - pharmacology ; Ionophores - pharmacology ; Male ; Mammalian male genital system ; Mannosidases - metabolism ; Mice ; Mice, Inbred C57BL ; Morphology. Physiology ; Sperm Capacitation ; Spermatozoa - enzymology ; Verapamil - pharmacology ; Vertebrates: reproduction</subject><ispartof>Biology of reproduction, 1999-09, Vol.61 (3), p.629-634</ispartof><rights>1999 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1939252$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10456838$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>LOESER, C. R</creatorcontrib><creatorcontrib>LYNCH, C. II</creatorcontrib><creatorcontrib>TULSIANI, D. R. P</creatorcontrib><title>Characterization of the Pharmacological-Sensitivity Profile of Neoglycoprotein-Induced Acrosome Reaction in Mouse Spermatozoa</title><title>Biology of reproduction</title><addtitle>Biol Reprod</addtitle><description>Mammalian spermatozoa undergo the acrosome reaction (AR) in response to the interaction of a carbohydrate-recognizing molecule(s)
on the sperm plasma membrane (sperm surface receptor) and its complementary glycan (ligand) moiety(ies) on the zona pellucida
(ZP). Previously, we demonstrated that a hexose (mannose) or two amino sugars (glucosaminyl or galactosaminyl residues) when
covalently conjugated to a protein backbone (neoglycoproteins) mimicked the mouse ZP3 glycoprotein and induced the AR in capacitated
mouse spermatozoa (Loeser and Tulsiani, Biol Reprod 1999; 60:94â101). To elucidate the mechanism underlying sperm-neoglycoprotein
interaction and the induction of the AR, we have examined the effect of several AR blockers on neoglycoprotein-induced AR.
Our data demonstrate that two known L-type Ca 2+ channel blockers prevented the induction of the AR by three neoglycoproteins (mannose-BSA, N -acetylglucosamine-BSA, and N -acetylgalactosamine-BSA). The fact that the L-type Ca 2+ channel blockers (verapamil, diltiazem) had no inhibitory effect on sperm surface galactosyltransferase or α- d -mannosidase, two carbohydrate-recognizing enzymes thought to be sperm surface receptors, suggests that the reagents block
the AR by a mechanism other than binding to the active site of the enzymes.</description><subject>Acrosome Reaction - drug effects</subject><subject>alpha-Mannosidase</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calcimycin - pharmacology</subject><subject>Calcium Channel Blockers - pharmacology</subject><subject>Cell Membrane - enzymology</subject><subject>Diltiazem - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glucosyltransferases - metabolism</subject><subject>Glycoproteins - pharmacology</subject><subject>Ionophores - pharmacology</subject><subject>Male</subject><subject>Mammalian male genital system</subject><subject>Mannosidases - metabolism</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Morphology. Physiology</subject><subject>Sperm Capacitation</subject><subject>Spermatozoa - enzymology</subject><subject>Verapamil - pharmacology</subject><subject>Vertebrates: reproduction</subject><issn>0006-3363</issn><issn>1529-7268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkEtLxDAURoMoOj7-gAvpQt11TPOadimDL_CFj3VJ05tpJG3GJOMwgv_diCOuApfD4eRD6LDA4wJX_KwxznqYe9eKYkzHglQbaFRwUuUTIspNNMIYi5xSQXfQbghvGBeMErqNdgrMuChpOUJf0056qSJ48ymjcUPmdBY7yB7TvZfKWTczStr8GYZgovkwcZU9eqeNhR_0HtzMrpRLFRHMkN8M7UJBm50r74LrIXuCZP_xmiG7c4sA2fMckjm6Tyf30ZaWNsDB-t1Dr5cXL9Pr_Pbh6mZ6fpt3RIiYMw0NxS0mbak10Yy3nIOkWE64kqwk6buUNQKAgyjSDAxY00yU0pxhzEtJ99Dprzdlvi8gxLo3QYG1coDUVIuqqrDgLIFHa3DR9NDWc2966Vf132AJOF4DMqRZtJeDMuGfq2hFOEnYyS_WmVm3NB7q0Etrk5XWy-VSFDWtUyj9BhNEjEI</recordid><startdate>19990901</startdate><enddate>19990901</enddate><creator>LOESER, C. R</creator><creator>LYNCH, C. II</creator><creator>TULSIANI, D. R. P</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>19990901</creationdate><title>Characterization of the Pharmacological-Sensitivity Profile of Neoglycoprotein-Induced Acrosome Reaction in Mouse Spermatozoa</title><author>LOESER, C. R ; LYNCH, C. II ; TULSIANI, D. R. P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h266t-4feb30d02d8ff2f45d55ea30a75ca48272634b6ee5e616294e4bb7ccf540058a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Acrosome Reaction - drug effects</topic><topic>alpha-Mannosidase</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calcimycin - pharmacology</topic><topic>Calcium Channel Blockers - pharmacology</topic><topic>Cell Membrane - enzymology</topic><topic>Diltiazem - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glucosyltransferases - metabolism</topic><topic>Glycoproteins - pharmacology</topic><topic>Ionophores - pharmacology</topic><topic>Male</topic><topic>Mammalian male genital system</topic><topic>Mannosidases - metabolism</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Morphology. Physiology</topic><topic>Sperm Capacitation</topic><topic>Spermatozoa - enzymology</topic><topic>Verapamil - pharmacology</topic><topic>Vertebrates: reproduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>LOESER, C. R</creatorcontrib><creatorcontrib>LYNCH, C. II</creatorcontrib><creatorcontrib>TULSIANI, D. R. P</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>LOESER, C. R</au><au>LYNCH, C. II</au><au>TULSIANI, D. R. P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of the Pharmacological-Sensitivity Profile of Neoglycoprotein-Induced Acrosome Reaction in Mouse Spermatozoa</atitle><jtitle>Biology of reproduction</jtitle><addtitle>Biol Reprod</addtitle><date>1999-09-01</date><risdate>1999</risdate><volume>61</volume><issue>3</issue><spage>629</spage><epage>634</epage><pages>629-634</pages><issn>0006-3363</issn><eissn>1529-7268</eissn><coden>BIREBV</coden><abstract>Mammalian spermatozoa undergo the acrosome reaction (AR) in response to the interaction of a carbohydrate-recognizing molecule(s)
on the sperm plasma membrane (sperm surface receptor) and its complementary glycan (ligand) moiety(ies) on the zona pellucida
(ZP). Previously, we demonstrated that a hexose (mannose) or two amino sugars (glucosaminyl or galactosaminyl residues) when
covalently conjugated to a protein backbone (neoglycoproteins) mimicked the mouse ZP3 glycoprotein and induced the AR in capacitated
mouse spermatozoa (Loeser and Tulsiani, Biol Reprod 1999; 60:94â101). To elucidate the mechanism underlying sperm-neoglycoprotein
interaction and the induction of the AR, we have examined the effect of several AR blockers on neoglycoprotein-induced AR.
Our data demonstrate that two known L-type Ca 2+ channel blockers prevented the induction of the AR by three neoglycoproteins (mannose-BSA, N -acetylglucosamine-BSA, and N -acetylgalactosamine-BSA). The fact that the L-type Ca 2+ channel blockers (verapamil, diltiazem) had no inhibitory effect on sperm surface galactosyltransferase or α- d -mannosidase, two carbohydrate-recognizing enzymes thought to be sperm surface receptors, suggests that the reagents block
the AR by a mechanism other than binding to the active site of the enzymes.</abstract><cop>Madison, WI</cop><pub>Society for the Study of Reproduction</pub><pmid>10456838</pmid><doi>10.1095/biolreprod61.3.629</doi><tpages>6</tpages></addata></record> |
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source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Oxford University Press Journals All Titles (1996-Current) |
subjects | Acrosome Reaction - drug effects alpha-Mannosidase Animals Biological and medical sciences Calcimycin - pharmacology Calcium Channel Blockers - pharmacology Cell Membrane - enzymology Diltiazem - pharmacology Fundamental and applied biological sciences. Psychology Glucosyltransferases - metabolism Glycoproteins - pharmacology Ionophores - pharmacology Male Mammalian male genital system Mannosidases - metabolism Mice Mice, Inbred C57BL Morphology. Physiology Sperm Capacitation Spermatozoa - enzymology Verapamil - pharmacology Vertebrates: reproduction |
title | Characterization of the Pharmacological-Sensitivity Profile of Neoglycoprotein-Induced Acrosome Reaction in Mouse Spermatozoa |
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