Alterations of branching and differential expression of sialic acid on alpha-1-acid glycoprotein in human seminal plasma
Background: The degree of branching and types of fucosylation of glycans on α 1-acid glycoprotein (AGP) have been found to be associated with α 1-acid glycoprotein concentrations in human seminal plasma. The glycosylation pattern of α 1-acid glycoprotein in seminal plasma obtained from men living in...
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| Veröffentlicht in: | Clinica chimica acta 2003-05, Vol.331 (1), p.87-95 |
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| creator | Kratz, Ewa Poland, Dennis C.W. van Dijk, Willem Kątnik-Prastowska, Iwona |
| description | Background: The degree of branching and types of fucosylation of glycans on α
1-acid glycoprotein (AGP) have been found to be associated with α
1-acid glycoprotein concentrations in human seminal plasma. The glycosylation pattern of α
1-acid glycoprotein in seminal plasma obtained from men living in infertile couples can undergo alterations in relation to sperm analysis and/or α
1-acid glycoprotein concentrations.
Methods: The glycosylation of α
1-acid glycoprotein was studied upon the reactivity with specific lectins by crossed affinity immunoelectrophoresis (concanavalin A), and by glycoprotein lectin immunosorbent assay (
Maackia amurensis and
Sambucus nigra lectins), as well as high pH anion-exchange chromatography with pulsed amperometric detection.
Results: Nonsignificant differences in α
1-acid glycoprotein glycan branching and degree of its sialylation were observed among the AGP derived from seminal plasmas in relation to spermiogram and sperm morphology. However, significant concentration-dependent differences were found in extent of branching and type of sialylation.
Conclusions: The presence in seminal plasma of high concentrations of aberrantly glycosylated AGP molecules might be indicative for a chronic inflammatory condition in the reproductive tract, and can be used as additional tool to subdivide the seminal plasmas of men living in infertile couples. |
| doi_str_mv | 10.1016/S0009-8981(03)00084-6 |
| format | Article |
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1-acid glycoprotein (AGP) have been found to be associated with α
1-acid glycoprotein concentrations in human seminal plasma. The glycosylation pattern of α
1-acid glycoprotein in seminal plasma obtained from men living in infertile couples can undergo alterations in relation to sperm analysis and/or α
1-acid glycoprotein concentrations.
Methods: The glycosylation of α
1-acid glycoprotein was studied upon the reactivity with specific lectins by crossed affinity immunoelectrophoresis (concanavalin A), and by glycoprotein lectin immunosorbent assay (
Maackia amurensis and
Sambucus nigra lectins), as well as high pH anion-exchange chromatography with pulsed amperometric detection.
Results: Nonsignificant differences in α
1-acid glycoprotein glycan branching and degree of its sialylation were observed among the AGP derived from seminal plasmas in relation to spermiogram and sperm morphology. However, significant concentration-dependent differences were found in extent of branching and type of sialylation.
Conclusions: The presence in seminal plasma of high concentrations of aberrantly glycosylated AGP molecules might be indicative for a chronic inflammatory condition in the reproductive tract, and can be used as additional tool to subdivide the seminal plasmas of men living in infertile couples.</description><identifier>ISSN: 0009-8981</identifier><identifier>EISSN: 1873-3492</identifier><identifier>DOI: 10.1016/S0009-8981(03)00084-6</identifier><identifier>PMID: 12691868</identifier><identifier>CODEN: CCATAR</identifier><language>eng</language><publisher>Shannon: Elsevier B.V</publisher><subject>Adult ; Alpha-1-acid glycoprotein ; Biological and medical sciences ; Carbohydrate Conformation ; Chromatography, Ion Exchange - methods ; Genital system. Mammary gland ; Glycosylation ; Humans ; Immunoelectrophoresis, Two-Dimensional ; Investigative techniques, diagnostic techniques (general aspects) ; Lectins - chemistry ; Male ; Medical sciences ; Middle Aged ; Orosomucoid - chemistry ; Orosomucoid - metabolism ; Pathology. Cytology. Biochemistry. Spectrometry. Miscellaneous investigative techniques ; Semen - chemistry ; Semen - metabolism ; Seminal plasma ; Sialic Acids - biosynthesis ; Sialic Acids - chemistry ; Sialylation</subject><ispartof>Clinica chimica acta, 2003-05, Vol.331 (1), p.87-95</ispartof><rights>2003 Elsevier Science B.V.</rights><rights>2003 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c459t-d9c5670d7839bc463fcdaa840f3c64992f5cc7b281a595978fb24fe1619fb5103</citedby><cites>FETCH-LOGICAL-c459t-d9c5670d7839bc463fcdaa840f3c64992f5cc7b281a595978fb24fe1619fb5103</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0009-8981(03)00084-6$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14700159$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12691868$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kratz, Ewa</creatorcontrib><creatorcontrib>Poland, Dennis C.W.</creatorcontrib><creatorcontrib>van Dijk, Willem</creatorcontrib><creatorcontrib>Kątnik-Prastowska, Iwona</creatorcontrib><title>Alterations of branching and differential expression of sialic acid on alpha-1-acid glycoprotein in human seminal plasma</title><title>Clinica chimica acta</title><addtitle>Clin Chim Acta</addtitle><description>Background: The degree of branching and types of fucosylation of glycans on α
1-acid glycoprotein (AGP) have been found to be associated with α
1-acid glycoprotein concentrations in human seminal plasma. The glycosylation pattern of α
1-acid glycoprotein in seminal plasma obtained from men living in infertile couples can undergo alterations in relation to sperm analysis and/or α
1-acid glycoprotein concentrations.
Methods: The glycosylation of α
1-acid glycoprotein was studied upon the reactivity with specific lectins by crossed affinity immunoelectrophoresis (concanavalin A), and by glycoprotein lectin immunosorbent assay (
Maackia amurensis and
Sambucus nigra lectins), as well as high pH anion-exchange chromatography with pulsed amperometric detection.
Results: Nonsignificant differences in α
1-acid glycoprotein glycan branching and degree of its sialylation were observed among the AGP derived from seminal plasmas in relation to spermiogram and sperm morphology. However, significant concentration-dependent differences were found in extent of branching and type of sialylation.
Conclusions: The presence in seminal plasma of high concentrations of aberrantly glycosylated AGP molecules might be indicative for a chronic inflammatory condition in the reproductive tract, and can be used as additional tool to subdivide the seminal plasmas of men living in infertile couples.</description><subject>Adult</subject><subject>Alpha-1-acid glycoprotein</subject><subject>Biological and medical sciences</subject><subject>Carbohydrate Conformation</subject><subject>Chromatography, Ion Exchange - methods</subject><subject>Genital system. Mammary gland</subject><subject>Glycosylation</subject><subject>Humans</subject><subject>Immunoelectrophoresis, Two-Dimensional</subject><subject>Investigative techniques, diagnostic techniques (general aspects)</subject><subject>Lectins - chemistry</subject><subject>Male</subject><subject>Medical sciences</subject><subject>Middle Aged</subject><subject>Orosomucoid - chemistry</subject><subject>Orosomucoid - metabolism</subject><subject>Pathology. Cytology. Biochemistry. Spectrometry. Miscellaneous investigative techniques</subject><subject>Semen - chemistry</subject><subject>Semen - metabolism</subject><subject>Seminal plasma</subject><subject>Sialic Acids - biosynthesis</subject><subject>Sialic Acids - chemistry</subject><subject>Sialylation</subject><issn>0009-8981</issn><issn>1873-3492</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1rFTEUhoMo9rb6E5RslLoYTSaZTLIqpfgFBRfqOpxJTnojM5kxmSvtvzf3A7sUAuE9POeDh5BXnL3njKsP3xljptFG80sm3tWgZaOekA3XvWiENO1TsvmHnJHzUn7VKJniz8kZb5XhWukNub8eV8ywxjkVOgc6ZEhuG9MdheSpjyFgxrRGGCneLxlLqeQeLLUUHQUXPa0VGJctNLw55Lvxwc1LnleMida33U2QaMEppjpnGaFM8II8CzAWfHn6L8jPTx9_3Hxpbr99_npzfds42Zm18cZ1qme-18IMTioRnAfQkgXhlDSmDZ1z_dBqDp3pTK_D0MqAXHETho4zcUHeHufWe37vsKx2isXhOELCeVdsL1rGhOEV7I6gy3MpGYNdcpwgP1jO7F65PSi3e5-WCXtQblXte31asBsm9I9dJ8cVeHMCoDgYw95wLI-c7Bnjnanc1ZHDquNPxGyLi5gc-pjRrdbP8T-n_AUfP57Y</recordid><startdate>20030501</startdate><enddate>20030501</enddate><creator>Kratz, Ewa</creator><creator>Poland, Dennis C.W.</creator><creator>van Dijk, Willem</creator><creator>Kątnik-Prastowska, Iwona</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>IQODW</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>20030501</creationdate><title>Alterations of branching and differential expression of sialic acid on alpha-1-acid glycoprotein in human seminal plasma</title><author>Kratz, Ewa ; Poland, Dennis C.W. ; van Dijk, Willem ; Kątnik-Prastowska, Iwona</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c459t-d9c5670d7839bc463fcdaa840f3c64992f5cc7b281a595978fb24fe1619fb5103</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Adult</topic><topic>Alpha-1-acid glycoprotein</topic><topic>Biological and medical sciences</topic><topic>Carbohydrate Conformation</topic><topic>Chromatography, Ion Exchange - methods</topic><topic>Genital system. Mammary gland</topic><topic>Glycosylation</topic><topic>Humans</topic><topic>Immunoelectrophoresis, Two-Dimensional</topic><topic>Investigative techniques, diagnostic techniques (general aspects)</topic><topic>Lectins - chemistry</topic><topic>Male</topic><topic>Medical sciences</topic><topic>Middle Aged</topic><topic>Orosomucoid - chemistry</topic><topic>Orosomucoid - metabolism</topic><topic>Pathology. Cytology. Biochemistry. Spectrometry. Miscellaneous investigative techniques</topic><topic>Semen - chemistry</topic><topic>Semen - metabolism</topic><topic>Seminal plasma</topic><topic>Sialic Acids - biosynthesis</topic><topic>Sialic Acids - chemistry</topic><topic>Sialylation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kratz, Ewa</creatorcontrib><creatorcontrib>Poland, Dennis C.W.</creatorcontrib><creatorcontrib>van Dijk, Willem</creatorcontrib><creatorcontrib>Kątnik-Prastowska, Iwona</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>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Clinica chimica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kratz, Ewa</au><au>Poland, Dennis C.W.</au><au>van Dijk, Willem</au><au>Kątnik-Prastowska, Iwona</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Alterations of branching and differential expression of sialic acid on alpha-1-acid glycoprotein in human seminal plasma</atitle><jtitle>Clinica chimica acta</jtitle><addtitle>Clin Chim Acta</addtitle><date>2003-05-01</date><risdate>2003</risdate><volume>331</volume><issue>1</issue><spage>87</spage><epage>95</epage><pages>87-95</pages><issn>0009-8981</issn><eissn>1873-3492</eissn><coden>CCATAR</coden><abstract>Background: The degree of branching and types of fucosylation of glycans on α
1-acid glycoprotein (AGP) have been found to be associated with α
1-acid glycoprotein concentrations in human seminal plasma. The glycosylation pattern of α
1-acid glycoprotein in seminal plasma obtained from men living in infertile couples can undergo alterations in relation to sperm analysis and/or α
1-acid glycoprotein concentrations.
Methods: The glycosylation of α
1-acid glycoprotein was studied upon the reactivity with specific lectins by crossed affinity immunoelectrophoresis (concanavalin A), and by glycoprotein lectin immunosorbent assay (
Maackia amurensis and
Sambucus nigra lectins), as well as high pH anion-exchange chromatography with pulsed amperometric detection.
Results: Nonsignificant differences in α
1-acid glycoprotein glycan branching and degree of its sialylation were observed among the AGP derived from seminal plasmas in relation to spermiogram and sperm morphology. However, significant concentration-dependent differences were found in extent of branching and type of sialylation.
Conclusions: The presence in seminal plasma of high concentrations of aberrantly glycosylated AGP molecules might be indicative for a chronic inflammatory condition in the reproductive tract, and can be used as additional tool to subdivide the seminal plasmas of men living in infertile couples.</abstract><cop>Shannon</cop><pub>Elsevier B.V</pub><pmid>12691868</pmid><doi>10.1016/S0009-8981(03)00084-6</doi><tpages>9</tpages></addata></record> |
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| subjects | Adult Alpha-1-acid glycoprotein Biological and medical sciences Carbohydrate Conformation Chromatography, Ion Exchange - methods Genital system. Mammary gland Glycosylation Humans Immunoelectrophoresis, Two-Dimensional Investigative techniques, diagnostic techniques (general aspects) Lectins - chemistry Male Medical sciences Middle Aged Orosomucoid - chemistry Orosomucoid - metabolism Pathology. Cytology. Biochemistry. Spectrometry. Miscellaneous investigative techniques Semen - chemistry Semen - metabolism Seminal plasma Sialic Acids - biosynthesis Sialic Acids - chemistry Sialylation |
| title | Alterations of branching and differential expression of sialic acid on alpha-1-acid glycoprotein in human seminal plasma |
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