Spam1 (PH-20) Expression in the Extratesticular Duct and Accessory Organs of the Mouse: A Possible Role in Sperm Fluid Reabsorption
A widely conserved sperm antigen, the sperm adhesion molecule 1 (SPAM1 or PH-20) is a glycosylphosphatidyl inositol-linked protein with multiple roles in mammalian fertilization. It has been shown to be dually expressed in testis and epididymis and this is conserved in the four species (mouse, rat,...
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Veröffentlicht in: | Biology of reproduction 2004-10, Vol.71 (4), p.1101-1107 |
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container_title | Biology of reproduction |
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creator | HONG ZHANG MORALES, Carlos R BADRAN, Haitham EL-ALFY, Mohamed MARTIN-DELEON, Patricia A |
description | A widely conserved sperm antigen, the sperm adhesion molecule 1 (SPAM1 or PH-20) is a glycosylphosphatidyl inositol-linked
protein with multiple roles in mammalian fertilization. It has been shown to be dually expressed in testis and epididymis
and this is conserved in the four species (mouse, rat, macaques, humans) that have been studied to date. Here, we report Spam1
RNA and protein expression in the murine vas deferens and efferent ducts. In situ hybridization and immunohistochemistry indicate
that transcript and protein are distributed in the nonciliated epithelial cells and that the efferent ducts have the most
intense staining of all three regions of the excurrent ducts. Spam1 products were also present in the accessory organs, the prostate, and seminal vesicles and its fluid. Using hyaluronic acid
substrate gel electrophoresis, hyaluronidase activity at pH 7.0 was detected in the vas deferens but was absent from the efferent
ducts, the prostate, and the seminal vesicles/fluid. This suggests that Spam1 may play a nonenzymatic role in these organs.
In the efferent ducts, where Spam1 is enriched in the apical (but not basolateral) membrane of nonciliated cells, it is likely
to play a role in sperm concentration, which is the established function of that organ. |
doi_str_mv | 10.1095/biolreprod.104.030403 |
format | Article |
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protein with multiple roles in mammalian fertilization. It has been shown to be dually expressed in testis and epididymis
and this is conserved in the four species (mouse, rat, macaques, humans) that have been studied to date. Here, we report Spam1
RNA and protein expression in the murine vas deferens and efferent ducts. In situ hybridization and immunohistochemistry indicate
that transcript and protein are distributed in the nonciliated epithelial cells and that the efferent ducts have the most
intense staining of all three regions of the excurrent ducts. Spam1 products were also present in the accessory organs, the prostate, and seminal vesicles and its fluid. Using hyaluronic acid
substrate gel electrophoresis, hyaluronidase activity at pH 7.0 was detected in the vas deferens but was absent from the efferent
ducts, the prostate, and the seminal vesicles/fluid. This suggests that Spam1 may play a nonenzymatic role in these organs.
In the efferent ducts, where Spam1 is enriched in the apical (but not basolateral) membrane of nonciliated cells, it is likely
to play a role in sperm concentration, which is the established function of that organ.</description><identifier>ISSN: 0006-3363</identifier><identifier>EISSN: 1529-7268</identifier><identifier>DOI: 10.1095/biolreprod.104.030403</identifier><identifier>PMID: 15175239</identifier><identifier>CODEN: BIREBV</identifier><language>eng</language><publisher>Madison, WI: Society for the Study of Reproduction</publisher><subject>Animals ; Biological and medical sciences ; Body Fluids - metabolism ; Cell Adhesion Molecules - genetics ; Cell Adhesion Molecules - metabolism ; Ejaculatory Ducts - cytology ; Ejaculatory Ducts - metabolism ; Epithelial Cells - metabolism ; Fundamental and applied biological sciences. Psychology ; Genitalia, Male - cytology ; Genitalia, Male - metabolism ; Hyaluronoglucosaminidase ; Male ; Mammalian male genital system ; Mice ; Morphology. Physiology ; Prostate - cytology ; Prostate - metabolism ; RNA - analysis ; Seminal Vesicles - cytology ; Seminal Vesicles - metabolism ; Spermatozoa - metabolism ; Vas Deferens - cytology ; Vas Deferens - metabolism ; Vertebrates: reproduction</subject><ispartof>Biology of reproduction, 2004-10, Vol.71 (4), p.1101-1107</ispartof><rights>2004 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16135354$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15175239$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>HONG ZHANG</creatorcontrib><creatorcontrib>MORALES, Carlos R</creatorcontrib><creatorcontrib>BADRAN, Haitham</creatorcontrib><creatorcontrib>EL-ALFY, Mohamed</creatorcontrib><creatorcontrib>MARTIN-DELEON, Patricia A</creatorcontrib><title>Spam1 (PH-20) Expression in the Extratesticular Duct and Accessory Organs of the Mouse: A Possible Role in Sperm Fluid Reabsorption</title><title>Biology of reproduction</title><addtitle>Biol Reprod</addtitle><description>A widely conserved sperm antigen, the sperm adhesion molecule 1 (SPAM1 or PH-20) is a glycosylphosphatidyl inositol-linked
protein with multiple roles in mammalian fertilization. It has been shown to be dually expressed in testis and epididymis
and this is conserved in the four species (mouse, rat, macaques, humans) that have been studied to date. Here, we report Spam1
RNA and protein expression in the murine vas deferens and efferent ducts. In situ hybridization and immunohistochemistry indicate
that transcript and protein are distributed in the nonciliated epithelial cells and that the efferent ducts have the most
intense staining of all three regions of the excurrent ducts. Spam1 products were also present in the accessory organs, the prostate, and seminal vesicles and its fluid. Using hyaluronic acid
substrate gel electrophoresis, hyaluronidase activity at pH 7.0 was detected in the vas deferens but was absent from the efferent
ducts, the prostate, and the seminal vesicles/fluid. This suggests that Spam1 may play a nonenzymatic role in these organs.
In the efferent ducts, where Spam1 is enriched in the apical (but not basolateral) membrane of nonciliated cells, it is likely
to play a role in sperm concentration, which is the established function of that organ.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Body Fluids - metabolism</subject><subject>Cell Adhesion Molecules - genetics</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Ejaculatory Ducts - cytology</subject><subject>Ejaculatory Ducts - metabolism</subject><subject>Epithelial Cells - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genitalia, Male - cytology</subject><subject>Genitalia, Male - metabolism</subject><subject>Hyaluronoglucosaminidase</subject><subject>Male</subject><subject>Mammalian male genital system</subject><subject>Mice</subject><subject>Morphology. Physiology</subject><subject>Prostate - cytology</subject><subject>Prostate - metabolism</subject><subject>RNA - analysis</subject><subject>Seminal Vesicles - cytology</subject><subject>Seminal Vesicles - metabolism</subject><subject>Spermatozoa - metabolism</subject><subject>Vas Deferens - cytology</subject><subject>Vas Deferens - metabolism</subject><subject>Vertebrates: reproduction</subject><issn>0006-3363</issn><issn>1529-7268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkE1vFDEMhiNERZfCTwDlAoLDtM54JjvhtiotrdSqVQvnUT483aDMR5MZLT3zx4lgUS-2bD1-7deMvRNwLEDVJ8aPIdIUR5fr6hgQKsAXbCXqUhXrUjYv2QoAZIEo8ZC9TukngKiwxFfsUNRiXZeoVuz3_aR7wT_dXhQlfOZnv6ZIKflx4H7g85ZyZ456pjR7uwQd-dfFzlwPjm-szeQYn_hNfNBD4mP3d-B6XBJ94Rt-O2YhE4jfjTlkufuJYs_Pw-IdvyNt8vA051Vv2EGnQ6K3-3zEfpyffT-9KK5uvl2ebq6KbbYzF02HsnG1qiQQdlpmy2swBprOSaUkyUZaqkRDBksnodZCWOfKzjjZgJGER-zjP938tcclW2p7nyyFoAfKR7dSNgqVVBl8vwcX05Nrp-h7HZ_a_2_LwIc9oJPVoYt6sD49c1JgjXX1vHHrH7Y7H6lNvQ4hy2K72-3Woq1aIUDgH-J4i6w</recordid><startdate>20041001</startdate><enddate>20041001</enddate><creator>HONG ZHANG</creator><creator>MORALES, Carlos R</creator><creator>BADRAN, Haitham</creator><creator>EL-ALFY, Mohamed</creator><creator>MARTIN-DELEON, Patricia A</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>20041001</creationdate><title>Spam1 (PH-20) Expression in the Extratesticular Duct and Accessory Organs of the Mouse: A Possible Role in Sperm Fluid Reabsorption</title><author>HONG ZHANG ; MORALES, Carlos R ; BADRAN, Haitham ; EL-ALFY, Mohamed ; MARTIN-DELEON, Patricia A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h268t-8f368d59460e3fa603070bb08fd6996e686ce418eb32d605a11cdd2fbd680b6e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Body Fluids - metabolism</topic><topic>Cell Adhesion Molecules - genetics</topic><topic>Cell Adhesion Molecules - metabolism</topic><topic>Ejaculatory Ducts - cytology</topic><topic>Ejaculatory Ducts - metabolism</topic><topic>Epithelial Cells - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genitalia, Male - cytology</topic><topic>Genitalia, Male - metabolism</topic><topic>Hyaluronoglucosaminidase</topic><topic>Male</topic><topic>Mammalian male genital system</topic><topic>Mice</topic><topic>Morphology. Physiology</topic><topic>Prostate - cytology</topic><topic>Prostate - metabolism</topic><topic>RNA - analysis</topic><topic>Seminal Vesicles - cytology</topic><topic>Seminal Vesicles - metabolism</topic><topic>Spermatozoa - metabolism</topic><topic>Vas Deferens - cytology</topic><topic>Vas Deferens - metabolism</topic><topic>Vertebrates: reproduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>HONG ZHANG</creatorcontrib><creatorcontrib>MORALES, Carlos R</creatorcontrib><creatorcontrib>BADRAN, Haitham</creatorcontrib><creatorcontrib>EL-ALFY, Mohamed</creatorcontrib><creatorcontrib>MARTIN-DELEON, Patricia A</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>HONG ZHANG</au><au>MORALES, Carlos R</au><au>BADRAN, Haitham</au><au>EL-ALFY, Mohamed</au><au>MARTIN-DELEON, Patricia A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Spam1 (PH-20) Expression in the Extratesticular Duct and Accessory Organs of the Mouse: A Possible Role in Sperm Fluid Reabsorption</atitle><jtitle>Biology of reproduction</jtitle><addtitle>Biol Reprod</addtitle><date>2004-10-01</date><risdate>2004</risdate><volume>71</volume><issue>4</issue><spage>1101</spage><epage>1107</epage><pages>1101-1107</pages><issn>0006-3363</issn><eissn>1529-7268</eissn><coden>BIREBV</coden><abstract>A widely conserved sperm antigen, the sperm adhesion molecule 1 (SPAM1 or PH-20) is a glycosylphosphatidyl inositol-linked
protein with multiple roles in mammalian fertilization. It has been shown to be dually expressed in testis and epididymis
and this is conserved in the four species (mouse, rat, macaques, humans) that have been studied to date. Here, we report Spam1
RNA and protein expression in the murine vas deferens and efferent ducts. In situ hybridization and immunohistochemistry indicate
that transcript and protein are distributed in the nonciliated epithelial cells and that the efferent ducts have the most
intense staining of all three regions of the excurrent ducts. Spam1 products were also present in the accessory organs, the prostate, and seminal vesicles and its fluid. Using hyaluronic acid
substrate gel electrophoresis, hyaluronidase activity at pH 7.0 was detected in the vas deferens but was absent from the efferent
ducts, the prostate, and the seminal vesicles/fluid. This suggests that Spam1 may play a nonenzymatic role in these organs.
In the efferent ducts, where Spam1 is enriched in the apical (but not basolateral) membrane of nonciliated cells, it is likely
to play a role in sperm concentration, which is the established function of that organ.</abstract><cop>Madison, WI</cop><pub>Society for the Study of Reproduction</pub><pmid>15175239</pmid><doi>10.1095/biolreprod.104.030403</doi><tpages>7</tpages></addata></record> |
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source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; EZB-FREE-00999 freely available EZB journals; BioOne Complete |
subjects | Animals Biological and medical sciences Body Fluids - metabolism Cell Adhesion Molecules - genetics Cell Adhesion Molecules - metabolism Ejaculatory Ducts - cytology Ejaculatory Ducts - metabolism Epithelial Cells - metabolism Fundamental and applied biological sciences. Psychology Genitalia, Male - cytology Genitalia, Male - metabolism Hyaluronoglucosaminidase Male Mammalian male genital system Mice Morphology. Physiology Prostate - cytology Prostate - metabolism RNA - analysis Seminal Vesicles - cytology Seminal Vesicles - metabolism Spermatozoa - metabolism Vas Deferens - cytology Vas Deferens - metabolism Vertebrates: reproduction |
title | Spam1 (PH-20) Expression in the Extratesticular Duct and Accessory Organs of the Mouse: A Possible Role in Sperm Fluid Reabsorption |
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