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Testins Are Structurally Related Sertoli Cell Proteins Whose Secretion Is Tightly Coupled to the Presence of Germ Cells
Previous studies from this laboratory have shown that Sertoli cell-enriched culture medium contained two immunologically and structurally related proteins designated CMB-22 and CMB-23 with Mr of 37,000 and 40,000, respectively. We have now demonstrated that both CMB-22 and CMB-23 are monomeric prote...
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| Published in: | The Journal of biological chemistry 1989-12, Vol.264 (35), p.21386-21393 |
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| container_issue | 35 |
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| creator | Cheng, C Y Grima, J Stahler, M S Lockshin, R A Bardin, C W |
| description | Previous studies from this laboratory have shown that Sertoli cell-enriched culture medium contained two immunologically and structurally related proteins designated CMB-22 and CMB-23 with Mr of 37,000 and 40,000, respectively. We have now demonstrated that both CMB-22 and CMB-23 are monomeric proteins with the following NH2-terminal amino acid sequences: CMB-22, NH2-TPDPSLDVEWNEWRTKHGKTYNMNEERLKR; CMB-23, NH2-XAPXPDPSLDVEXNEXRTK. These sequences are virtually identical except that CMB-23 has three extra NH2 terminus amino acids of X-A-P. Comparison of these sequences with those in the Protein Identification Resource revealed that they are unique proteins. CMB-22 and CMB-23 are highly concentrated in testes and their levels in this tissue increase with age. Studies using [35S]methionine incorporation and immunoprecipitation demonstrated that Sertoli cells synthesize and secrete these proteins in vitro. Because they seem not to have been isolated previously, are concentrated in and synthesized by the testes, and are structurally related, we propose that CMB-22 and CMB-23 be designated testin I and testin II, respectively. The distribution of these proteins in biological fluids were compared with those of testibumin and rat androgen binding protein (rABP), two other Sertoli cell proteins. The results suggest that testins, unlike testibumin and rABP, are not transported to the epididymis. Although the amount of testins secreted by Sertoli cells in vitro is similar to that of testibumin and rABP, the concentrations in testis and rete testis fluid are several orders of magnitude less than that of testibumin and rABP. These observations suggest that the secretion of these proteins in vivo might be suppressed by germ cells. The fact that 10 times more testins are secreted by tubules from immature rats than by those from adult rats and that there is an increase in the testicular content of testins following a single dose of busulfan, which depleted the germ cells from the seminiferous epithelium, supports this hypothesis. Thus, the secretion of testins by Sertoli cells appears to be tightly coupled to the presence of germ cells; there is an inverse relationship between the amount of testins in the testis and the number of germ cells. These results suggest that testins are unique testicular proteins that can be used to study Sertoli cell-germ cell interactions in the seminiferous epithelium. |
| doi_str_mv | 10.1016/S0021-9258(19)30092-4 |
| format | article |
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We have now demonstrated that both CMB-22 and CMB-23 are monomeric proteins with the following NH2-terminal amino acid sequences: CMB-22, NH2-TPDPSLDVEWNEWRTKHGKTYNMNEERLKR; CMB-23, NH2-XAPXPDPSLDVEXNEXRTK. These sequences are virtually identical except that CMB-23 has three extra NH2 terminus amino acids of X-A-P. Comparison of these sequences with those in the Protein Identification Resource revealed that they are unique proteins. CMB-22 and CMB-23 are highly concentrated in testes and their levels in this tissue increase with age. Studies using [35S]methionine incorporation and immunoprecipitation demonstrated that Sertoli cells synthesize and secrete these proteins in vitro. Because they seem not to have been isolated previously, are concentrated in and synthesized by the testes, and are structurally related, we propose that CMB-22 and CMB-23 be designated testin I and testin II, respectively. The distribution of these proteins in biological fluids were compared with those of testibumin and rat androgen binding protein (rABP), two other Sertoli cell proteins. The results suggest that testins, unlike testibumin and rABP, are not transported to the epididymis. Although the amount of testins secreted by Sertoli cells in vitro is similar to that of testibumin and rABP, the concentrations in testis and rete testis fluid are several orders of magnitude less than that of testibumin and rABP. These observations suggest that the secretion of these proteins in vivo might be suppressed by germ cells. The fact that 10 times more testins are secreted by tubules from immature rats than by those from adult rats and that there is an increase in the testicular content of testins following a single dose of busulfan, which depleted the germ cells from the seminiferous epithelium, supports this hypothesis. Thus, the secretion of testins by Sertoli cells appears to be tightly coupled to the presence of germ cells; there is an inverse relationship between the amount of testins in the testis and the number of germ cells. These results suggest that testins are unique testicular proteins that can be used to study Sertoli cell-germ cell interactions in the seminiferous epithelium.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)30092-4</identifier><identifier>PMID: 2592382</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Cells, Cultured ; Fundamental and applied biological sciences. Psychology ; Glycoproteins - analysis ; Glycoproteins - blood ; Glycoproteins - isolation & purification ; Immune Sera ; Male ; Miscellaneous ; Molecular Sequence Data ; Molecular Weight ; Orchiectomy ; Organ Specificity ; Proteins ; Radioimmunoassay ; Rats ; Rats, Inbred Strains ; Sertoli Cells - physiology ; testin</subject><ispartof>The Journal of biological chemistry, 1989-12, Vol.264 (35), p.21386-21393</ispartof><rights>1989 © 1989 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c496t-f748f82ef7ebde6be37940db737ba27ccbdd742f41603a9def9217d17e34bc3a3</citedby><cites>FETCH-LOGICAL-c496t-f748f82ef7ebde6be37940db737ba27ccbdd742f41603a9def9217d17e34bc3a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6727390$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2592382$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cheng, C Y</creatorcontrib><creatorcontrib>Grima, J</creatorcontrib><creatorcontrib>Stahler, M S</creatorcontrib><creatorcontrib>Lockshin, R A</creatorcontrib><creatorcontrib>Bardin, C W</creatorcontrib><title>Testins Are Structurally Related Sertoli Cell Proteins Whose Secretion Is Tightly Coupled to the Presence of Germ Cells</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Previous studies from this laboratory have shown that Sertoli cell-enriched culture medium contained two immunologically and structurally related proteins designated CMB-22 and CMB-23 with Mr of 37,000 and 40,000, respectively. We have now demonstrated that both CMB-22 and CMB-23 are monomeric proteins with the following NH2-terminal amino acid sequences: CMB-22, NH2-TPDPSLDVEWNEWRTKHGKTYNMNEERLKR; CMB-23, NH2-XAPXPDPSLDVEXNEXRTK. These sequences are virtually identical except that CMB-23 has three extra NH2 terminus amino acids of X-A-P. Comparison of these sequences with those in the Protein Identification Resource revealed that they are unique proteins. CMB-22 and CMB-23 are highly concentrated in testes and their levels in this tissue increase with age. Studies using [35S]methionine incorporation and immunoprecipitation demonstrated that Sertoli cells synthesize and secrete these proteins in vitro. Because they seem not to have been isolated previously, are concentrated in and synthesized by the testes, and are structurally related, we propose that CMB-22 and CMB-23 be designated testin I and testin II, respectively. The distribution of these proteins in biological fluids were compared with those of testibumin and rat androgen binding protein (rABP), two other Sertoli cell proteins. The results suggest that testins, unlike testibumin and rABP, are not transported to the epididymis. Although the amount of testins secreted by Sertoli cells in vitro is similar to that of testibumin and rABP, the concentrations in testis and rete testis fluid are several orders of magnitude less than that of testibumin and rABP. These observations suggest that the secretion of these proteins in vivo might be suppressed by germ cells. The fact that 10 times more testins are secreted by tubules from immature rats than by those from adult rats and that there is an increase in the testicular content of testins following a single dose of busulfan, which depleted the germ cells from the seminiferous epithelium, supports this hypothesis. Thus, the secretion of testins by Sertoli cells appears to be tightly coupled to the presence of germ cells; there is an inverse relationship between the amount of testins in the testis and the number of germ cells. These results suggest that testins are unique testicular proteins that can be used to study Sertoli cell-germ cell interactions in the seminiferous epithelium.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cells, Cultured</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins - analysis</subject><subject>Glycoproteins - blood</subject><subject>Glycoproteins - isolation & purification</subject><subject>Immune Sera</subject><subject>Male</subject><subject>Miscellaneous</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Orchiectomy</subject><subject>Organ Specificity</subject><subject>Proteins</subject><subject>Radioimmunoassay</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Sertoli Cells - physiology</subject><subject>testin</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><recordid>eNqFkU1v1DAQhi0EKtvCT6jkA0L0EPBX4viEqhWUSpVA7CK4WY49IUbZeGs7VP33eD-0HOuLD_M84_G8CF1S8p4S2nxYEcJopVjdvqPqihOiWCWeoQUlLa94TX89R4sT8hKdp_SHlCMUPUNnrFaMt2yBHtaQsp8Svo6AVznONs_RjOMj_g6jyeDwCmIOo8dLGEf8LYYMO_znEFIRwEbIPkz4NuG1_z3kIi7DvB2LmAPOAxQFEkwWcOjxDcTNvlF6hV70Zkzw-nhfoB-fP62XX6q7rze3y-u7ygrV5KqXou1bBr2EzkHTAZdKENdJLjvDpLWdc1KwXtCGcKMc9IpR6agELjrLDb9Abw99tzHcz-WveuOTLROYCcKctFS8EaomT4K0FjXnDS9gfQBtDClF6PU2-o2Jj5oSvUtG75PRu7VrqvQ-GS2Kd3l8YO424E7WMYpSf3Osm2TN2EczWZ9OWCOZ5Ir8x4ay7gcfQXc-2AE2mjVC81ozytumYB8PGJTl_vUQdbJ-F4Mris3aBf_EvP8AFdi3PQ</recordid><startdate>19891215</startdate><enddate>19891215</enddate><creator>Cheng, C Y</creator><creator>Grima, J</creator><creator>Stahler, M S</creator><creator>Lockshin, R A</creator><creator>Bardin, C W</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19891215</creationdate><title>Testins Are Structurally Related Sertoli Cell Proteins Whose Secretion Is Tightly Coupled to the Presence of Germ Cells</title><author>Cheng, C Y ; Grima, J ; Stahler, M S ; Lockshin, R A ; Bardin, C W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c496t-f748f82ef7ebde6be37940db737ba27ccbdd742f41603a9def9217d17e34bc3a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cells, Cultured</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins - analysis</topic><topic>Glycoproteins - blood</topic><topic>Glycoproteins - isolation & purification</topic><topic>Immune Sera</topic><topic>Male</topic><topic>Miscellaneous</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Orchiectomy</topic><topic>Organ Specificity</topic><topic>Proteins</topic><topic>Radioimmunoassay</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Sertoli Cells - physiology</topic><topic>testin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cheng, C Y</creatorcontrib><creatorcontrib>Grima, J</creatorcontrib><creatorcontrib>Stahler, M S</creatorcontrib><creatorcontrib>Lockshin, R A</creatorcontrib><creatorcontrib>Bardin, C W</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cheng, C Y</au><au>Grima, J</au><au>Stahler, M S</au><au>Lockshin, R A</au><au>Bardin, C W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Testins Are Structurally Related Sertoli Cell Proteins Whose Secretion Is Tightly Coupled to the Presence of Germ Cells</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1989-12-15</date><risdate>1989</risdate><volume>264</volume><issue>35</issue><spage>21386</spage><epage>21393</epage><pages>21386-21393</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>Previous studies from this laboratory have shown that Sertoli cell-enriched culture medium contained two immunologically and structurally related proteins designated CMB-22 and CMB-23 with Mr of 37,000 and 40,000, respectively. We have now demonstrated that both CMB-22 and CMB-23 are monomeric proteins with the following NH2-terminal amino acid sequences: CMB-22, NH2-TPDPSLDVEWNEWRTKHGKTYNMNEERLKR; CMB-23, NH2-XAPXPDPSLDVEXNEXRTK. These sequences are virtually identical except that CMB-23 has three extra NH2 terminus amino acids of X-A-P. Comparison of these sequences with those in the Protein Identification Resource revealed that they are unique proteins. CMB-22 and CMB-23 are highly concentrated in testes and their levels in this tissue increase with age. Studies using [35S]methionine incorporation and immunoprecipitation demonstrated that Sertoli cells synthesize and secrete these proteins in vitro. Because they seem not to have been isolated previously, are concentrated in and synthesized by the testes, and are structurally related, we propose that CMB-22 and CMB-23 be designated testin I and testin II, respectively. The distribution of these proteins in biological fluids were compared with those of testibumin and rat androgen binding protein (rABP), two other Sertoli cell proteins. The results suggest that testins, unlike testibumin and rABP, are not transported to the epididymis. Although the amount of testins secreted by Sertoli cells in vitro is similar to that of testibumin and rABP, the concentrations in testis and rete testis fluid are several orders of magnitude less than that of testibumin and rABP. These observations suggest that the secretion of these proteins in vivo might be suppressed by germ cells. The fact that 10 times more testins are secreted by tubules from immature rats than by those from adult rats and that there is an increase in the testicular content of testins following a single dose of busulfan, which depleted the germ cells from the seminiferous epithelium, supports this hypothesis. Thus, the secretion of testins by Sertoli cells appears to be tightly coupled to the presence of germ cells; there is an inverse relationship between the amount of testins in the testis and the number of germ cells. These results suggest that testins are unique testicular proteins that can be used to study Sertoli cell-germ cell interactions in the seminiferous epithelium.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>2592382</pmid><doi>10.1016/S0021-9258(19)30092-4</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1989-12, Vol.264 (35), p.21386-21393 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cells, Cultured Fundamental and applied biological sciences. Psychology Glycoproteins - analysis Glycoproteins - blood Glycoproteins - isolation & purification Immune Sera Male Miscellaneous Molecular Sequence Data Molecular Weight Orchiectomy Organ Specificity Proteins Radioimmunoassay Rats Rats, Inbred Strains Sertoli Cells - physiology testin |
| title | Testins Are Structurally Related Sertoli Cell Proteins Whose Secretion Is Tightly Coupled to the Presence of Germ Cells |
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