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Characterization of Mammalian ADAM2 and Its Absence from Human Sperm
The members of the ADAM (a disintegrin and metalloprotease) family are membrane-anchored multi-domain proteins that play prominent roles in male reproduction. ADAM2, which was one of the first identified ADAMs, is the best studied ADAM in reproduction. In the male germ cells of mice, ADAM2 and other...
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Published in: | PloS one 2016-06, Vol.11 (6), p.e0158321-e0158321 |
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creator | Choi, Heejin Jin, Sora Kwon, Jun Tae Kim, Jihye Jeong, Juri Kim, Jaehwan Jeon, Suyeon Park, Zee Yong Jung, Kang-Jin Park, Kwangsung Cho, Chunghee |
description | The members of the ADAM (a disintegrin and metalloprotease) family are membrane-anchored multi-domain proteins that play prominent roles in male reproduction. ADAM2, which was one of the first identified ADAMs, is the best studied ADAM in reproduction. In the male germ cells of mice, ADAM2 and other ADAMs form complexes that contribute to sperm-sperm adhesion, sperm-egg interactions, and the migration of sperm in the female reproductive tract. Here, we generated specific antibodies against mouse and human ADAM2, and investigated various features of ADAM2 in mice, monkeys and humans. We found that the cytoplasmic domain of ADAM2 might enable the differential association of this protein with other ADAMs in mice. Western blot analysis with the anti-human ADAM2 antibodies showed that ADAM2 is present in the testis and sperm of monkeys. Monkey ADAM2 was found to associate with chaperone proteins in testis. In humans, we identified ADAM2 as a 100-kDa protein in the testis, but failed to detect it in sperm. This is surprising given the results in mice and monkeys, but it is consistent with the failure of ADAM2 identification in the previous proteomic analyses of human sperm. These findings suggest that the reproductive functions of ADAM2 differ between humans and mice. Our protein analysis showed the presence of potential ADAM2 complexes involving yet-unknown proteins in human testis. Taken together, our results provide new information regarding the characteristics of ADAM2 in mammalian species, including humans. |
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ADAM2, which was one of the first identified ADAMs, is the best studied ADAM in reproduction. In the male germ cells of mice, ADAM2 and other ADAMs form complexes that contribute to sperm-sperm adhesion, sperm-egg interactions, and the migration of sperm in the female reproductive tract. Here, we generated specific antibodies against mouse and human ADAM2, and investigated various features of ADAM2 in mice, monkeys and humans. We found that the cytoplasmic domain of ADAM2 might enable the differential association of this protein with other ADAMs in mice. Western blot analysis with the anti-human ADAM2 antibodies showed that ADAM2 is present in the testis and sperm of monkeys. Monkey ADAM2 was found to associate with chaperone proteins in testis. In humans, we identified ADAM2 as a 100-kDa protein in the testis, but failed to detect it in sperm. This is surprising given the results in mice and monkeys, but it is consistent with the failure of ADAM2 identification in the previous proteomic analyses of human sperm. These findings suggest that the reproductive functions of ADAM2 differ between humans and mice. Our protein analysis showed the presence of potential ADAM2 complexes involving yet-unknown proteins in human testis. Taken together, our results provide new information regarding the characteristics of ADAM2 in mammalian species, including humans.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0158321</identifier><identifier>PMID: 27341348</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; Amino acids ; Analysis ; Animals ; Antibodies ; Biology and Life Sciences ; Chemical properties ; Chromatography, Liquid ; Epidermal growth factor ; Failure analysis ; Fertilins - chemistry ; Fertilins - genetics ; Fertilins - metabolism ; Germ cells ; Humans ; Immunoglobulins ; Life sciences ; Macaca fascicularis ; Male ; Mammals ; Mammals - metabolism ; Medicine and Health Sciences ; Metalloproteinase ; Mice ; Monkeys ; Physiological aspects ; Protein Interaction Domains and Motifs ; Proteins ; Proteomics ; Reproduction ; Reproductive system ; Research and Analysis Methods ; Sperm ; Spermatozoa - metabolism ; Tandem Mass Spectrometry ; Testis - metabolism</subject><ispartof>PloS one, 2016-06, Vol.11 (6), p.e0158321-e0158321</ispartof><rights>COPYRIGHT 2016 Public Library of Science</rights><rights>2016 Choi et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2016 Choi et al 2016 Choi et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c725t-d700e019ceb32a471d4cd804d36e758fea1ad68c22772af9cf1899d300a811863</citedby><cites>FETCH-LOGICAL-c725t-d700e019ceb32a471d4cd804d36e758fea1ad68c22772af9cf1899d300a811863</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1799362764/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1799362764?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27341348$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Gill, Andrew C.</contributor><creatorcontrib>Choi, Heejin</creatorcontrib><creatorcontrib>Jin, Sora</creatorcontrib><creatorcontrib>Kwon, Jun Tae</creatorcontrib><creatorcontrib>Kim, Jihye</creatorcontrib><creatorcontrib>Jeong, Juri</creatorcontrib><creatorcontrib>Kim, Jaehwan</creatorcontrib><creatorcontrib>Jeon, Suyeon</creatorcontrib><creatorcontrib>Park, Zee Yong</creatorcontrib><creatorcontrib>Jung, Kang-Jin</creatorcontrib><creatorcontrib>Park, Kwangsung</creatorcontrib><creatorcontrib>Cho, Chunghee</creatorcontrib><title>Characterization of Mammalian ADAM2 and Its Absence from Human Sperm</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The members of the ADAM (a disintegrin and metalloprotease) family are membrane-anchored multi-domain proteins that play prominent roles in male reproduction. ADAM2, which was one of the first identified ADAMs, is the best studied ADAM in reproduction. In the male germ cells of mice, ADAM2 and other ADAMs form complexes that contribute to sperm-sperm adhesion, sperm-egg interactions, and the migration of sperm in the female reproductive tract. Here, we generated specific antibodies against mouse and human ADAM2, and investigated various features of ADAM2 in mice, monkeys and humans. We found that the cytoplasmic domain of ADAM2 might enable the differential association of this protein with other ADAMs in mice. Western blot analysis with the anti-human ADAM2 antibodies showed that ADAM2 is present in the testis and sperm of monkeys. Monkey ADAM2 was found to associate with chaperone proteins in testis. In humans, we identified ADAM2 as a 100-kDa protein in the testis, but failed to detect it in sperm. This is surprising given the results in mice and monkeys, but it is consistent with the failure of ADAM2 identification in the previous proteomic analyses of human sperm. These findings suggest that the reproductive functions of ADAM2 differ between humans and mice. Our protein analysis showed the presence of potential ADAM2 complexes involving yet-unknown proteins in human testis. Taken together, our results provide new information regarding the characteristics of ADAM2 in mammalian species, including humans.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Analysis</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Biology and Life Sciences</subject><subject>Chemical properties</subject><subject>Chromatography, Liquid</subject><subject>Epidermal growth factor</subject><subject>Failure analysis</subject><subject>Fertilins - chemistry</subject><subject>Fertilins - genetics</subject><subject>Fertilins - metabolism</subject><subject>Germ cells</subject><subject>Humans</subject><subject>Immunoglobulins</subject><subject>Life sciences</subject><subject>Macaca fascicularis</subject><subject>Male</subject><subject>Mammals</subject><subject>Mammals - metabolism</subject><subject>Medicine and Health Sciences</subject><subject>Metalloproteinase</subject><subject>Mice</subject><subject>Monkeys</subject><subject>Physiological aspects</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Reproduction</subject><subject>Reproductive system</subject><subject>Research and Analysis Methods</subject><subject>Sperm</subject><subject>Spermatozoa - 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ADAM2, which was one of the first identified ADAMs, is the best studied ADAM in reproduction. In the male germ cells of mice, ADAM2 and other ADAMs form complexes that contribute to sperm-sperm adhesion, sperm-egg interactions, and the migration of sperm in the female reproductive tract. Here, we generated specific antibodies against mouse and human ADAM2, and investigated various features of ADAM2 in mice, monkeys and humans. We found that the cytoplasmic domain of ADAM2 might enable the differential association of this protein with other ADAMs in mice. Western blot analysis with the anti-human ADAM2 antibodies showed that ADAM2 is present in the testis and sperm of monkeys. Monkey ADAM2 was found to associate with chaperone proteins in testis. In humans, we identified ADAM2 as a 100-kDa protein in the testis, but failed to detect it in sperm. This is surprising given the results in mice and monkeys, but it is consistent with the failure of ADAM2 identification in the previous proteomic analyses of human sperm. These findings suggest that the reproductive functions of ADAM2 differ between humans and mice. Our protein analysis showed the presence of potential ADAM2 complexes involving yet-unknown proteins in human testis. Taken together, our results provide new information regarding the characteristics of ADAM2 in mammalian species, including humans.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>27341348</pmid><doi>10.1371/journal.pone.0158321</doi><tpages>e0158321</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Amino acids Analysis Animals Antibodies Biology and Life Sciences Chemical properties Chromatography, Liquid Epidermal growth factor Failure analysis Fertilins - chemistry Fertilins - genetics Fertilins - metabolism Germ cells Humans Immunoglobulins Life sciences Macaca fascicularis Male Mammals Mammals - metabolism Medicine and Health Sciences Metalloproteinase Mice Monkeys Physiological aspects Protein Interaction Domains and Motifs Proteins Proteomics Reproduction Reproductive system Research and Analysis Methods Sperm Spermatozoa - metabolism Tandem Mass Spectrometry Testis - metabolism |
title | Characterization of Mammalian ADAM2 and Its Absence from Human Sperm |
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