{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T10:35:37Z","timestamp":1788863737420,"version":"build-2803163510"},"reference-count":11,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2004,2,23]],"date-time":"2004-02-23T00:00:00Z","timestamp":1077494400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"NIH\u2041","award":["HD37282"],"award-info":[{"award-number":["HD37282"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Reproduction Devel"],"published-print":{"date-parts":[[2004,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Experimental evidence indicates that the membrane\u2010associated proteins polycystin\u20101 and polycystin\u20102 operate as a receptor\u2010calcium channel complex that regulates signaling pathways essential for modulation of renal tubulogenesis. Polycystic kidney disease is characterized by defective renal tubular structure and results from mutations in either <jats:italic>PKD1<\/jats:italic> or <jats:italic>PKD2<\/jats:italic> genes. Recent data suggest that polycystin\u20101 and polycystin\u20102 might localize to primary cilium in principal cells of renal collecting tubules and are thought to act as mechanosensors of fluid flow and contents. Ciliary bending by fluid flow or mechanical stimulation induce Ca<jats:sup>2+<\/jats:sup> release from intracellular stores, presumably to modulate ion influx in response to tubular fluid flow. Polycystins are also emerging as playing a significant role in sperm development and function. <jats:italic>Drosophila<\/jats:italic> polycystin\u20102 is associated with the head and tail of mature sperm. Targeted disruption of the <jats:italic>PKD2<\/jats:italic> homolog results in nearly complete male sterility without disrupting spermatogenesis. Mutant sperm are motile but are unable to reach the female storage organs (seminal receptacles and spermathecae). The sea urchin polycystin\u20101\u2010equivalent suPC2 colocalizes with the polycystin\u20101 homolog REJ3 to the plasma membrane over the acrosomal vesicle. This localization site suggests that the suPC2\u2010REJ3 complex may function as a cation channel mediating acrosome reaction when sperm contact the jelly layer surrounding the egg at fertilization. Future studies leading to the identification of specific ligands for polycystins, including the signaling pathways, might define the puzzling relationship between renal tubular morphogenesis and sperm development and function. Mol. Reprod. Dev. 67: 385\u2013388, 2004. \u00a9 2004 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/mrd.20042","type":"journal-article","created":{"date-parts":[[2004,2,26]],"date-time":"2004-02-26T20:39:14Z","timestamp":1077827954000},"page":"385-388","source":"Crossref","is-referenced-by-count":31,"title":["Polycystins: what polycystic kidney disease tells us about sperm"],"prefix":"10.1002","volume":"67","author":[{"given":"Abraham L.","family":"Kierszenbaum","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2004,2,23]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cub.2003.11.053"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1038\/ng1097-179"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1242\/dev.127.11.2347"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1002\/mrd.20033"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0960-9822(02)00869-2"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1091\/mbc.12.3.589"},{"key":"e_1_2_1_8_1","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/S0015-0282(16)57683-3","article-title":"Polycystic kidney disease and infertility","volume":"64","author":"van der Linden EF","year":"1995","journal-title":"Fertil Steril"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cub.2003.12.002"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1056\/NEJMra022161"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)81570-6"},{"key":"e_1_2_1_12_1","first-page":"2502","article-title":"The polycystic kidney disease proteins polycystin\u20101, polycystin\u20102, polaris, and cystin, are colocalized in renal cilia","volume":"13","author":"Yoder B","year":"2002","journal-title":"J Am Soc Neprol"}],"container-title":["Molecular Reproduction and Development"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fmrd.20042","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fmrd.20042","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/mrd.20042","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,13]],"date-time":"2023-10-13T04:02:51Z","timestamp":1697169771000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/mrd.20042"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2004,2,23]]},"references-count":11,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2004,4]]}},"alternative-id":["10.1002\/mrd.20042"],"URL":"https:\/\/doi.org\/10.1002\/mrd.20042","archive":["Portico"],"relation":{},"ISSN":["1040-452X","1098-2795"],"issn-type":[{"value":"1040-452X","type":"print"},{"value":"1098-2795","type":"electronic"}],"subject":[],"published":{"date-parts":[[2004,2,23]]}}}