{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,3]],"date-time":"2026-05-03T23:42:25Z","timestamp":1777851745617,"version":"3.51.4"},"reference-count":40,"publisher":"SAGE Publications","issue":"7","license":[{"start":{"date-parts":[[2022,7,1]],"date-time":"2022-07-01T00:00:00Z","timestamp":1656633600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"funder":[{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","award":["HD089980"],"award-info":[{"award-number":["HD089980"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","award":["HD078313"],"award-info":[{"award-number":["HD078313"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","award":["HD021350"],"award-info":[{"award-number":["HD021350"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","award":["AG057758"],"award-info":[{"award-number":["AG057758"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.sagepub.com"],"crossmark-restriction":true},"short-container-title":["J Histochem Cytochem."],"published-print":{"date-parts":[[2022,7]]},"abstract":"<jats:p>\n                    Increased phosphorylation of decidual insulin-like growth factor\u2013binding protein-1 (IGFBP-1) can contribute to intrauterine growth restriction (IUGR) by decreasing the bioavailability of insulin-like growth factor-1 (IGF-1). However, the molecular mechanisms regulating IGFBP-1 phosphorylation at the maternal\u2013fetal interface are poorly understood. Protein kinase A (PKA) is required for normal decidualization. Consensus sequences for PKA are present in IGFBP-1. We hypothesized that the expression\/interaction of PKA with decidual IGFBP-1 is increased in IUGR. Parallel reaction monitoring-mass spectrometry (PRM-MS) identified multiple PKA peptides ( n=&gt;30) co-immunoprecipitating with IGFBP-1 in decidualized primary human endometrial stromal cells (HESC). PRM-MS also detected active PKA\n                    <jats:sup>pThr197<\/jats:sup>\n                    and greater site-specific IGFBP-1 phosphorylation\n                    <jats:sup>(pSer119), (pSer98+pSer101) (pSer169+pSer174)<\/jats:sup>\n                    in response to hypoxia. Hypoxia promoted colocalization [dual immunofluorescence (IF)] of PKA with IGFBP-1 in decidualized HESC. Colocalization (IF) and interaction (proximity ligation assay) of PKA and IGFBP-1 were increased in decidua collected from placenta of human IUGR pregnancies ( n=8) compared with decidua from pregnancies with normal fetal growth. Similar changes were detected in decidual PKA\/IGFBP-1 using placenta from baboons subjected to maternal nutrient reduction (MNR) vs controls ( n=3 each). In baboons, these effects were evident in MNR at gestational day 120 prior to IUGR onset. Increased PKA-mediated phosphorylation of decidual IGFBP-1 may contribute to decreased IGF-1 bioavailability in the maternal\u2013fetal interface in IUGR.\n                  <\/jats:p>","DOI":"10.1369\/00221554221112702","type":"journal-article","created":{"date-parts":[[2022,7,8]],"date-time":"2022-07-08T08:58:52Z","timestamp":1657270732000},"page":"515-530","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":3,"title":["Increased Colocalization and Interaction Between Decidual Protein Kinase A and Insulin-like Growth Factor\u2013Binding Protein-1 in Intrauterine Growth Restriction"],"prefix":"10.1369","volume":"70","author":[{"given":"Madhulika B.","family":"Gupta","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Department of Pediatrics, University of Western Ontario, London, ON, Canada"},{"name":"Children\u2019s Health Research Institute, London, ON, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kyle K.","family":"Biggar","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, Carleton University, Ottawa, ON, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cun","family":"Li","sequence":"additional","affiliation":[{"name":"University of Wyoming, Laramie, Wyoming"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0802-0084","authenticated-orcid":false,"given":"Peter W.","family":"Nathanielsz","sequence":"additional","affiliation":[{"name":"University of Wyoming, Laramie, Wyoming"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Thomas","family":"Jansson","sequence":"additional","affiliation":[{"name":"Southwest National Primate Research Center, San Antonio, Texas"},{"name":"Division of Reproductive Sciences, Department of Obstetrics and Gynecology, University of Colorado Anschutz Medical Campus, Aurora, Colorado"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"179","published-online":{"date-parts":[[2022,7,8]]},"reference":[{"key":"bibr1-00221554221112702","doi-asserted-by":"publisher","DOI":"10.1093\/molehr\/7.1.79"},{"key":"bibr2-00221554221112702","doi-asserted-by":"publisher","DOI":"10.1002\/mrd.1080350409"},{"issue":"6","key":"bibr3-00221554221112702","volume":"82","author":"Martina NA","year":"1997","journal-title":"J Clin Endocrinol Metab"},{"key":"bibr4-00221554221112702","doi-asserted-by":"publisher","DOI":"10.1210\/en.2008-0657"},{"issue":"6","key":"bibr5-00221554221112702","volume":"79","author":"Westwood M","year":"1994","journal-title":"J Clin Endocrinol Metab"},{"issue":"3","key":"bibr6-00221554221112702","volume":"69","author":"Forbes K","year":"2008","journal-title":"Horm Res"},{"key":"bibr7-00221554221112702","doi-asserted-by":"publisher","DOI":"10.1172\/JCI0210077"},{"key":"bibr8-00221554221112702","doi-asserted-by":"publisher","DOI":"10.1210\/en.2013-1759"},{"key":"bibr9-00221554221112702","doi-asserted-by":"publisher","DOI":"10.1016\/j.ajpath.2017.09.009"},{"key":"bibr10-00221554221112702","doi-asserted-by":"publisher","DOI":"10.1016\/j.mce.2021.111400"},{"key":"bibr11-00221554221112702","doi-asserted-by":"publisher","DOI":"10.1210\/jc.2018-00820"},{"key":"bibr12-00221554221112702","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)55239-X"},{"key":"bibr13-00221554221112702","doi-asserted-by":"publisher","DOI":"10.1016\/j.mce.2015.12.006"},{"key":"bibr14-00221554221112702","doi-asserted-by":"crossref","unstructured":"Asaoka Y. Chapter thirteen\u2014phosphorylation of Gli by cAMP-dependent protein kinase. In: Litwack G, editor. Vitamins & hormones. 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