{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,13]],"date-time":"2026-02-13T06:51:10Z","timestamp":1770965470155,"version":"3.50.1"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2004,4,1]]},"abstract":"<jats:p>Ephrins are ligands for the Eph receptor tyrosine kinases, which play important roles in patterning nervous and vascular systems. Ephrin-A1 is a glycosylphosphatidylinositol-anchored ligand that binds to the EphA receptor tyrosine kinases. In the present study, we have identified a new ephrin-A1 isoform, denoted ephrin-A1b (ephrin-A1 isoform b). Compared with the originally described ephrin-A1 sequence, ephrin-A1a [Holzman, Marks and Dixit (1990) Mol. Cell. Biol. 10, 5830\u20135838], ephrin-A1b lacks a segment of 22 amino acids (residues 131\u2013152). At the transcript level, exon 3 is spliced out in the transcript encoding ephrin-A1b. Transfection of HEK-293T cells (human embryonic kidney 293 cells) with an ephrin-A1b-expressing plasmid resulted in a significant expression of the protein on the cell surface. However, soluble EphA2 receptor (EphA2-Fc) bound weakly to ephrin-A1b-expressing transfectants, but bound strongly to ephrin-A1a-expressing transfectants. Ephrins have been shown to undergo regulated cleavage after interaction with their receptors. This process is inhibited by co-expression of ephrin-A1a and ephrin-A1b, indicating that ephrin-A1b influences the cleavage process. Taken together, these findings indicate that this newly described isoform may regulate the function of its ephrin-A1a counterpart.<\/jats:p>","DOI":"10.1042\/bj20031619","type":"journal-article","created":{"date-parts":[[2004,4,13]],"date-time":"2004-04-13T15:13:59Z","timestamp":1081869239000},"page":"39-46","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["A new ephrin-A1 isoform (ephrin-A1b) with altered receptor binding properties abrogates the cleavage of ephrin-A1a"],"prefix":"10.1042","volume":"379","author":[{"given":"Eivind F.","family":"FINNE","sequence":"first","affiliation":[{"name":"Department of Immunology, The Norwegian Radium Hospital, Montebello, 0310 Oslo, Norway"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Else","family":"MUNTHE","sequence":"additional","affiliation":[{"name":"Department of Immunology, The Norwegian Radium Hospital, Montebello, 0310 Oslo, Norway"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hans-Christian","family":"AASHEIM","sequence":"additional","affiliation":[{"name":"Department of Immunology, The Norwegian Radium Hospital, Montebello, 0310 Oslo, Norway"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/379\/1\/39\/713061\/bj3790039.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/379\/1\/39\/713061\/bj3790039.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,22]],"date-time":"2021-11-22T13:55:08Z","timestamp":1637589308000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/379\/1\/39\/43176\/A-new-ephrin-A1-isoform-ephrin-A1b-with-altered"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2004,4,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2004,4,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj20031619","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[2004,4,1]]}}}