{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T07:48:13Z","timestamp":1790754493753,"version":"4.1.0"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1995,6,15]]},"abstract":"<jats:p>The presence of the heat shock protein (hsp-70) has been detected in exocytosed vesicles (which are named exosomes) from mammalian and avian immature red cells (i.e. reticulocytes) as well as from a differentiating avian erythroleukaemic cell line. The close, but non-covalent, association of hsp-70 with the transferrin receptor (TFR) in exosomes is demonstrated by: (1) the ability to cross-link hsp-70 to TFR; (2) the co-immunoprecipitation of hsp-70 and TFR with an antibody against TFR, and the co-immunoprecipitation of TFR and hsp-70 with antibody against hsp-70; and (3) the retention of TFR by hsp-70 bound to ATP-agarose and the simultaneous elution of both proteins by excess ATP. Semi-quantitative analysis of the relative efficiency of cross-linking of these proteins in exosomes versus plasma membranes shows that TFR in exosomes is preferentially bound to hsp-70. From an analysis of the relative amounts of hsp-70 and TFR regenerated from the cross-linked complex, the ratio of TFR monomer bound to hsp-70 is approximately 1.5 to 1. Given the presence of hsp-70 in exosomes from several species and its close association with TFR (the major protein lost during reticulocyte maturation) it is proposed that hsp-70 plays a role in exosome formation and\/or release in immature red cells.<\/jats:p>","DOI":"10.1042\/bj3080823","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:43:44Z","timestamp":1439243024000},"page":"823-830","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":82,"title":["Hsp-70 is closely associated with the transferrin receptor in exosomes from maturing reticulocytes"],"prefix":"10.1042","volume":"308","author":[{"given":"A","family":"Mathew","sequence":"first","affiliation":[{"name":"Department of Biochemistry, McGill University, 3655 Drummond St., Montr\u00e9al, Quebec, Canada H3G 1Y6"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A","family":"Bell","sequence":"additional","affiliation":[{"name":"Sheldon Biotechnology Institute, McGill University, Montreal, Canada."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R M","family":"Johnstone","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, McGill University, 3655 Drummond St., Montr\u00e9al, Quebec, Canada H3G 1Y6"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/308\/3\/823\/620861\/bj3080823.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/308\/3\/823\/620861\/bj3080823.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,23]],"date-time":"2021-11-23T23:37:21Z","timestamp":1637710641000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/308\/3\/823\/31908\/Hsp-70-is-closely-associated-with-the-transferrin"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1995,6,15]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1995,6,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj3080823","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1995,6,15]]}}}