{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,11]],"date-time":"2026-06-11T05:33:37Z","timestamp":1781156017081,"version":"3.54.1"},"reference-count":38,"publisher":"MathDoc\/Centre Mersenne","issue":"2","license":[{"start":{"date-parts":[[2014,12,24]],"date-time":"2014-12-24T00:00:00Z","timestamp":1419379200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":["em-consulte.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":[],"abstract":"<jats:p id=\"spar0005\">Hemoglobin-based oxygen carriers (HBOCs) may generate oxidative stress, vasoconstriction and inflammation. To reduce these undesirable vasoactive properties, we increased hemoglobin (Hb) molecular size by genetic engineering with octameric Hb, recombinant (r) Hb\u03b2G83C. We investigate the potential side effects of rHb\u03b2G83C on endothelial cells. The rHb\u03b2G83C has no impact on cell viability, and induces a huge repression of endothelial nitric oxide synthase gene transcription, a marker of vasomotion. No induction of Intermolecular-Adhesion Molecule 1 and E-selectin (inflammatory markers) transcription was seen. In the presence of rHb\u03b2G83C, the transcription of heme oxygenase-1 (oxidative stress marker) is weakly increased compared to the two other HBOCs (references) or Voluven (control). This genetically engineered octameric Hb, based on a human Hb \u03b2G83C mutant, leads to little impact at the level of endothelial cell inflammatory response and thus appears as an interesting molecule for HBOC development.<\/jats:p>","DOI":"10.1016\/j.crvi.2014.11.004","type":"journal-article","created":{"date-parts":[[2014,12,24]],"date-time":"2014-12-24T08:48:50Z","timestamp":1419410930000},"page":"95-102","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"title":["Interaction of recombinant octameric hemoglobin with endothelial cells"],"prefix":"10.5802","volume":"338","author":[{"given":"Caroline","family":"Gaucher","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"\u00c9lisa","family":"Domingues-Hamdi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christine","family":"Prin-Mathieu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrick","family":"Menu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"V\u00e9ronique","family":"Baudin-Creuza","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"3842","published-online":{"date-parts":[[2014,12,24]]},"reference":[{"key":"key2025102316383933661_1","doi-asserted-by":"crossref","first-page":"2314","DOI":"10.1089\/ars.2012.4917","article-title":"Development of recombinant hemoglobin-based oxygen carriers","volume":"18","author":"Varnado, C.L.","year":"2013","unstructured":"[1] Varnado, C.L.; Mollan, T.L.; Birukou, I.; Smith, B.J.; Henderson, D.P.; Olson, J.S. Development of recombinant hemoglobin-based oxygen carriers, Antioxid. Redox. Signal., Volume 18 (2013), pp. 2314-2328","journal-title":"Antioxid. Redox. Signal."},{"key":"key2025102316383933661_2","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1038\/356258a0","article-title":"A human recombinant haemoglobin designed for use as a blood substitute","volume":"35","author":"Looker, D.","year":"1992","unstructured":"[2] Looker, D.; Abbott-Brown, D.; Cozart, P.; Durfee, S.; Hoffman, S.; Mathews, A.J.; Miller-Roehrich, J.; Shoemaker, S.; Trimble, S.; Fermi, G.; Komiyama, N.H.; Nagai, K.; Stetler, G.L. 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Stable octameric structure of recombinant hemoglobin alpha(2)beta(2)83 Gly\u2192Cys, Protein Sci., Volume 12 (2003), pp. 690-695","journal-title":"Protein Sci."},{"key":"key2025102316383933661_16","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1111\/j.1742-4658.2005.05063.x","article-title":"Recombinant hemoglobin \u03b2G83CF41Y: an octameric protein","volume":"273","author":"Vasseur-Godbillon, C.","year":"2006","unstructured":"[16] Vasseur-Godbillon, C.; Sahu, S.C.; Domingues, E.; Fablet, C.; Giovannelli, J.L.; Tam, T.C.; Ho, N.T.; Ho, C.; Marden, M.C.; Baudin-Creuza, V. 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