{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T03:46:21Z","timestamp":1790739981247,"version":"4.1.0"},"reference-count":200,"publisher":"SAGE Publications","issue":"1","license":[{"start":{"date-parts":[[2014,7,1]],"date-time":"2014-07-01T00:00:00Z","timestamp":1404172800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":["journals.sagepub.com"],"crossmark-restriction":true},"short-container-title":["Antioxidants &amp; Redox Signaling"],"published-print":{"date-parts":[[2014,7]]},"abstract":"<jats:p>\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Significance:<\/jats:italic>\n                    <\/jats:bold>\n                    Eryptosis, the suicidal erythrocyte death, is characterized by cell shrinkage, membrane blebbing, and phosphatidylserine translocation to the outer membrane leaflet. Phosphatidylserine at the erythrocyte surface binds endothelial CXCL16\/SR-PSOX (CXC-Motiv-Chemokin-16\/Scavenger-receptor-for-phosphatidylserine-and-oxidized-low-density-lipoprotein) and fosters engulfment of affected erythrocytes by phagocytosing cells. Eryptosis serves to eliminate infected or defective erythrocytes, but excessive eryptosis may lead to anemia and may interfere with microcirculation. Clinical conditions with excessive eryptosis include diabetes, chronic renal failure, hemolytic uremic syndrome, sepsis, malaria, iron deficiency, sickle cell anemia, thalassemia, glucose 6-phosphate dehydrogenase deficiency, glutamate cysteine ligase modulator deficiency, and Wilson's disease.\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Recent Advances:<\/jats:italic>\n                    <\/jats:bold>\n                    Eryptosis is triggered by a wide variety of xenobiotics and other injuries such as oxidative stress. Signaling of eryptosis includes prostaglandin E\n                    <jats:sub>2<\/jats:sub>\n                    formation with subsequent activation of Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -permeable cation channels, Ca\n                    <jats:sup>2+<\/jats:sup>\n                    entry, activation of Ca\n                    <jats:sup>2+<\/jats:sup>\n                    -sensitive K\n                    <jats:sup>+<\/jats:sup>\n                    channels, and cell membrane scrambling, as well as phospholipase A\n                    <jats:sub>2<\/jats:sub>\n                    stimulation with release of platelet-activating factor, sphingomyelinase activation, and ceramide formation. Eryptosis may involve stimulation of caspases and calpain with subsequent degradation of the cytoskeleton. It is regulated by AMP-activated kinase, cGMP-dependent protein kinase, Janus-activated kinase 3, casein kinase 1\u03b1, p38 kinase, and p21-activated kinase 2. It is inhibited by erythropoietin, antioxidants, and further small molecules.\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Critical Issues:<\/jats:italic>\n                    <\/jats:bold>\n                    It remains uncertain for most disorders whether eryptosis is rather beneficial because it precedes and thus prevents hemolysis or whether it is harmful because of induction of anemia and impairment of microcirculation.\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Future Directions:<\/jats:italic>\n                    <\/jats:bold>\n                    This will address the significance of eryptosis, further mechanisms underlying eryptosis, and additional pharmacological tools fostering or inhibiting eryptosis.\n                    <jats:italic toggle=\"yes\">Antioxid. Redox Signal.<\/jats:italic>\n                    21, 138\u2013153.\n                  <\/jats:p>","DOI":"10.1089\/ars.2013.5747","type":"journal-article","created":{"date-parts":[[2013,12,20]],"date-time":"2013-12-20T10:11:48Z","timestamp":1387534308000},"page":"138-153","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":132,"title":["Oxidative Stress and Suicidal Erythrocyte Death"],"prefix":"10.1177","volume":"21","author":[{"given":"Florian","family":"Lang","sequence":"first","affiliation":[{"name":"University of T\u00fcbingen","place":["Germany"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Majed","family":"Abed","sequence":"additional","affiliation":[{"name":"University of T\u00fcbingen","place":["Germany"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elisabeth","family":"Lang","sequence":"additional","affiliation":[{"name":"University of T\u00fcbingen","place":["Germany"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"F\u00f6ller","sequence":"additional","affiliation":[{"name":"University of T\u00fcbingen","place":["Germany"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"179","published-online":{"date-parts":[[2014,7,1]]},"reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1152\/ajpcell.00239.2012"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.tox.2012.10.006"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1053\/j.ackd.2008.12.009"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI112294"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1159\/000350141"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1097\/00062752-199903000-00004"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jprot.2011.04.009"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1159\/000089839"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1111\/bjh.12185"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrneph.2011.115"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.semnephrol.2011.11.008"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1203\/01.pdr.0000203098.77573.39"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)41289-1"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.46.10.3180-3184.2002"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1182\/blood-2003-11-3820"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1155\/2012\/819310"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1159\/000083634"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2141.2008.06995.x"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1891\/0730-0832.18.2.9"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.1038\/ncb0705-645"},{"key":"e_1_3_2_22_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.cdd.4400905"},{"key":"e_1_3_2_23_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrneph.2010.139"},{"key":"e_1_3_2_24_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.trsl.2008.07.007"},{"key":"e_1_3_2_25_2","doi-asserted-by":"publisher","DOI":"10.1159\/000329956"},{"key":"e_1_3_2_26_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0009-8981(00)00384-3"},{"key":"e_1_3_2_27_2","first-page":"193","article-title":"Activation of calcium-dependent potassium channels in deoxygenated sickled red cells","volume":"240","author":"Bookchin RM","year":"1987","unstructured":"Bookchin RM, , Ortiz OE, , and Lew VL. 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