{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T03:42:57Z","timestamp":1777434177619,"version":"3.51.4"},"reference-count":56,"publisher":"SAGE Publications","issue":"5","license":[{"start":{"date-parts":[[2014,2,1]],"date-time":"2014-02-01T00:00:00Z","timestamp":1391212800000},"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":[[2014,2]]},"abstract":"<jats:p>\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Significance:<\/jats:italic>\n                    <\/jats:bold>\n                    Ventilatory responses to hypoxia are initiated by the carotid body, where inhibition of specific K\n                    <jats:sup>+<\/jats:sup>\n                    channels causes cell depolarization, voltage-gated Ca\n                    <jats:sup>2+<\/jats:sup>\n                    influx, and neurotransmitter release. The identity of the upstream oxygen (O\n                    <jats:sub>2<\/jats:sub>\n                    ) sensor is still controversial.\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Recent Advances:<\/jats:italic>\n                    <\/jats:bold>\n                    The activity of BK\n                    <jats:sub>Ca<\/jats:sub>\n                    channels is regulated by O\n                    <jats:sub>2<\/jats:sub>\n                    , carbon monoxide (CO), and hydrogen sulfide (H\n                    <jats:sub>2<\/jats:sub>\n                    S), suggesting that integration of these signals may be crucial to the physiological response of this tissue. BK\n                    <jats:sub>Ca<\/jats:sub>\n                    is colocalized with hemeoxygenase-2, an enzyme that generates CO in the presence of O\n                    <jats:sub>2<\/jats:sub>\n                    , and CO is a BK\n                    <jats:sub>Ca<\/jats:sub>\n                    channel opener. Reduced CO during hypoxia results in channel closure, conferring a degree of O\n                    <jats:sub>2<\/jats:sub>\n                    sensitivity to the BK\n                    <jats:sub>Ca<\/jats:sub>\n                    channel. Conversely, H\n                    <jats:sub>2<\/jats:sub>\n                    S is a potent BK\n                    <jats:sub>Ca<\/jats:sub>\n                    inhibitor. H\n                    <jats:sub>2<\/jats:sub>\n                    S is produced endogenously by cystathionine-\u03b2-synthase and cystathionine-\u03b3-lyase in the rat carotid body, and its intracellular concentration is dependent upon the balance between its enzymatic generation and its mitochondrial breakdown. During hypoxia, mitochondrial oxidation of H\n                    <jats:sub>2<\/jats:sub>\n                    S in many tissues is reduced, leading to hypoxia-evoked rises in its concentration. This may be sufficient to inhibit K\n                    <jats:sup>+<\/jats:sup>\n                    channels and lead to carotid body excitation.\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Critical Issues:<\/jats:italic>\n                    <\/jats:bold>\n                    Carotid body function is heavily dependent upon regulated production and breakdown of CO and H\n                    <jats:sub>2<\/jats:sub>\n                    S and integration of signals from these newly emerging gasotransmitters, in combination with several other proposed mechanisms, may refine, or even define, responses of this tissue to hypoxia.\n                    <jats:bold>\n                      <jats:italic toggle=\"yes\">Future Directions:<\/jats:italic>\n                    <\/jats:bold>\n                    Since several other sensors have been postulated, the challenge of future research is to begin to integrate each in a unifying mechanism, as has been attempted for the first time herein.\n                    <jats:italic toggle=\"yes\">Antioxid. Redox Signal<\/jats:italic>\n                    . 20, 794\u2013804.\n                  <\/jats:p>","DOI":"10.1089\/ars.2013.5377","type":"journal-article","created":{"date-parts":[[2013,5,18]],"date-time":"2013-05-18T17:19:23Z","timestamp":1368897563000},"page":"794-804","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":22,"title":["Oxygen Sensing by the Carotid Body: Is It All Just Rotten Eggs?"],"prefix":"10.1177","volume":"20","author":[{"given":"Paul J.","family":"Kemp","sequence":"first","affiliation":[{"name":"Cardiff University","place":["United Kingdom"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Vsevolod","family":"Telezhkin","sequence":"additional","affiliation":[{"name":"Cardiff University","place":["United Kingdom"]}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"179","published-online":{"date-parts":[[2014,2,10]]},"reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1523\/JNEUROSCI.16-03-01066.1996"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbrc.2004.05.195"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.74.8.3203"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1152\/ajplung.00383.2006"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.87.2.682"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00424-012-1089-8"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1469-7793.2000.00135.x"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.resp.2010.09.009"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1152\/ajpheart.00331.2004"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1242\/jeb.02376"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1113\/jphysiol.1992.sp019115"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1749-6632.2009.05041.x"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrm3311"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1006\/bbrc.1997.6878"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.84.24.9265"},{"key":"e_1_3_2_17_2","first-page":"23","article-title":"Stimulation of guanylate cyclase by sodium nitroprusside, nitroglycerin and nitric oxide in various tissue preparations and comparison to the effects of sodium azide and hydroxylamine","volume":"3","author":"Katsuki S","year":"1977","unstructured":"Katsuki S, , Arnold W, , Mittal C, , and Murad F. 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