{"id":71,"date":"2018-10-21T02:25:34","date_gmt":"2018-10-21T09:25:34","guid":{"rendered":"http:\/\/kinaseinhibitorlibrary.com\/?p=71"},"modified":"2022-01-13T16:31:18","modified_gmt":"2022-01-13T09:31:18","slug":"thermogenesis-activated-respiratory-substrate-complex","status":"publish","type":"post","link":"http:\/\/kinaseinhibitorlibrary.com\/index.php\/2018\/10\/21\/thermogenesis-activated-respiratory-substrate-complex\/","title":{"rendered":"Thermogenesis was activated by respiratory substrate of complex"},"content":{"rendered":"<p>In this report, thermogenesis was activated by respiratory substrate of complex 1 in media without added ATP. At present, it is not clear to us what the role of SERCA 1 in BAT mitochondria is. The following hypothetical possibilities are raised: in the particular case of BAT, Ca2+ would be released in mitochondria via the MAM as previously reported for other tissues. However the excess of Ca2+ would not be alleviated solely via MAM; it could also be pumped out of the mitochondria by the SERCA 1 located in mitochondrial <a href=\"http:\/\/www.abmole.com\/products\/boc-d-fmk.html\">BOC-D-FMK<\/a> cristae; SERCA 1 would be involved in the activation of thermogenesis promoted by the addition of low Ca2+ concentrations in the assay medium. In favor of this hypothesis are the following findings: the Ca2+ concentration needed for halfmaximal heat production is in the same range as the Ca2+ concentration needed to pump Ca2+ in vesicles derived from skeletal muscle sarcoplasmic reticulum ; Ca2+ activates only heat production and has no influence in the rate of oligomycin-sensitive ATP synthesis; In the presence of Ca2+, there is a significant discrepancy between the rates of oxygen <a href=\"http:\/\/www.abmole.com\/products\/bttaa.html\">BTTAA<\/a> consumption and heat production. This could be best seen in uncoupled mitochondria where all energy derived from respiration is dissipated as heat and none is used for oligomycin-sensitive ATP synthesis. Although Ca2+ activated both respiration and heat production, the enhancement of respiration was,30%, while activation of heat production was,60%. The amount of energy derived from each K O2 consumed is 52.6 kcal. In absence of Ca2+, the heat measured was slightly higher than the heat calculated from K O2 consumed, while in presence of Ca2+ it was 60% higher. This discrepancy may indicate that Ca2+ activates a thermogenic process that is not active in the presence of excess EGTA. The fact that heat production in the presence of either Ca2+ or EGTA was impaired by rotenone and cyanide indicates that the activation of heat production by Ca2+ is linked to flux of electrons through the cytochrome chain. SERCA 1 has been shown to be able to interconvert different forms of energy to synthesize ATP from ADP and Pi. These include energies derived from a gradient of Ca2+, pH, water activity or even thermal energy.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>In this report, thermogenesis was activated by respiratory substrate of complex 1 in media without added ATP. At present, it is not clear to us what the role of SERCA 1 in BAT mitochondria is. The following hypothetical possibilities are raised: in the particular case of BAT, Ca2+ would be released in mitochondria via the &hellip; <a href=\"http:\/\/kinaseinhibitorlibrary.com\/index.php\/2018\/10\/21\/thermogenesis-activated-respiratory-substrate-complex\/\" class=\"more-link\">Continue reading <span class=\"screen-reader-text\">Thermogenesis was activated by respiratory substrate of complex<\/span><\/a><\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":[],"categories":[1],"tags":[],"_links":{"self":[{"href":"http:\/\/kinaseinhibitorlibrary.com\/index.php\/wp-json\/wp\/v2\/posts\/71"}],"collection":[{"href":"http:\/\/kinaseinhibitorlibrary.com\/index.php\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"http:\/\/kinaseinhibitorlibrary.com\/index.php\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"http:\/\/kinaseinhibitorlibrary.com\/index.php\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"http:\/\/kinaseinhibitorlibrary.com\/index.php\/wp-json\/wp\/v2\/comments?post=71"}],"version-history":[{"count":1,"href":"http:\/\/kinaseinhibitorlibrary.com\/index.php\/wp-json\/wp\/v2\/posts\/71\/revisions"}],"predecessor-version":[{"id":72,"href":"http:\/\/kinaseinhibitorlibrary.com\/index.php\/wp-json\/wp\/v2\/posts\/71\/revisions\/72"}],"wp:attachment":[{"href":"http:\/\/kinaseinhibitorlibrary.com\/index.php\/wp-json\/wp\/v2\/media?parent=71"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"http:\/\/kinaseinhibitorlibrary.com\/index.php\/wp-json\/wp\/v2\/categories?post=71"},{"taxonomy":"post_tag","embeddable":true,"href":"http:\/\/kinaseinhibitorlibrary.com\/index.php\/wp-json\/wp\/v2\/tags?post=71"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}