{"id":8077,"date":"2012-12-01T16:07:41","date_gmt":"2012-12-02T00:07:41","guid":{"rendered":"http:\/\/www.functionalps.com\/blog\/?p=8077"},"modified":"2012-12-01T16:07:41","modified_gmt":"2012-12-02T00:07:41","slug":"serotonin-activates-glycolysis","status":"publish","type":"post","link":"https:\/\/www.functionalps.com\/blog\/2012\/12\/01\/serotonin-activates-glycolysis\/","title":{"rendered":"Serotonin Activates Glycolysis"},"content":{"rendered":"

Also see:
\nTryptophan Metabolism: Effects of Progesterone, Estrogen, and PUFA<\/a>
\nEstrogen Increases Serotonin<\/a>
\nHypothyroidism and Serotonin<\/a>
\nOmega -3 \u201cDeficiency\u201d Decreases Serotonin Producing Enzyme<\/a>
\nEnzyme to Know: Tryptophan Hydroxylase<\/a>
\nTryptophan, Sleep, and Depression<\/a>
\nCarbohydrate Lowers Free Tryptophan<\/a>
\nGelatin > Whey<\/a>
\nSerotonin, Fatigue, Training, and Performance<\/a>
\nGelatin, Glycine, and Metabolism<\/a>
\nWhey, Tryptophan, & Serotonin<\/a>
\nSerotonin and Melatonin Lower Progesterone<\/a>
\nRole of Serotonin in Preeclampsia
\n<\/a>Maternal Ingestion of Tryptophan and Cancer in Female Offspring
\n<\/a>Melatonin Lowers Body Temperature<\/a><\/p>\n

Serotonin activates glycolysis, forming lactic acid. Excess lactic acid tends to decrease efficient energy production by interfering with mitochondrial respiration.<\/em> -Ray Peat, PhD<\/p>\n

Mol Genet Metab. 1998 Mar;63(3):235-8.
\nActivation of membrane skeleton-bound phosphofructokinase in erythrocytes induced by serotonin.<\/strong>
\n<\/a>Assouline-Cohen M, Ben-Porat H, Beitner R.
\nWe show here that serotonin, both in vivo and in vitro, induced a marked activation of phosphofructokinase, the rate-limiting enzyme in glycolysis, in the membrane-skeleton fraction from erythrocytes. Concomitantly, the hormone induced a striking increase in lactate content, reflecting stimulation of glycolysis.<\/strong> The enzyme’s activity in the cytosolic (soluble) fraction remained unchanged. These results suggest a defense mechanism in the erythrocytes against the damaging effects of serotonin, whose concentration in plasma increases in many diseases and is implicated as playing an important role in circulation disturbances.<\/strong><\/p>\n

Mol Genet Metab. 2007 Dec;92(4):364-70. Epub 2007 Aug 27.
\nSerotonin stimulates mouse skeletal muscle 6-phosphofructo-1-kinase through tyrosine-phosphorylation of the enzyme altering its intracellular localization.<\/a>
\n<\/strong>Coelho WS, Costa KC, Sola-Penna M.
\nSerotonin (5-HT) is a hormone implicated in the regulation of many physiological and pathological events. One of its most intriguing properties is the ability to up-regulate mitosis. Moreover, it has been shown that 5-HT stimulate glucose uptake on skeletal muscle, suggesting that 5-HT may regulate glucose metabolism of peripheric tissues. <\/strong>Here we demonstrate that 5-HT stimulates skeletal muscle 6-phosphofructo-1-kinase (PFK) activity in a dose-response manner, through 5-HT(2A) receptor subtype. Maximal activation of the enzyme (2.5-fold compared to control) is achieved in the presence of 25pM 5-HT, increasing both PFK maximal velocity and affinity for the substrate fructose-6-phosphate. These effects occur due to tyrosine phosphorylation of the enzyme that is 2-fold enhanced upon 5-HT stimulation of skeletal muscles preparation. Once 5-HT-induced tyrosine phosphorylation of PFK is prevented by genistein, a tyrosine kinase inhibitor, the hormone stimulatory effect on PFK is abrogated. Wortmannin, a phosphatidylinositol-3-kinase (PI3K) inhibitor, does not interfere on 5-HT-induced stimulation of PFK, supporting that the observed effects are independent on insulin signaling pathway. Furthermore, 5-HT promotes the association of PFK to the muscle f-actin, suggesting that the hormone alters PFK intracellular distribution, favoring its association to the cytoskeleton. Altogether, our results support evidences that 5-HT augments skeletal muscle glucose consumption through stimulation of glycolysis key regulatory enzyme, PFK, throughout tyrosine phosphorylation and intracellular redistribution of the enzyme.<\/strong><\/p>\n

Gen Pharmacol. 1994 Oct;25(6):1257-62.
\nSerotonin-induced decrease in brain ATP, stimulation of brain anaerobic glycolysis and elevation of plasma hemoglobin; the protective action of calmodulin antagonists.<\/a>
\n<\/strong>Koren-Schwartzer N, Chen-Zion M, Ben-Porat H, Beitner R.
\n1. Injection of serotonin (5-hydroxytryptamine) to rats, induced a dramatic fall in brain ATP level, accompanied by an increase in P(i). Concomitant to these changes, the activity of cytosolic phosphofructokinase, the rate-limiting enzyme of glycolysis, was significantly enhanced. Stimulation of anaerobic glycolysis was also reflected by a marked increase in lactate content in brain.<\/strong> 2. Brain glucose 1,6-bisphosphate level was decreased, whereas fructose 2,6-bisphosphate was unaffected by serotonin. 3. All these serotonin-induced changes in brain, which are characteristic for cerebral ischemia, were prevented by treatment with the calmodulin (CaM) antagonists, trifluoperazine or thioridazine. 4. Injection of serotonin also induced a marked elevation of plasma hemoglobin, reflecting lysed erythrocytes, which was also prevented by treatment with the CaM antagonists. 5. The present results suggest that CaM antagonists may be effective drugs in treatment of many pathological conditions and diseases in which plasma serotonin levels are known to increase.<\/strong><\/p>\n","protected":false},"excerpt":{"rendered":"

Also see: Tryptophan Metabolism: Effects of Progesterone, Estrogen, and PUFA Estrogen Increases Serotonin Hypothyroidism and Serotonin Omega -3 \u201cDeficiency\u201d Decreases Serotonin Producing Enzyme Enzyme to Know: Tryptophan Hydroxylase Tryptophan, Sleep, and Depression Carbohydrate Lowers Free Tryptophan Gelatin > Whey Serotonin, Fatigue, Training, and Performance Gelatin, Glycine, and Metabolism Whey, Tryptophan, & Serotonin Serotonin and Melatonin […]<\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[1],"tags":[23,72,7,1218,397,396,460,4],"class_list":["post-8077","post","type-post","status-publish","format-standard","hentry","category-general","tag-cancer","tag-disease","tag-estrogen","tag-glycolysis","tag-lactate","tag-lactic-acid","tag-serotonin","tag-stress"],"_links":{"self":[{"href":"https:\/\/www.functionalps.com\/blog\/wp-json\/wp\/v2\/posts\/8077","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.functionalps.com\/blog\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.functionalps.com\/blog\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.functionalps.com\/blog\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/www.functionalps.com\/blog\/wp-json\/wp\/v2\/comments?post=8077"}],"version-history":[{"count":3,"href":"https:\/\/www.functionalps.com\/blog\/wp-json\/wp\/v2\/posts\/8077\/revisions"}],"predecessor-version":[{"id":8080,"href":"https:\/\/www.functionalps.com\/blog\/wp-json\/wp\/v2\/posts\/8077\/revisions\/8080"}],"wp:attachment":[{"href":"https:\/\/www.functionalps.com\/blog\/wp-json\/wp\/v2\/media?parent=8077"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.functionalps.com\/blog\/wp-json\/wp\/v2\/categories?post=8077"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.functionalps.com\/blog\/wp-json\/wp\/v2\/tags?post=8077"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}