S B Matthews, M B Hallett, A H Henderson, A K Campbell
{"title":"肾上腺素色素途径。炎症性疾病中肾上腺素代谢的潜在分解代谢途径。","authors":"S B Matthews, M B Hallett, A H Henderson, A K Campbell","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Polymorphonuclear leukocytes activated by latex (polystyrene) beads or the chemotactic peptide N-formyl Met Leu Phe stimulated the oxidation of adrenaline (0.3 microM-10 mM) to adrenochrome, detected spectrophotometrically at 480 nm or by a high-performance liquid chromatographic (HPLC) method. This oxidation was detectable within 5 min and continued for at least 4 hr. Over the concentration range 0.3-10 microM, more than 80% of the adrenaline oxidation occurred via the adrenochrome pathway rather than the amine oxidase-catechol methyltransferase pathway. Medium isolated after stimulation of the polymorphonuclear leukocytes retained the ability to oxidize adrenaline to adrenochrome. Serum from patients after myocardial infarction induced more oxidation of adrenaline to adrenochrome than control serum. Superoxide dismutase, catalase, and azide inhibited by 70-95% the oxidation of adrenaline to adrenochrome, either by cells or medium. Commercially available adrenochrome was biologically active, but some of the actions were due to contaminants of the preparation. HPLC of an extract of synovial fluid from a patient with rheumatoid arthritis, a fluid that contains polymorphonuclear leukocytes, showed a peak identical to that of the adrenochrome standard. The results provide a cellular mechanism for adrenochrome formation and preliminary evidence that adrenochrome can be produced in inflammatory conditions in which polymorphonuclear leukocyte infiltration occurs.</p>","PeriodicalId":77831,"journal":{"name":"Advances in myocardiology","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1985-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"The adrenochrome pathway. A potential catabolic route for adrenaline metabolism in inflammatory disease.\",\"authors\":\"S B Matthews, M B Hallett, A H Henderson, A K Campbell\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Polymorphonuclear leukocytes activated by latex (polystyrene) beads or the chemotactic peptide N-formyl Met Leu Phe stimulated the oxidation of adrenaline (0.3 microM-10 mM) to adrenochrome, detected spectrophotometrically at 480 nm or by a high-performance liquid chromatographic (HPLC) method. This oxidation was detectable within 5 min and continued for at least 4 hr. Over the concentration range 0.3-10 microM, more than 80% of the adrenaline oxidation occurred via the adrenochrome pathway rather than the amine oxidase-catechol methyltransferase pathway. Medium isolated after stimulation of the polymorphonuclear leukocytes retained the ability to oxidize adrenaline to adrenochrome. Serum from patients after myocardial infarction induced more oxidation of adrenaline to adrenochrome than control serum. Superoxide dismutase, catalase, and azide inhibited by 70-95% the oxidation of adrenaline to adrenochrome, either by cells or medium. Commercially available adrenochrome was biologically active, but some of the actions were due to contaminants of the preparation. HPLC of an extract of synovial fluid from a patient with rheumatoid arthritis, a fluid that contains polymorphonuclear leukocytes, showed a peak identical to that of the adrenochrome standard. The results provide a cellular mechanism for adrenochrome formation and preliminary evidence that adrenochrome can be produced in inflammatory conditions in which polymorphonuclear leukocyte infiltration occurs.</p>\",\"PeriodicalId\":77831,\"journal\":{\"name\":\"Advances in myocardiology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1985-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Advances in myocardiology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Advances in myocardiology","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
摘要
多形核白细胞被乳胶(聚苯乙烯)珠或趋化肽n -甲酰基Met Leu Phe激活,刺激肾上腺素(0.3微米-10毫米)氧化为肾上腺素色素,在480 nm分光光度法或高效液相色谱(HPLC)法检测。这种氧化在5分钟内可检测到,并持续至少4小时。在0.3 ~ 10微米的浓度范围内,80%以上的肾上腺素氧化是通过肾上腺素色素途径发生的,而不是通过胺氧化酶-儿茶酚甲基转移酶途径。刺激多形核白细胞后分离的培养基保留了将肾上腺素氧化为肾上腺素色素的能力。心肌梗死患者血清中肾上腺素氧化为肾上腺素色素的程度高于对照血清。超氧化物歧化酶、过氧化氢酶和叠氮化物被细胞或培养基抑制70-95%肾上腺素氧化为肾上腺素色素。市售肾上腺素色素具有生物活性,但有些活性是由于制备过程中的污染物造成的。类风湿性关节炎患者的滑膜液(一种含有多形核白细胞的液体)提取物的高效液相色谱显示出与肾上腺素色素标准相同的峰值。结果提供了肾上腺素色素形成的细胞机制,并初步证明肾上腺素色素可以在多形核白细胞浸润发生的炎症条件下产生。
The adrenochrome pathway. A potential catabolic route for adrenaline metabolism in inflammatory disease.
Polymorphonuclear leukocytes activated by latex (polystyrene) beads or the chemotactic peptide N-formyl Met Leu Phe stimulated the oxidation of adrenaline (0.3 microM-10 mM) to adrenochrome, detected spectrophotometrically at 480 nm or by a high-performance liquid chromatographic (HPLC) method. This oxidation was detectable within 5 min and continued for at least 4 hr. Over the concentration range 0.3-10 microM, more than 80% of the adrenaline oxidation occurred via the adrenochrome pathway rather than the amine oxidase-catechol methyltransferase pathway. Medium isolated after stimulation of the polymorphonuclear leukocytes retained the ability to oxidize adrenaline to adrenochrome. Serum from patients after myocardial infarction induced more oxidation of adrenaline to adrenochrome than control serum. Superoxide dismutase, catalase, and azide inhibited by 70-95% the oxidation of adrenaline to adrenochrome, either by cells or medium. Commercially available adrenochrome was biologically active, but some of the actions were due to contaminants of the preparation. HPLC of an extract of synovial fluid from a patient with rheumatoid arthritis, a fluid that contains polymorphonuclear leukocytes, showed a peak identical to that of the adrenochrome standard. The results provide a cellular mechanism for adrenochrome formation and preliminary evidence that adrenochrome can be produced in inflammatory conditions in which polymorphonuclear leukocyte infiltration occurs.