人促肾上腺皮质激素合成片段的酯酶活性

Esterase activity of synthetic fragments of human adrenocorticotrophic hormone.

作者信息

Eklund K K, Vainio P, Virtanen J A, Kinnunen P K

机构信息

Department of Medical Chemistry, University of Helsinki, Finland.

出版信息

Biochem Biophys Res Commun. 1991 May 31;177(1):235-42. doi: 10.1016/0006-291x(91)91973-g.

DOI:10.1016/0006-291x(91)91973-g

PMID:1645957

Abstract

The anterior pituitary hormone adrenocorticotrophin (ACTH) has been extensively studied in terms of structure-function relationships and in vivo and in vitro activities of different synthetic fragments of ACTH have been characterized. Here we describe the ability of synthetic fragments of ACTH to hydrolyze a fluorogenic esterase substrate 4-methylumbelliferyloleate (MUBO). The measured esterase activities (in mumol 4-MU mol-1 s-1) were 79.7 for ACTH1-13, 385.9 for ACTH3-18, 503.0 for ACTH1-19, 1249.9 for ACTH1-24 D-ser3, and 1350 for ACTH1-24. Although the significance of the observed esterase activities in the actual molecular mechanisms of action of ACTH remains to be established it is worth noticing that the esterase activities of the different ACTH fragments closely parallel their reported ability to activate the brain lipase as well as their in vivo ability to induce steroidogenesis in adrenal cortex.

摘要

垂体前叶激素促肾上腺皮质激素（ACTH）在结构 - 功能关系方面已得到广泛研究，并且不同ACTH合成片段的体内和体外活性也已得到表征。在此，我们描述了ACTH合成片段水解荧光酯酶底物4 - 甲基伞形酮油酸酯（MUBO）的能力。所测得的酯酶活性（以μmol 4 - MU mol⁻¹ s⁻¹为单位）分别为：ACTH1 - 13为79.7，ACTH3 - 18为385.9，ACTH1 - 19为503.0，ACTH1 - 24 D - ser3为1249.9，ACTH1 - 24为1350。尽管所观察到的酯酶活性在ACTH实际分子作用机制中的意义尚待确定，但值得注意的是，不同ACTH片段的酯酶活性与其报道的激活脑脂肪酶的能力以及其在体内诱导肾上腺皮质类固醇生成的能力密切平行。