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干扰素γ可诱导巨噬细胞中一种48 kDa蛋白的豆蔻酰化。

Interferon gamma induces the myristoylation of a 48-kDa protein in macrophages.

作者信息

Aderem A A, Marratta D E, Cohn Z A

机构信息

Laboratory of Cellular Physiology and Immunology, Rockefeller University, New York, NY 10021.

出版信息

Proc Natl Acad Sci U S A. 1988 Sep;85(17):6310-3. doi: 10.1073/pnas.85.17.6310.

DOI:10.1073/pnas.85.17.6310
PMID:3137568
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC281959/
Abstract

The lymphokine interferon gamma (IFN-gamma) induces the selective myristoylation of a macrophage protein with an apparent molecular mass of 48 kDa. The myristic acid-protein bond is resistant to treatment with hydroxylamine, suggesting that the fatty acid moiety is in an amide linkage. As little as 1 unit of IFN-gamma per ml induces the myristoylation of the 48-kDa protein, with half-maximal myristoylation being observed with 4 units/ml. The effect is observed within 1 hr after exposure to IFN-gamma and is maximal by 3-4 hr, after which it declines. IFN-alpha does not induce the myristoylation of the 48-kDa protein, and IFN-beta does so very poorly. Neither IFN-alpha nor IFN-beta has any effect on IFN-gamma-induced myristoylation of the 48-kDa protein. The 48-kDa protein is constitutively myristoylated in murine macrophages that have been activated in vivo by intraperitoneal injection of Corynebacterium parvum, suggesting that it may be an early intermediate in the activation of macrophages.

摘要

淋巴因子γ干扰素(IFN-γ)可诱导一种表观分子量为48 kDa的巨噬细胞蛋白发生选择性肉豆蔻酰化。肉豆蔻酸与蛋白的键对羟胺处理具有抗性,这表明脂肪酸部分是以酰胺键连接的。每毫升低至1单位的IFN-γ即可诱导48 kDa蛋白的肉豆蔻酰化,在4单位/毫升时观察到半最大肉豆蔻酰化。在暴露于IFN-γ后1小时内即可观察到这种效应,3至4小时达到最大值,之后下降。IFN-α不会诱导48 kDa蛋白的肉豆蔻酰化,IFN-β诱导效果也很差。IFN-α和IFN-β对IFN-γ诱导的48 kDa蛋白肉豆蔻酰化均无任何影响。在通过腹腔注射微小棒状杆菌在体内被激活的小鼠巨噬细胞中,48 kDa蛋白组成性地发生肉豆蔻酰化,这表明它可能是巨噬细胞激活过程中的早期中间体。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5f63/281959/578375629da9/pnas00296-0093-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5f63/281959/7485f510f8f9/pnas00296-0092-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5f63/281959/922d8ba85691/pnas00296-0092-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5f63/281959/209c8d865ad3/pnas00296-0093-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5f63/281959/532ee9b1020f/pnas00296-0093-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5f63/281959/578375629da9/pnas00296-0093-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5f63/281959/7485f510f8f9/pnas00296-0092-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5f63/281959/922d8ba85691/pnas00296-0092-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5f63/281959/209c8d865ad3/pnas00296-0093-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5f63/281959/532ee9b1020f/pnas00296-0093-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5f63/281959/578375629da9/pnas00296-0093-c.jpg

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本文引用的文献

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Identification of the NH2-terminal blocking group of calcineurin B as myristic acid.鉴定钙调神经磷酸酶B的氨基末端封闭基团为肉豆蔻酸。
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