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肾素通过一种不需要前肽表达的机制,在转染的PC12细胞中被分选到调节性分泌途径。

Renin is sorted to the regulated secretory pathway in transfected PC12 cells by a mechanism which does not require expression of the pro-peptide.

作者信息

Chidgey M A, Harrison T M

机构信息

Department of Biochemistry, University of Leicester, England.

出版信息

Eur J Biochem. 1990 May 31;190(1):139-44. doi: 10.1111/j.1432-1033.1990.tb15556.x.

DOI:10.1111/j.1432-1033.1990.tb15556.x
PMID:2194793
Abstract

The rat pheochromocytoma cell line PC12 targets secretory proteins into two distinct pathways. When DNA encoding human prorenin was transfected into PC12 cells, the protein was sorted into the regulated secretory pathway and released with similar kinetics to noradrenaline upon carbachol stimulation. To determine whether information for targeting prorenin lies within the pro-peptide we have transfected PC12 cells with a construct lacking the pro-peptide coding sequence. The transformed line secretes an apparently fully active enzyme and responds to carbachol stimulation with a rapid release of renin activity. We conclude that the pro-peptide of renin is not essential for targeting the protein to the regulated pathway in PC12 cells.

摘要

大鼠嗜铬细胞瘤细胞系PC12将分泌蛋白导向两条不同的途径。当将编码人肾素原的DNA转染到PC12细胞中时,该蛋白被分选到调节性分泌途径中,并在卡巴胆碱刺激下以与去甲肾上腺素相似的动力学释放。为了确定肾素原靶向的信息是否存在于前肽中,我们用一个缺乏前肽编码序列的构建体转染了PC12细胞。转化后的细胞系分泌一种显然完全有活性的酶,并在卡巴胆碱刺激下快速释放肾素活性。我们得出结论,肾素的前肽对于将该蛋白靶向PC12细胞中的调节途径不是必需的。

相似文献

1
Renin is sorted to the regulated secretory pathway in transfected PC12 cells by a mechanism which does not require expression of the pro-peptide.肾素通过一种不需要前肽表达的机制,在转染的PC12细胞中被分选到调节性分泌途径。
Eur J Biochem. 1990 May 31;190(1):139-44. doi: 10.1111/j.1432-1033.1990.tb15556.x.
2
A targeting sequence for dense secretory granules resides in the active renin protein moiety of human preprorenin.致密分泌颗粒的靶向序列存在于人类前肾素原的活性肾素蛋白部分中。
Mol Endocrinol. 1990 Dec;4(12):1905-13. doi: 10.1210/mend-4-12-1905.
3
The pro-peptide is not necessary for active renin secretion from transfected mammalian cells.前肽对于转染的哺乳动物细胞分泌活性肾素并非必需。
Proteins. 1989;5(4):259-65. doi: 10.1002/prot.340050402.
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Different secretory pathways of renin from mouse cells transfected with the human renin gene.用人肾素基因转染的小鼠细胞中肾素的不同分泌途径。
J Biol Chem. 1988 Mar 5;263(7):3137-41.
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Sta!le and transient expression of mouse submaxillary gland renin cDNA in AtT20 cells: proteolytic processing and secretory pathways.小鼠颌下腺肾素cDNA在AtT20细胞中的稳定和瞬时表达:蛋白水解加工及分泌途径
FEBS Lett. 1989 Mar 13;245(1-2):70-4. doi: 10.1016/0014-5793(89)80194-2.
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Post-translational processing and secretory pathway of human atriopeptin in rat pheochromocytoma cells.人心房肽在大鼠嗜铬细胞瘤细胞中的翻译后加工及分泌途径
Biochem Biophys Res Commun. 1991 May 15;176(3):1232-8. doi: 10.1016/0006-291x(91)90417-6.
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Effects of propeptide deletion on human renin secretion from mouse pituitary AtT-20 cells.前肽缺失对小鼠垂体AtT-20细胞分泌人肾素的影响。
FEBS Lett. 1990 May 7;264(1):67-70. doi: 10.1016/0014-5793(90)80766-c.
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Lithium augments fos protoonocogene expression in PC12 pheochromocytoma cells: implications for therapeutic action of lithium.锂可增强PC12嗜铬细胞瘤细胞中fos原癌基因的表达:对锂治疗作用的启示。
Brain Res. 1990 Jun 25;521(1-2):47-54. doi: 10.1016/0006-8993(90)91523-j.
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Prorenin is sorted into the regulated secretory pathway independent of its processing to renin in mouse pituitary AtT-20 cells.
FEBS Lett. 1989 Oct 23;257(1):89-92. doi: 10.1016/0014-5793(89)81793-4.
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Atrial natriuretic factor inhibits norepinephrine release in an adrenergic clonal cell line (PC12).心房利钠因子抑制肾上腺素能克隆细胞系(PC12)中去甲肾上腺素的释放。
Eur J Pharmacol. 1988 May 20;150(1-2):175-9. doi: 10.1016/0014-2999(88)90765-0.

引用本文的文献

1
Two dipolar α-helices within hormone-encoding regions of proglucagon are sorting signals to the regulated secretory pathway.胰高血糖素原激素编码区域内的两个偶极α螺旋是调节性分泌途径的分选信号。
J Biol Chem. 2014 May 23;289(21):14968-80. doi: 10.1074/jbc.M114.563684. Epub 2014 Apr 11.
2
Secretory protein traffic. Chromogranin A contains a dominant targeting signal for the regulated pathway.分泌蛋白运输。嗜铬粒蛋白A含有一个用于调节途径的主要靶向信号。
J Clin Invest. 1993 Aug;92(2):1042-54. doi: 10.1172/JCI116609.
3
Processing and sorting of human prorenin.
人肾素原的加工与分选
Cell Biophys. 1991 Oct-Dec;19(1-3):63-71. doi: 10.1007/BF02989880.