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由猫肉瘤病毒麦克多诺株转化的细胞表面所表达的gp140v - fms分子在酪氨酸和丝氨酸处发生磷酸化。

gp140v-fms molecules expressed at the surface of cells transformed by the McDonough strain of feline sarcoma virus are phosphorylated in tyrosine and serine.

作者信息

Tamura T, Simon E, Niemann H, Snoek G T, Bauer H

出版信息

Mol Cell Biol. 1986 Dec;6(12):4745-8. doi: 10.1128/mcb.6.12.4745-4748.1986.

Abstract

Cells transformed by the McDonough strain of feline sarcoma virus express at their surface a v-fms-specific transmembrane glycoprotein designated gp140v-fms. By labeling with 32Pi, gp140v-fms was shown to be phosphorylated 30-fold more in serine residues than were the cytosolic v-fms polypeptides gp180gag-fms and gp120v-fms. By using the phosphotyrosine phosphatase-specific inhibitor sodium orthovanadate, an additional tyrosine phosphorylation was observed in vivo, again involving predominantly gp140v-fms. In vitro studies showed that the v-fms proteins were phosphorylated by protein kinase C in a calcium- and phosphatidylserine-dependent manner.

摘要

被猫肉瘤病毒麦克多诺株转化的细胞在其表面表达一种v-fms特异性跨膜糖蛋白,命名为gp140v-fms。通过用32Pi标记,发现gp140v-fms在丝氨酸残基上的磷酸化程度比胞质v-fms多肽gp180gag-fms和gp120v-fms高30倍。通过使用磷酸酪氨酸磷酸酶特异性抑制剂原钒酸钠,在体内观察到了额外的酪氨酸磷酸化,同样主要涉及gp140v-fms。体外研究表明,v-fms蛋白被蛋白激酶C以钙和磷脂酰丝氨酸依赖的方式磷酸化。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a81e/367261/d07f7fe6f803/molcellb00096-0612-a.jpg

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