...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>The biochemical journal >Stanniocalcin 1 and 2 are secreted as phosphoproteins from human fibrosarcoma cells
【24h】

Stanniocalcin 1 and 2 are secreted as phosphoproteins from human fibrosarcoma cells

机译：桑烯酰霉素1和2分泌为来自人纤维瘤细胞的磷蛋白蛋白

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

pStanniocalcin 1 (STC1) and stanniocalcin 2 (STC2) are two recently identified mammalian peptide hormones. STC1 plays a role in calcium and phosphate homoeostasis, while the role of STC2 is unknown. We examined a human fibrosarcoma cell line, HT1080, that has high steady-state STC1 and STC2 mRNA levels, to determine whether these proteins are secreted. Following incubation of HT1080 cells with sup32/supP, labelled STC1 and STC2 were found to be secreted into the medium. STC1 was phosphorylated iin vitro/i by protein kinase C (PKC). iIn vitro/i and iin vivo/i phosphorylation both occurred exclusively on serine and the phosphopeptide maps were similar, suggesting that PKC might be the iin vivo/i kinase. STC2 was phosphorylated iin vitro/i by casein kinase II (CK2), iin vitro/i and iin vivo/i phosphorylation were exclusively on serine and the phosphopeptide maps were indistinguishable. Phosphorylation of STC2 in intact cells resulted from the action of an ecto-protein kinase, since exogenous STC2 was phosphorylated by HT1080 cells and no phosphorylated STC2 was detectable inside the cells. The ectokinase activity was abolished by heparin and GTP could substitute for ATP as the phosphate donor, indicative of an ecto-CK2-like activity. The iin vitro/i CK2 phosphorylation site was shown by matrix-assisted laser-desorption ionization–time-of-flight MS to be a single serine located between Ser-285 and Ser-298 in the C-terminal region of STC2. This is the first report of the secretion of STC1 or STC2 from mammalian cells. We conclude that these human fibrosarcoma cells express both STC1 and STC2 as secreted phosphoproteins iin vivo/i, with STC2 being phosphorylated by an ecto-CK2-like enzyme./p
机译：>辛酮蛋白1（STC1）和桑烯酰亚胺素2（STC2）是最近鉴定的哺乳动物肽激素的两个。 STC1在钙和磷酸盐同性恋中起作用，而STC2的作用是未知的。我们检查了具有高稳态STC1和STC2 mRNA水平的人纤维肉瘤HT1080，以确定这些蛋白质是否分泌。用 32℃温育HT1080细胞后，发现标记的STC1和STC2分泌到培养基中。 STC1通过蛋白激酶C（PKC）在体外磷酸化。在体外（体外）中的体外磷酸化磷酸化在丝氨酸和磷酸肽图中都是相似的，表明PKC可能是体内激酶中的。 STC2通过酪蛋白激酶II（CK2）在体外磷酸化的，在体外体外，磷酸化磷酸化在丝氨酸中，磷酸肽图难以区分。由胞外蛋白激酶的作用产生的STC2在完整细胞中的磷酸化，因为外源STC2通过HT1080细胞磷酸化，并且在细胞内没有检测磷酸化的STC2。肝素和GTP消除了非酮酶活性，GTP可以替代ATP作为磷酸盐供体，指示EcTO-CK2样活性。通过基质辅助激光解吸离子化 - 飞行时间MS显示磷酸化位点，是位于C末端区域中Ser-285和Ser-298之间的单个丝氨酸的单一丝氨酸STC2。这是来自哺乳动物细胞STC1或STC2分泌的第一个报告。我们得出结论，这些人类纤维肉瘤细胞在体内表达STC1和STC2作为分泌的磷蛋白，STC2用ECTO-CK2样酶磷酸化。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号