Profiling of Ubiquitination Modification Sites in Talin in Colorectal Carcinoma by Mass Spectrometry

doi:10.1007/s40242-019-8377-1

高等学校化学研究 ›› 2019, Vol. 35 ›› Issue (3): 377-381.doi: 10.1007/s40242-019-8377-1

Profiling of Ubiquitination Modification Sites in Talin in Colorectal Carcinoma by Mass Spectrometry

WANG Ke¹, QIAO Lu¹, LI Xiaoou², LI Shimeng¹, WANG Yimin¹, XU Xuesong¹, HE Chengyan¹, FANG Ling¹

1. China-Japan Union Hospital, Jilin University, Changchun 130033, P. R. China;
2. Tumor Hospital of Jilin Province, Changchun 130012, P. R. China

收稿日期:2018-12-07 修回日期:2019-01-09 出版日期:2019-06-01 发布日期:2019-03-27
通讯作者: WANG Yimin, XU Xuesong E-mail:13844038189@126.com;yiminwang@hotmail.com
基金资助:
Supported by the Fund of the Science and Technology Department of Jilin Province, China(No.20150414015GH) and the National Natural Science Foundation of China(Nos.81572082, 81472454).

Profiling of Ubiquitination Modification Sites in Talin in Colorectal Carcinoma by Mass Spectrometry

WANG Ke¹, QIAO Lu¹, LI Xiaoou², LI Shimeng¹, WANG Yimin¹, XU Xuesong¹, HE Chengyan¹, FANG Ling¹

1. China-Japan Union Hospital, Jilin University, Changchun 130033, P. R. China;
2. Tumor Hospital of Jilin Province, Changchun 130012, P. R. China

Received:2018-12-07 Revised:2019-01-09 Online:2019-06-01 Published:2019-03-27
Contact: WANG Yimin, XU Xuesong E-mail:13844038189@126.com;yiminwang@hotmail.com
Supported by:
Supported by the Fund of the Science and Technology Department of Jilin Province, China(No.20150414015GH) and the National Natural Science Foundation of China(Nos.81572082, 81472454).

摘要/Abstract

摘要： Talin protein was partially purified from human colorectal carcinoma tissues, which was subject to tryptic digestion. Immunoaffinity precipitation with specific antibodies that recognize diglycyl-lysine(Lys) remnants from tryptic digestion of ubiquitinated peptides was used to enrich ubiquitinated sites in talin. Mass spectrometry coupled with capillary reverse-phase high-performance liquid chromatography was used to analyze the enriched peptides. Specifically, four peptides containing diglycyl-Lys remnants from talin, namely, TAK(ub)VLVEDTK, QQQYK(ub) FLPSELRDEH, K(ub)STVLQQQYNR, and EGILK(ub)TAK can be determined using mass spectrometric data. This study provides an analytical method for further study in the relationship between ubiquitination modification of talin and its biological activity in colorectal cancer tissues with different pathological processes.

关键词: Talin, Ubiquitination, Colorectal carcinoma, Mass spectrometry

Abstract: Talin protein was partially purified from human colorectal carcinoma tissues, which was subject to tryptic digestion. Immunoaffinity precipitation with specific antibodies that recognize diglycyl-lysine(Lys) remnants from tryptic digestion of ubiquitinated peptides was used to enrich ubiquitinated sites in talin. Mass spectrometry coupled with capillary reverse-phase high-performance liquid chromatography was used to analyze the enriched peptides. Specifically, four peptides containing diglycyl-Lys remnants from talin, namely, TAK(ub)VLVEDTK, QQQYK(ub) FLPSELRDEH, K(ub)STVLQQQYNR, and EGILK(ub)TAK can be determined using mass spectrometric data. This study provides an analytical method for further study in the relationship between ubiquitination modification of talin and its biological activity in colorectal cancer tissues with different pathological processes.

Key words: Talin, Ubiquitination, Colorectal carcinoma, Mass spectrometry

WANG Ke, QIAO Lu, LI Xiaoou, LI Shimeng, WANG Yimin, XU Xuesong, HE Chengyan, FANG Ling. Profiling of Ubiquitination Modification Sites in Talin in Colorectal Carcinoma by Mass Spectrometry[J]. 高等学校化学研究, 2019, 35(3): 377-381.

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Profiling of Ubiquitination Modification Sites in Talin in Colorectal Carcinoma by Mass Spectrometry

Profiling of Ubiquitination Modification Sites in Talin in Colorectal Carcinoma by Mass Spectrometry

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