Chemical Research in Chinese Universities ›› 2019, Vol. 35 ›› Issue (3): 377-381.doi: 10.1007/s40242-019-8377-1

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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. 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).

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