A target-specific approach for the identification of tyrosine-sulfated hemostatic proteins

Tzu An Liu; Shin Yasuda; Frederick E. Williams; Ming Yih Liu; Masahito Suiko; Yoichi Sakakibara; Yuh-Shyong Yang; Ming Cheh Liu

doi:10.1016/j.ab.2009.04.002

A target-specific approach for the identification of tyrosine-sulfated hemostatic proteins

Tzu An Liu, Shin Yasuda, Frederick E. Williams, Ming Yih Liu, Masahito Suiko, Yoichi Sakakibara, Yuh-Shyong Yang, Ming Cheh Liu^*

^*Corresponding author for this work

Department of Biological Science and Technology

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

A simple methodology for the identification of hemostatic proteins that are subjected to posttranslational tyrosine sulfation was developed. The procedure involves sequence analysis of members of the three hemostatic pathways using the Sulfinator prediction algorithm, followed by [³⁵S]sulfate labeling of cultured HepG2 human hepatoma cells, immunoprecipitation of targeted [³⁵S]sulfate-labeled hemostatic proteins, and tyrosine O-[³⁵S]sulfate analysis of immunoprecipitated proteins. Three new tyrosine-sulfated hemostatic proteins-protein S, prekallikrein, and plasminogen-were identified. Such a target-specific approach will allow investigation of tyrosine-sulfated proteins of other biochemical/physiological pathways/processes and contribute to a better understanding of the functional role of posttranslational tyrosine sulfation.

Original language	English
Pages (from-to)	88-90
Number of pages	3
Journal	Analytical Biochemistry
Volume	390
Issue number	1
DOIs	https://doi.org/10.1016/j.ab.2009.04.002
State	Published - 1 Jul 2009

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title = "A target-specific approach for the identification of tyrosine-sulfated hemostatic proteins",

abstract = "A simple methodology for the identification of hemostatic proteins that are subjected to posttranslational tyrosine sulfation was developed. The procedure involves sequence analysis of members of the three hemostatic pathways using the Sulfinator prediction algorithm, followed by [35S]sulfate labeling of cultured HepG2 human hepatoma cells, immunoprecipitation of targeted [35S]sulfate-labeled hemostatic proteins, and tyrosine O-[35S]sulfate analysis of immunoprecipitated proteins. Three new tyrosine-sulfated hemostatic proteins-protein S, prekallikrein, and plasminogen-were identified. Such a target-specific approach will allow investigation of tyrosine-sulfated proteins of other biochemical/physiological pathways/processes and contribute to a better understanding of the functional role of posttranslational tyrosine sulfation.",

author = "Liu, {Tzu An} and Shin Yasuda and Williams, {Frederick E.} and Liu, {Ming Yih} and Masahito Suiko and Yoichi Sakakibara and Yuh-Shyong Yang and Liu, {Ming Cheh}",

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AU - Liu, Tzu An

AU - Yasuda, Shin

AU - Williams, Frederick E.

AU - Liu, Ming Yih

AU - Suiko, Masahito

AU - Sakakibara, Yoichi

AU - Yang, Yuh-Shyong

AU - Liu, Ming Cheh

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AB - A simple methodology for the identification of hemostatic proteins that are subjected to posttranslational tyrosine sulfation was developed. The procedure involves sequence analysis of members of the three hemostatic pathways using the Sulfinator prediction algorithm, followed by [35S]sulfate labeling of cultured HepG2 human hepatoma cells, immunoprecipitation of targeted [35S]sulfate-labeled hemostatic proteins, and tyrosine O-[35S]sulfate analysis of immunoprecipitated proteins. Three new tyrosine-sulfated hemostatic proteins-protein S, prekallikrein, and plasminogen-were identified. Such a target-specific approach will allow investigation of tyrosine-sulfated proteins of other biochemical/physiological pathways/processes and contribute to a better understanding of the functional role of posttranslational tyrosine sulfation.

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A target-specific approach for the identification of tyrosine-sulfated hemostatic proteins

Abstract

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