Abstract
Tyrosine (Tyr) sulfation is a common posttranslational modification of secreted proteins or membrane-bound proteins that is implicated in numerous physiological and pathological processes. The Tyr sulfation modifies proteinprotein interactions involved in leukocyte adhesion, homeostasis, and receptor-mediated signaling. To data, 80 Tyrsulfated proteins have been identified. As new methodologies and bioinformatics for the detection of Tyr sulfation become available, the number of Tyr-sulfated acceptor proteins discovered is bound to increase. Further, recent advances in microscopy and fluorescence technology will provide information on the true spatial and temporal nature of Tyr-sulfated proteins within the intact cell. This review summarizes the methods for the detection of Tyr O-sulfation as well as the biological functions of sulfated Tyr. Further, illustrative examples of the impact of Tyr sulfation on the pharmacological properties are presented.
Keywords: Tyrosine sulfation, tyrosine O-sulfation, tyrosylprotein sulfotransferase, TPST, posttranslational modification, membrane-bound proteins, numerous physiological, pathological processes, leukocyte adhesion, bioinformatics, homeostasis, fluorescence technology, intact cell, true spatial
Current Pharmaceutical Biotechnology
Title:Current Status and Future Prospects for Research on Tyrosine Sulfation
Volume: 13 Issue: 14
Author(s): Nobuya Sasaki
Affiliation:
Keywords: Tyrosine sulfation, tyrosine O-sulfation, tyrosylprotein sulfotransferase, TPST, posttranslational modification, membrane-bound proteins, numerous physiological, pathological processes, leukocyte adhesion, bioinformatics, homeostasis, fluorescence technology, intact cell, true spatial
Abstract: Tyrosine (Tyr) sulfation is a common posttranslational modification of secreted proteins or membrane-bound proteins that is implicated in numerous physiological and pathological processes. The Tyr sulfation modifies proteinprotein interactions involved in leukocyte adhesion, homeostasis, and receptor-mediated signaling. To data, 80 Tyrsulfated proteins have been identified. As new methodologies and bioinformatics for the detection of Tyr sulfation become available, the number of Tyr-sulfated acceptor proteins discovered is bound to increase. Further, recent advances in microscopy and fluorescence technology will provide information on the true spatial and temporal nature of Tyr-sulfated proteins within the intact cell. This review summarizes the methods for the detection of Tyr O-sulfation as well as the biological functions of sulfated Tyr. Further, illustrative examples of the impact of Tyr sulfation on the pharmacological properties are presented.
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Cite this article as:
Sasaki Nobuya, Current Status and Future Prospects for Research on Tyrosine Sulfation, Current Pharmaceutical Biotechnology 2012; 13 (14) . https://dx.doi.org/10.2174/138920101314151120122922
DOI https://dx.doi.org/10.2174/138920101314151120122922 |
Print ISSN 1389-2010 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4316 |
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