Sulfonation, an underexploited area: from skeletal development to infectious diseases and cancer.
Sulfonation is one of the most abundant cellular reactions modifying a wide range of xenobiotics as well as endogenous molecules which regulate important biological processes including blood clotting, formation of connective tissues, and functionality of secreted proteins, hormones, and signaling molecules. Sulfonation is ubiquitous in all tissues and widespread in nature (plants, animals, and microorganisms). Although sulfoconjugates were discovered over a century ago when, in 1875, Baumann isolated phenyl sulfate in the urine of a patient given phenol as an antiseptic, the significance of sulfonation and its roles in human diseases have been underappreciated until recent years. Here, we provide a current overview of the significance of sulfonation reactions in a variety of biological functions and medical conditions (with emphasis on cancer). We also discuss research areas that warrant further attention if we are to fully understand how deficiencies in sulfonation could impact human health which, in turn, could help define treatments to effect improvements in health.
Experimental Therapeutics, BC Cancer Research Centre, Vancouver, BC, Canada.|Department of Pathology and Laboratory Medicine, University of British Columbia, Vancouver, BC, Canada.
Ada W. Y.
AW
Leung
Experimental Therapeutics, BC Cancer Research Centre, Vancouver, BC, Canada.
Ian
I
Backstrom
Experimental Therapeutics, BC Cancer Research Centre, Vancouver, BC, Canada.|Department of Pathology and Laboratory Medicine, University of British Columbia, Vancouver, BC, Canada.|Faculty of Pharmaceutical Sciences, University of British Columbia, Vancouver, BC, Canada.|Centre for Drug Research and Development, Vancouver, BC, Canada.
Marcel B
MB
Bally
D000818:Animals; D001846:Bone Development; D002467:Cell Nucleus / Q000378:metabolism; D003141:Communicable Diseases / Q000209:etiology*; D006801:Humans; D009097:Multienzyme Complexes / Q000502:physiology*; D009369:Neoplasms / Q000209:etiology*; D011499:Protein Processing, Post-Translational; D013430:Sulfate Adenylyltransferase / Q000502:physiology*; D014443:Tyrosine / Q000378:metabolism; D015262:Xenobiotics / Q000378:metabolism
D009097:Multienzyme Complexes; D015262:Xenobiotics; D014443:Tyrosine; C022322:PAPS synthetase; D013430:Sulfate Adenylyltransferase
PAPSS; heparan sulfate; sulfonation; sulfotransferases; tyrosine sulfation