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Roles of Sulfatases and Sulfotransferases in Fundamental Biological Processes

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (30 June 2022) | Viewed by 1872

Special Issue Editor


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Guest Editor
Jesse Brown VA Medical Center, University of Illinois at Chicago, Chicago, IL 60612, USA
Interests: role of sulfatases and sulfotransferases in human diseases
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Special Issue Information

Dear Colleagues,

Identification of the roles of sulfatases, sulfotransferase enzymes, and sulfated glycosaminoglycans (GAGs) in signaling, transcription, and cell differentiation has focused on the mechanisms of action in well-defined biological systems. Together, sulfatases, sulfotransferases, and sulfated GAGs confer remarkable specificity in the regulation of vital processes in plants, microbiota, and macrobiota. By post-translational modifications of carbohydrates, including glycosaminoglycans, lipids, proteins, and steroids, sulfation influences interactions within and between cells and in response to the extracellular environment. Thus, changes in sulfation impact subsequent phosphorylations and other post-translational events. The specific, chemically precise recognition signals attributable to localized sulfates can influence vital cell processes in immunity and host cell responses to infection, as well as in activation/inactivation of steroid hormones, coagulation, drug metabolism, and cell signaling. The complex biochemistry required for the removal or addition of sulfate residues reflects the importance of molecular recognition and the potential harm of molecular mimicry, such as by the food additive carrageenan, to disrupt homeostatic mechanisms. The articles in this issue on this topic will reveal the range of effects of sulfation, outline what is known about the underlying molecular and biochemical pathways, and suggest avenues for future investigations.

Dr. Joanne Tobacman

Guest Editor

Dr. Joanne Tobacman
Guest Editor

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Keywords

  • Sulfatase
  • Sulfotransferase
  • Heparin
  • Chondroitin Sulfate
  • Sulfated Glycosaminoglycans (GAGs)
  • Sulfation

Published Papers (1 paper)

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Review

35 pages, 24534 KiB  
Review
Profound Impact of Decline in N-Acetylgalactosamine-4-Sulfatase (Arylsulfatase B) on Molecular Pathophysiology and Human Diseases
by Joanne K. Tobacman and Sumit Bhattacharyya
Int. J. Mol. Sci. 2022, 23(21), 13146; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms232113146 - 29 Oct 2022
Cited by 7 | Viewed by 1596
Abstract
The enzyme N-acetylgalactosamine-4-sulfatase (Arylsulfatase B; ARSB) was originally identified as a lysosomal enzyme which was deficient in Mucopolysaccharidosis VI (MPS VI; Maroteaux-Lamy Syndrome). The newly directed attention to the impact of ARSB in human pathobiology indicates a broader, more pervasive effect, encompassing roles [...] Read more.
The enzyme N-acetylgalactosamine-4-sulfatase (Arylsulfatase B; ARSB) was originally identified as a lysosomal enzyme which was deficient in Mucopolysaccharidosis VI (MPS VI; Maroteaux-Lamy Syndrome). The newly directed attention to the impact of ARSB in human pathobiology indicates a broader, more pervasive effect, encompassing roles as a tumor suppressor, transcriptional mediator, redox switch, and regulator of intracellular and extracellular-cell signaling. By controlling the degradation of chondroitin 4-sulfate and dermatan sulfate by removal or failure to remove the 4-sulfate residue at the non-reducing end of the sulfated glycosaminoglycan chain, ARSB modifies the binding or release of critical molecules into the cell milieu. These molecules, such as galectin-3 and SHP-2, in turn, influence crucial cellular processes and events which determine cell fate. Identification of ARSB at the cell membrane and in the nucleus expands perception of the potential impact of decline in ARSB activity. The regulation of availability of sulfate from chondroitin 4-sulfate and dermatan sulfate may also affect sulfate assimilation and production of vital molecules, including glutathione and cysteine. Increased attention to ARSB in mammalian cells may help to integrate and deepen our understanding of diverse biological phenomenon and to approach human diseases with new insights. Full article
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