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Molecular Biology of Sulfatase

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

Deadline for manuscript submissions: 20 May 2025 | Viewed by 1813

Special Issue Editor


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Guest Editor
Jesse Brown VA Medical Center, University of Illinois at Chicago, Chicago, IL 60612, USA
Interests: glycosaminoglycan sulfatases; sulfotransferases; steroid and other sulfatases; metabolic pathways affected by sulfation; impact of changes in sulfation in disease
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Special Issue Information

Dear Colleagues,

The impact of sulfation on biological processes has been of interest for decades, particularly with regard to the inherited deficiency of sulfatases in the mucopolysaccharidoses; these include MPS VI (Maroteaux-Lamy Syndrome), in which there is a deficiency of N-acetylgalactosamine-4-sulfatase, and MPS IVA, in which there is a deficiency of N-acetylgalactosamine-6-sulfatase (Morquio Syndrome). Recently, attention has been directed to the molecular consequences of an acquired decline in sulfatase activity due to changes in the cellular microenvironment. Identification of the roles of sulfatases and sulfotransferase enzymes in signaling, transcription, and cell differentiation has focused on the mechanisms of action of specific enzymes in well-defined biological systems. Together, sulfatases and sulfotransferase confer remarkable specificity in the regulation of vital processes in plants, microbiota, and macrobiota. Via the post-translational modification of carbohydrates, including glycosaminoglycans, lipids, proteins, and steroids, sulfation confers precise interactions within and between cells and in response to the extracellular environment. In this collection of articles, the range of effects of sulfation and of sulfatase and sulfotransferase activity on pathobiology will be examined. This increased focus on the role of sulfation in signalling and the regulation of vital cell functions, including proliferation, differentiation, and transcription, may provide novel insights into basic metabolic and molecular pathways and offer new targets able to improve human health.

Dr. Joanne Tobacman
Guest Editor

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Keywords

  • chondroitin sulfatases
  • sulfotransferases
  • steroid, tyrosine, and other sulfatases
  • metabolic pathways affected by sulfation
  • impact of changes in sulfation on disease

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Published Papers (1 paper)

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Research

17 pages, 2991 KiB  
Article
N-Acetylgalactosamine-4-sulfatase (Arylsulfatase B) Regulates PD-L1 Expression in Melanoma by an HDAC3-Mediated Epigenetic Mechanism
by Sumit Bhattacharyya, InSug O-Sullivan and Joanne K. Tobacman
Int. J. Mol. Sci. 2024, 25(11), 5851; https://doi.org/10.3390/ijms25115851 - 28 May 2024
Viewed by 1366
Abstract
The effects of the enzyme N-acetylgalactosamine-4-sulfatase (Arylsulfatase B, ARSB), which removes the 4-sulfate group at the non-reducing end of chondroitin 4-sulfate, on the expression of PD-L1 were determined, and the underlying mechanism of PD-L1 expression was elucidated. Initial experiments in human melanoma cells [...] Read more.
The effects of the enzyme N-acetylgalactosamine-4-sulfatase (Arylsulfatase B, ARSB), which removes the 4-sulfate group at the non-reducing end of chondroitin 4-sulfate, on the expression of PD-L1 were determined, and the underlying mechanism of PD-L1 expression was elucidated. Initial experiments in human melanoma cells (A375) showed that PD-L1 expression increased from 357 ± 31 to 796 ± 50 pg/mg protein (p < 10−11) when ARSB was silenced in A375 cells. In subcutaneous B16F10 murine melanomas, PD-L1 declined from 1227 ± 189 to 583 ± 110 pg/mg protein (p = 1.67 × 10−7), a decline of 52%, following treatment with exogenous, bioactive recombinant ARSB. This decline occurred in association with reduced tumor growth and prolongation of survival, as previously reported. The mechanism of regulation of PD-L1 expression by ARSB is attributed to ARSB-mediated alteration in chondroitin 4-sulfation, leading to changes in free galectin-3, c-Jun nuclear localization, HDAC3 expression, and effects of acetyl-H3 on the PD-L1 promoter. These findings indicate that changes in ARSB contribute to the expression of PD-L1 in melanoma and can thereby affect the immune checkpoint response. Exogenous ARSB acted on melanoma cells and normal melanocytes through the IGF2 receptor. The decline in PD-L1 expression by exogenous ARSB may contribute to the impact of ARSB on melanoma progression. Full article
(This article belongs to the Special Issue Molecular Biology of Sulfatase)
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