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Proteoglycan desulfation: a critical step in oncogenesis?
1Department of Molecular Reproduction, Development and Genetics, Indian Institute of Science, Bangalore 560012, India, vishalsinghbaghel@gmail.com.
Frontiers in Bioscience (Landmark Edition)
|October 6, 2019
Summary
Arylsulfatases, enzymes that remove sulfate groups, are crucial for proteoglycan function. Their dysregulation is linked to cancer spread, suggesting therapeutic potential.
Area of Science:
- Biochemistry
- Molecular Biology
- Cancer Research
Background:
- Proteoglycans are vital components of cellular microenvironments, influencing cell structure and signaling.
- Proteoglycan function is modulated by sulfation, a process involving sulfotransferases and sulfatases.
- Arylsulfatases are a conserved family of desulfating enzymes, with some acting on proteoglycans.
Purpose of the Study:
- To examine the biochemistry of arylsulfatases.
- To review the role of arylsulfatase activity on proteoglycans in carcinogenesis and carcinomatosis.
- To explore the potential of arylsulfatases as therapeutic targets for cancer.
Main Methods:
- Biochemical analysis of arylsulfatase family enzymes.
- Review of existing literature on arylsulfatases, proteoglycans, and cancer.
- Analysis of the consequences of aberrant arylsulfatase expression in cancer.
Main Results:
- Arylsulfatases are conserved desulfating enzymes, with a subset specifically targeting proteoglycans.
- Aberrant expression of these arylsulfatases is associated with carcinogenesis and carcinomatosis (cancer cell dissemination).
Conclusions:
- Understanding the cellular-molecular roles of arylsulfatases in proteoglycan desulfation is key.
- Arylsulfatases represent a promising avenue for developing novel cancer therapies.
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