Insights into miRNA regulation of the human glycome

Brian T. Kasper, Sujeethraj Koppolu, Lara Mahal

Research output: Contribution to journalArticle

Abstract

Glycosylation is an intricate process requiring the coordinated action of multiple proteins, including glycosyltransferases, glycosidases, sugar nucleotide transporters and trafficking proteins. Work by several groups points to a role for microRNA (miRNA) in controlling the levels of specific glycosyltransferases involved in cancer, neural migration and osteoblast formation. Recent work in our laboratory suggests that miRNA are a principal regulator of the glycome, translating genomic information into the glycocode through tuning of enzyme levels. Herein we overlay predicted miRNA regulation of glycosylation related genes (glycogenes) onto maps of the common N-linked and O-linked glycan biosynthetic pathways to identify key regulatory nodes of the glycome. Our analysis provides insights into glycan regulation and suggests that at the regulatory level, glycogenes are non-redundant.

Original languageEnglish (US)
Pages (from-to)774-779
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume445
Issue number4
DOIs
StatePublished - Mar 21 2014

Fingerprint

Glycosylation
MicroRNAs
Glycosyltransferases
Polysaccharides
Point groups
Glycoside Hydrolases
Biosynthetic Pathways
Osteoblasts
Protein Transport
Sugars
Proteins
Nucleotides
Tuning
Genes
Enzymes
Neoplasms

Keywords

  • Carbohydrate pathways
  • Glycan biosynthesis
  • Glycan regulation
  • Glycogenes
  • Glycosylation
  • MicroRNA
  • miRNA

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

Insights into miRNA regulation of the human glycome. / Kasper, Brian T.; Koppolu, Sujeethraj; Mahal, Lara.

In: Biochemical and Biophysical Research Communications, Vol. 445, No. 4, 21.03.2014, p. 774-779.

Research output: Contribution to journalArticle

Kasper, Brian T. ; Koppolu, Sujeethraj ; Mahal, Lara. / Insights into miRNA regulation of the human glycome. In: Biochemical and Biophysical Research Communications. 2014 ; Vol. 445, No. 4. pp. 774-779.
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