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Protein paucimannosylation is a novel N-glycosylation signature of human cancers

ABSTRACT: This is the first study to systematically investigate and document an association between protein paucimannosylation, a recently identified human N-glycosylation type, and human cancers. The study provides evidence of an over-representation of paucimannosylation in diverse cancer types, and further points to a stage-specific expression, catalytic involvement of ?-hexosaminidase and cancer cell surface expression of paucimannosidic proteins. Our findings expand our knowledge of the glyco-phenotypes underpinning human cancer, and, at the same time, open many enticing questions concerning the biogenesis, protein carrier(s), subcellular localisation(s) and function(s) of paucimannosylation in the heterogeneous tumour micro-environment. Thus, this work contributes to the fundamental knowledge required to improve the diagnosis, treatment, and, eventually, prevention of human cancers.

INSTRUMENT(S): Agilent 1260, Velos Plus

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Dr. Morten Thaysen-Andersen

PROVIDER: MSV000083727 | MassIVE | Thu Apr 25 19:00:00 BST 2019

REPOSITORIES: MassIVE

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Project description:Dysregulation of glyco-gene expression in cancer can lead to aberrant glycans and glycoconjugates, which in turn can promote tumorigenesis. Cervical cancer display augmentation of aberrant sialylated glycans and increase of glyco-genes, which encoded enzymes participate in the sialylation pathways. Besides sialiltranferases, other glyco-genes, analyzed individually are reported as altered in cervical cancer. Here we show a comprehensive analysis of glyco-gene expression in cervical cancer to obtain a wide scenery of global changes in glycosylation pathways. First, we compared glyco-gene expression between normal tissue and cervical cancer. Second, we analyzed the glycogene expression in subtypes of cc to obtain hallmarks of glyco-gene expression in each case. Our results indicate that in cervical cancer the GPI-anchored biosynthesis is increased in cc while the synthesis of chondroitin and dermatan sulfate are decreased. Moreover, data show that adenocarcinoma displayed a homogenous glyco-gene expression pattern, where chondroitin /dermatan sulfate and heparan sulfate glycogenes are decreased, while keratan sulfate genes are increased. Dysregulation of glyco-gene expression in cancer can lead to aberrant glycans and glycoconjugates, which in turn can promote tumorigenesis. Cervical cancer display augmentation of aberrant sialylated glycans and increase of glyco-genes, which encoded enzymes participate in the sialylation pathways. Besides sialiltranferases, other glyco-genes, analyzed individually are reported as altered in cervical cancer. Here we show a comprehensive analysis of glyco-gene expression in cervical cancer to obtain a wide scenery of global changes in glycosylation pathways. First, we compared glyco-gene expression between normal tissue and cervical cancer. Second, we analyzed the glycogene expression in subtypes of cc to obtain hallmarks of glyco-gene expression in each case. Our results indicate that in cervical cancer the GPI-anchored biosynthesis is increased in cc while the synthesis of chondroitin and dermatan sulfate are decreased. Moreover, data show that adenocarcinoma displayed a homogenous glyco-gene expression pattern, where chondroitin /dermatan sulfate and heparan sulfate glycogenes are decreased, while keratan sulfate genes are increased.

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Protein paucimannosylation is a novel N-glycosylation signature of human cancers

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