Biology subjects

Toonstra, C.

Publications and source records attributed to Toonstra, C..

2 recordsLinked to original sources

bioRxiv2019

Expression of endoplasmic reticulum mannosyl-oligosaccharide α1, 2-mannosidase regulates tumorigenicity of prostate cancer cells

It has been previously demonstrated that glycogenes can function as important pleiotropic regulators of tumorigenesis. In this study, we investigated the function of endoplasmic reticulum mannosyl-oligosaccharide 1, 2-alpha-mannosidase (MAN1B1) on the behavior of prostate cancer cells and found that overexpression of MAN1B1 in androgen-independent PC3 cells reduced cellular migration. We extended the analysis to an androgen dependent cell line, LNCaP, and another androgen independent cell line, LNCaP-AI, observing a similar migratory phenotype. By using quantitative proteomics, we found the downregulation of vimentin expression when PC3 or LNCaP-AI cells with overexpressed MAN1B1. The current study suggests that MAN1B1 may regulate cellular migration and promote epithelial-to-mesenchymal transition (EMT) phenotype in prostate cancer cells.

cancer biology↗

bioRxiv2018

Deciphering the roles of N-glycans on collagen-platelet interactions

Collagen is a potent agonist for platelet activation, presenting itself as a key contributor to coagulation via interactions with platelet glycoproteins. The fine-details dictating platelet-collagen interactions are poorly understood. In particular, glycosylation could be a key determinant in the platelet-collagen interaction. Here we report an affinity purification coupled to mass spectrometry-based approach to elucidate the function of N-glycans in dictating platelet-collagen interactions. By integrative proteomic and glycoproteomic analysis of collagen-platelet interactive proteins with N-glycan manipulation, we demonstrate that the interaction of platelet adhesive receptors with collagen are highly N-glycan regulated, with glycans on many receptors playing positive roles on collagen binding, with glycans on other platelet glycoproteins exhibiting inhibitory roles on the binding to collagen. Our results significantly enhance our understanding of the details of glycans influencing the platelet-collagen interaction.

biochemistry↗