Mucin-type O-glycosylation is one of the most common posttranslational modifications of proteins. The abnormal expression of various polypeptide GalNAc-transferases (GalNAc-Ts) which initiate and define sites of O-glycosylation are linked to many cancers and other diseases. Current O-glycosyation prediction programs utilize O-glycoproteomics data obtained without regard to the transferase isoform (s) responsible for the glycosylation. With 20 different GalNAc-Ts in humans, having an ability to predict and interpret O-glycosylation sites in terms of specific GalNAc-T isoforms is invaluable. To fill this gap, ISOGlyP (Isoform-Specific O-Glycosylation Prediction) has been developed. Using position-specific enhancement values generated based on GalNAc-T isoform-specific amino acid preferences, ISOGlyP predicts the propensity that a site would be glycosylated by a specific transferase. ISOGlyP gave an overall prediction accuracy of 70% against in vivo data, which is comparable to that of the NetOGlyc4.0 predictor. Additionally, ISOGlyP can identify the known effects of long- and short-range prior glycosylation and can generate potential peptide sequences selectively glycosylated by specific isoforms. ISOGlyP is freely available for use at ISOGlyP.utep.edu. The code is also available on GitHub (https://github.com/jonmohl/ISOGlyP).
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8022967 | PMC |
| http://dx.doi.org/10.1093/glycob/cwaa067 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Decoding Extracellular Protein Glycosylation in Human Health and Disease.
Annu Rev Anal Chem (Palo Alto Calif)
January 2025
Department of Chemistry, Yale University, New Haven, Connecticut, USA;
Protein glycosylation, the covalent attachment of carbohydrate, or glycan, structures onto the protein backbone, is one of the most complex and heterogeneous post-translational modifications (PTMs). Extracellular protein glycosylation, in particular N- and mucin-type O-glycosylation, plays pivotal roles in a number of biophysical and biochemical processes, such as protein folding and stability, cell adhesion, signaling, and protection. As such, aberrant glycosylation is implicated in a variety of diseases, including cancer.
View Article and Find Full Text PDFGALNT6 drives lenvatinib resistance in hepatocellular carcinoma through autophagy and cancer-associated fibroblast activation.
Cell Oncol (Dordr)
December 2024
Liver Cancer Institute, Zhongshan Hospital, Fudan University, Shanghai, 200032, China.
Background: Hepatocellular carcinoma (HCC) remains a significant global health challenge with limited treatment options. Lenvatinib, a tyrosine kinase inhibitor, has shown promise but is often undermined by the development of drug resistance.
Methods: Utilizing high-throughput sequencing, we investigated the molecular mechanisms underlying lenvatinib resistance in HCC cells, with a focus on metabolic pathways.
Golgi pH elevation due to loss of V-ATPase subunit V0a2 function correlates with tissue-specific glycosylation changes and globozoospermia.
Cell Mol Life Sci
December 2024
Institute of Human Genetics, University Medical Center Göttingen, 37073, Göttingen, Germany.
Loss-of-function variants in ATP6V0A2, encoding the trans Golgi V-ATPase subunit V0a2, cause wrinkly skin syndrome (WSS), a connective tissue disorder with glycosylation defects and aberrant cortical neuron migration. We used knock-out (Atp6v0a2) and knock-in (Atp6v0a2) mice harboring the R755Q missense mutation selectively abolishing V0a2-mediated proton transport to investigate the WSS pathomechanism. Homozygous mutants from both strains displayed a reduction of growth, dermis thickness, and elastic fiber formation compatible with WSS.
View Article and Find Full Text PDFLeucine zipper-based SAIM imaging identifies therapeutic agents to disrupt the cancer cell glycocalyx for enhanced immunotherapy.
bioRxiv
December 2024
Graduate Field of Biophysics, Cornell University, Ithaca, NY, USA.
The abnormally thick glycocalyx of cancer cells can provide a physical barrier to immune cell recognition and effective immunotherapy. Here, we demonstrate an optical method based on Scanning Angle Interference Microscopy (SAIM) for the screening of therapeutic agents that can disrupt the glycocalyx layer as a strategy to improve anti-cancer immune responses. We developed a new membrane labeling strategy utilizing leucine zipper pairs to fluorescently mark the glycocalyx layer boundary for precise and robust measurement of glycocalyx thickness with SAIM.
View Article and Find Full Text PDFTargeting Tn Antigen Suppresses Aberrant O-Glycosylation-Elicited Metastasis in Breast Cancer.
J Cell Mol Med
December 2024
Department of Gynecology and Obstetrics, Beijing Chao-Yang Hospital, Capital Medical University, Beijing, China.
Article Synopsis
- - The study investigates the Tn antigen, an abnormal sugar molecule often found in breast cancer, and its relationship to cancer spread (metastasis) and patient outcomes.
- - Researchers discovered that Tn antigen is commonly present in breast cancer tissues, especially in metastatic areas, and its expression is linked to more advanced disease and lower survival rates.
- - Targeting the Tn antigen in breast cancer cells showed promise in reducing their ability to invade and spread, suggesting it could be an effective therapeutic target for treating aggressive breast cancer.
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!