AI Article Synopsis
- Abnormal glycosylation and phosphorylation are linked to brain aging, with their interactions influencing pathological processes, yet prior studies rarely examined both simultaneously.
- A new tandem HILIC-IMAC method was developed to analyze N-glycosylation and phosphorylation in mouse brains from two different ages, revealing a wealth of data including nearly 11,000 glycopeptides and phosphopeptides.
- Results indicated that aging affected glycoproteins related to cell adhesion and extracellular matrix, while phosphoproteins influenced microtubule dynamics and synaptic transmission, showing opposing expression trends in glycosylation and phosphorylation.
Article Abstract
Abnormal glycosylation and phosphorylation are strongly associated with brain aging. N-glycosylation and phosphorylation are closely involved in pathological processes in a crosstalk dependent manner. However, simultaneous characterization of glycosylation and phosphorylation together in aging brain was uncommon. Herein we developed a novel tandem HILIC-IMAC strategy for simultaneous analysis of N-glycoproteomics and phosphoproteomics. This tandem method showed higher enrichment repeatability, more identifications of glycopeptides and phosphopeptides, and lower overlap. Application of the established method to mouse brain at two ages (8 weeks and 65 weeks) to explore changes in glycosylation and phosphorylation during aging. Up to 10,990 N-glycopeptides and 11,409 phosphopeptides were identified from mouse brain. Among these, differentially expressed phosphoproteins were involved in regulation of microtubule depolymerization, synapse, and transmission of nerve impulse. And glycoproteins differentially expressed with age were mostly related to cell adhesion processes and extracellular matrix. Furthermore, we found the opposite expression trends in glycosylation and phosphorylation during aging on Grin2b. Together, the HILIC-IMAC strategy has potential to discover aging biomarkers and analyze complex biosamples, paving the way for in-depth investigations for the changes of protein glycosylation and phosphorylation in aging brain.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.chroma.2024.465525 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Phosphorylation of N-glycans in the brain: The case for a non-canonical pathway?
BBA Adv
December 2024
Genos Glycoscience Research Laboratory, Zagreb, Croatia.
Asparagine-linked glycosylation (N-glycosylation) is a common co- and post-translational modification that refers to the addition of complex carbohydrates, called N-linked glycans (N-glycans), to asparagine residues within defined sequons of polypeptide acceptors. Some N-glycans can be modified by the addition of phosphate moieties to their monosaccharide residues, thus forming phospho-N-glycans (PNGs). The most prominent such carbohydrate modification is mannose-6-phosphate (M6P) which plays a well-established role in trafficking of acid hydrolases to lysosomes.
View Article and Find Full Text PDFTopical Anti-Inflammatory Effects of Quercetin Glycosides on Atopic Dermatitis-Like Lesions: Influence of the Glycone Type on Efficacy and Skin Absorption.
Inflammation
January 2025
Research Center for Food and Cosmetic Safety and Center for Drug Research and Development, Chang Gung University of Science and Technology, Kweishan, Taoyuan, Taiwan.
Atopic dermatitis (AD) is a multifaceted inflammatory skin condition characterized by the involvement of various cell types, such as keratinocytes, macrophages, neutrophils, and mast cells. Research indicates that flavonoids possess anti-inflammatory properties that may be beneficial in the management of AD. However, the investigation of the glycoside forms for anti-AD therapy is limited.
View Article and Find Full Text PDFInsights on post-translational modifications in fatty liver and fibrosis progression.
Biochim Biophys Acta Mol Basis Dis
January 2025
Ion Channel Biology Laboratory, AU-KBC Research Centre, Madras Institute of Technology Campus, Anna University, Chrompet, Chennai 600 044, Tamil Nadu, India. Electronic address:
Metabolic dysfunction-associated steatotic liver disease [MASLD] is a pervasive multifactorial health burden. Post-translational modifications [PTMs] of amino acid residues in protein domains demonstrate pivotal roles for imparting dynamic alterations in the cellular micro milieu. The crux of identifying novel druggable targets relies on comprehensively studying the etiology of metabolic disorders.
View Article and Find Full Text PDFDiverse perspectives on proteomic posttranslational modifications to address EGFR-TKI resistance in non-small cell lung cancer.
Front Cell Dev Biol
December 2024
Department of International Medical Department, The Second Affiliated Hospital of Dalian Medical University, Dalian, China.
Non-small cell lung cancer (NSCLC) is the main histological subtype of lung cancer. For locally advanced and advanced NSCLC, epidermal growth factor receptor (EGFR) tyrosine kinase inhibitor (TKI)-targeted therapy has been the first choice for NSCLC patients with EGFR mutations. TKIs, as targeted drugs, inhibit kinase activity and autophosphorylation by competitively binding to the ATP binding site of the EGFR tyrosine kinase domain, which blocks the signal transduction mediated by EGFR and thus inhibits the proliferation of tumor cells.
View Article and Find Full Text PDF-GlcNAcylation of Focal Adhesion Kinase Regulates Cell Adhesion, Migration, and Proliferation via the FAK/AKT Pathway.
Biomolecules
December 2024
Division of Regulatory Glycobiology, Graduate School of Pharmaceutical Sciences, Tohoku Medical and Pharmaceutical University, Sendai 980-0845, Miyagi, Japan.
Focal Adhesion Kinase (FAK) is a non-receptor tyrosine kinase pivotal in cellular signal transduction, regulating cell adhesion, migration, growth, and survival. However, the regulatory mechanisms of FAK during tumorigenesis and progression still need to be fully understood. Our previous study demonstrated that -GlcNAcylation regulates integrin-mediated cell adhesion.
View Article and Find Full Text PDFWant 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!