GML

Last update 23 Jan 2025

Basic Info

Synonyms

Glycosyl-phosphatidylinositol-anchored molecule-like protein, glycosylphosphatidylinositol anchored molecule like, GML

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Introduction

May play a role in the apoptotic pathway or cell-cycle regulation induced by p53/TP53 after DNA damage.

100 Clinical Results associated with GML

100 Translational Medicine associated with GML

0 Patents (Medical) associated with GML

396

Literatures (Medical) associated with GML

01 Dec 2024·European Journal of Clinical Investigation

Evolution of CEACAM pathogen decoy receptors in primates

Article

Author: Zimmermann, Wolfgang ; Kammerer, Robert

AbstractBackgroundCEACAM1 in leukocytes controls cell activation during inflammation. This and its expression in epithelial cells led to frequent independent appropriation of CEACAM1 as receptor by pathogens in humans and other species to gain host access and to downregulate its immune response. As a countermeasure, decoy receptors with CEACAM1‐like pathogen‐binding domains evolved. The granulocyte‐specific human CEACAM3 endocytic receptor diverts CEACAM1‐binding pathogens to neutrophils for internalization and destruction. The role of the glycosylphosphatidylinositol‐anchored CEACAM5 and CEACAM6 which can also bind CEACAM1‐targeting pathogens in humans is less clear.MethodsWe analyzed the selection of CEACAMs to avoid pathogen binding and to maintain similarity between pathogen receptors and decoy receptors in 148 primate species.ResultsNotably, functional CEACAM3 genes were not found in gibbons and New World monkeys. Interestingly, CEACAM6 in these primates exhibits similar high ratios of rates of nonsynonymous and synonymous substitution (dN/dS) in their pathogen‐binding N domain exons as found for CEACAM1. High dN/dS ratios are indicative of selection for diversification typically seen in pathogen receptors. Human CEACAM6 is expressed on granulocytes and epithelial cells. Therefore, CEACAM6 could substitute for the missing endocytic receptor CEACAM3. In nearly all investigated primate groups also N exons of the epithelially expressed CEACAM5 exhibit selection for diversification. In African populations, five high‐frequency polymorphisms are observed in the pathogen‐binding region of CEACAM5 (I80V, V83A, I100T, I112V, I113T) with 3‐4 polymorphisms combined in the same individual. These polymorphisms correspond to CEACAM1 pathogen‐binding domain sequences.ConclusionThe glycosylphosphatidylinositol‐anchored CEACAM5 and CEACAM6 are under selection to maintain similarity to the pathogen receptor CEACAM1 in most primate species, indicating a function as decoy receptors.

15 Nov 2024·Chemistry – A European Journal

Deciphering the Cell Surface Sugar‐Coating via Biochemical Pathways

Review

Author: Ghosh, Pritam

AbstractCell surface components, specifically glycans, play a significant role in several biological functions like cell structure, crosstalk between cells, and eventual target recognition of the cells for therapeutics. The dense layer of glycans, i. e., glycocalyx, could differ in taxon, species, and cell type. Glycans are coupled with lipids and proteins to form glycolipids, glycoproteins, proteoglycans, and glycosylphosphatidylinositol‐anchored proteins, making their study challenging. However, understanding glycosylation at the cellular level is vital for fundamental research and advancing glycan‐targeted therapy. Among different pathways, metabolic glycan labelling uses the natural metabolic processes of the cell to introduce abiotic functionality into glycan residues. The Bertozzi group pioneered metabolic oligosaccharide engineering using glycan salvage pathways to convert monosaccharides with unnatural modifications. This eventually results in the probe becoming part of the complex cellular glycan structures via click chemistry using copper. On the other hand, the boronic acid‐based probe can recognise carbohydrates in a single step without any chemical modification of the surface. This review discusses the significance of glycans as biomarkers for different diseases and the necessity to evaluate them in situ within the physiological environment. The review also discusses the prospect of this field and its potential applications.

22 Oct 2024·Bioscience, Biotechnology, and Biochemistry

Glycosylphosphatidylinositol-anchored lipid transfer proteins influence root cap cuticle formation at primary root tips, promoting NaCl tolerance in Arabidopsis seedlings

Article

Author: Uemura, Yuta ; Tsukagoshi, Hironaka ; Sakaoka, Satomi ; Morikami, Atsushi

ABSTRACTRoot cap cuticles (RCCs), comprising mainly very-long-chain fatty acids (VLCFAs), promote salt tolerance by preventing ion influx. Glycosylphosphatidylinositol-anchored lipid transfer protein (LTPG)1 and LTPG2 participate in VLCFA deposition in the extracellular region, aiding RCC formation in the lateral roots. In this study, we investigated whether LTPG1 and LTPG2 have similar functions in the primary roots of young Arabidopsis thaliana. Phenotypic analyses, fluorescence microscopy, and quantitative real-time reverse transcription polymerase chain reaction confirmed that NaCl exposure induced LTPG1 and LTPG2 expression and promoted RCC formation in young primary roots. The loss of RCC in the ltpg1 and ltpg2 mutants resulted in increased NaCl sensitivity of root elongation. NaCl also upregulated the expression of several NaCl-responsive genes in ltpg1 and ltpg2. We conclude that RCC formation via LTPG function is pivotal in enhancing salt tolerance in young primary roots.

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