Glycosylation Regulation by TMEM230 in Aging and Autoimmunity DOI Open Access
Eleonora Piscitelli, Edoardo Abeni,

Cristiana Balbino

и другие.

International Journal of Molecular Sciences, Год журнала: 2025, Номер 26(6), С. 2412 - 2412

Опубликована: Март 7, 2025

Aging is often a choice between developing cancer or autoimmune disorders, due in part to loss of self-tolerance immunological recognition rogue-acting tumor cells. Self-tolerance and cell by the immune system are processes very much dependent on specific signatures glycans glycosylated factors present plasma membrane stromal components tissue. Glycosylated generated nearly innumerable variations nature, allowing for immensely diverse role these aging flexibility necessary cellular interactions tissue functionality. In previous studies, we showed that differential expression TMEM230, an endoplasmic reticulum (ER) protein was associated with enzymes regulating glycan synthesis processing glycosylation rheumatoid arthritis synovial using single-cell transcript sequencing. this current study, characterize genes pathways co-modulated all types processing, as well glycosylation. Genes biological molecular hallmarks were mitochondria-dependent oxidative phosphorylation reactive oxygen species synthesis, ER-dependent stress unfolded response, DNA repair (UV response P53 signaling pathways), senescence, glycolysis apoptosis regulation through PI3K-AKT-mTOR have been shown play important roles neurodegeneration (such Parkinson’s Alzheimer’s disease). We propose downregulation TMEM230 RNASET2 may represent paradigm study age-dependent disorders their glycosylation, signaling.

Язык: Английский

Role of TMEM230 in the Aberrant Glycosylation in Human Autoimmunity and Cancer DOI Creative Commons
Elena Angeli, Cinzia Cocola, Edoardo Abeni

и другие.

Proteoglycan Research, Год журнала: 2025, Номер 3(1)

Опубликована: Янв. 1, 2025

ABSTRACT Alterations in glycoconjugate profiles are thought to promote changes cell‐to‐cell and cell‐to‐intracellular extracellular scaffold interactions human disease. The nearly unlimited number of “glycoforms” that may exist nature difficult study due glycosylation modifications being associated with non‐genome coded posttranscription post‐translation processes. Specific products generated by dependent on concentration sub‐cellular locations glycan synthesis processing enzymes. An indirect “high‐throughput” approach is characterize enzymes (hydrolases transferases) single cell sequencing all types tissue diseases. We previously identified TMEM230 as an endoplasmic reticulum (ER) protein regulates NOTCH glycoprotein receptor ligand signaling zebrafish blood vessel formation destructive remodeling capacities diverse including fibroblast, phagocytic immune system cells patients cancer or granulomatous systemic vasculitis autoimmune disorder. represents a paradigm mediated signal transduction supports the role modifications. ER initiates earliest steps synthesis, sorting, trafficking. As remodeling, Notch hallmarks disorders, we investigated whether aberrant expression was also rheumatoid arthritis (RA). In this current study, analysis supported downregulated synovial RA while were predominantly upregulated. contrast, upregulated high‐grade compared low‐grade gliomas it N‐linked (GlcNAc), glycosaminoglycan expression. Our collective results support glycan/glycoconjugate aggressive gliomas. therefore be therapeutic target marker for clinical treatment induced autoimmunity disorders cancer.

Язык: Английский

Процитировано

1
Glycosylation Regulation by TMEM230 in Aging and Autoimmunity DOI Open Access
Eleonora Piscitelli, Edoardo Abeni,

Cristiana Balbino

и другие.

International Journal of Molecular Sciences, Год журнала: 2025, Номер 26(6), С. 2412 - 2412

Опубликована: Март 7, 2025

Aging is often a choice between developing cancer or autoimmune disorders, due in part to loss of self-tolerance immunological recognition rogue-acting tumor cells. Self-tolerance and cell by the immune system are processes very much dependent on specific signatures glycans glycosylated factors present plasma membrane stromal components tissue. Glycosylated generated nearly innumerable variations nature, allowing for immensely diverse role these aging flexibility necessary cellular interactions tissue functionality. In previous studies, we showed that differential expression TMEM230, an endoplasmic reticulum (ER) protein was associated with enzymes regulating glycan synthesis processing glycosylation rheumatoid arthritis synovial using single-cell transcript sequencing. this current study, characterize genes pathways co-modulated all types processing, as well glycosylation. Genes biological molecular hallmarks were mitochondria-dependent oxidative phosphorylation reactive oxygen species synthesis, ER-dependent stress unfolded response, DNA repair (UV response P53 signaling pathways), senescence, glycolysis apoptosis regulation through PI3K-AKT-mTOR have been shown play important roles neurodegeneration (such Parkinson’s Alzheimer’s disease). We propose downregulation TMEM230 RNASET2 may represent paradigm study age-dependent disorders their glycosylation, signaling.

Язык: Английский

Процитировано

0