The mechanisms of gastric cancer (GC) occurrence and development are still unclear. Although glycosyltransferase 8 domain containing 1 (GLT8D1) has been implicated in GC, its specific role and molecular mechanisms in GC progression need to be further investigated. Tissue microarrays were used to detect the expression levels of GLT8D1 in 80 GC tissues and their corresponding non-tumor adjacent tissues. The correlations between the GLT8D1 expression level and clinicopathological characteristics were evaluated. A series of and functional experiments were performed to explore the role of GLT8D1 in GC progression. Combined with transcriptomic RNA sequencing (RNA-seq) and Weighted Gene Co-expression Network Analysis (WGCNA), we delineated the potential mechanisms via experimental verification. Elevated expression of GLT8D1 in GC tissues was positively correlated with advanced clinical stages and poor prognosis. Konckdown of GLT8D1 significantly inhibited GC cell proliferation and induced apoptosis, whereas overexpression did the opposite. Further researches demonstrated that protein tyrosine phosphatase non-receptor type 6 (PTPN6), a downstream target of GLT8D1, has the capacity to modulate the activity of the JAK2/STAT3 signaling pathway. Our study indicated that GLT8D1 expression was upregulated in GC tissues and correlated with poor prognosis. We reveal a potential molecular mechanism by which GLT8D1 promotes GC progression.
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http://dx.doi.org/10.7150/ijms.102719 | DOI Listing |
Sci Rep
December 2024
Neurogenetics Department, The Cyprus Institute of Neurology and Genetics, Nicosia, Cyprus.
Amyotrophic lateral sclerosis (ALS) is a devastating, uniformly lethal degenerative disease of motor neurons, presenting with relentlessly progressive muscle atrophy and weakness. More than fifty genes carrying causative or disease-modifying variants have been identified since the 1990s, when the first ALS-associated variant in the gene SOD1 was discovered. The most commonly mutated ALS genes in the European populations include the C9orf72, SOD1, TARDBP and FUS.
View Article and Find Full Text PDFInt J Med Sci
December 2024
Department of Gastroenterology, Tongji Hospital, School of Medicine, Tongji University, Shanghai, 200065, China.
Sci Rep
December 2023
Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, 2780-157, Oeiras, Portugal.
Glycosyltransferases (GTs) are enzymes that catalyze the formation of glycosidic bonds and hundreds of GTs have been identified so far in humans. Glycosyltransferase 8 domain-containing protein 1 (GLT8D1) has been associated with central nervous system diseases and cancer. However, evidence on its enzymatic properties, including its substrates, has been scarcely described.
View Article and Find Full Text PDFBMC Med Genomics
June 2023
Lanzhou University Second Hospital, Lanzhou, 730030, P.R. China.
BMC Med Genomics
June 2023
Lanzhou University Second Hospital, Lanzhou, 730030, P.R. China.
Background: Glycosylation involved in various biological function, aberrant glycosylation plays an important role in cancer development and progression. Glycosyltransferase 8 domain containing 1 (GLT8D1) and GLT8D2, as members of the glycosyltransferase family proteins, are associated with transferase activity. However, the association between GLT8D1/2 and gastric cancer (GC) remains unclear.
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