Reduced expression of TANGO in colon and hepatocellular carcinomas

Arndt, Stephanie; Boßerhoff, Anja

doi:10.3892/or.18.4.885

Cited by 23 publications

(31 citation statements)

References 19 publications

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“…MIA3, also referred to as ARNT or TANGO, belongs to the melanoma inhibitory activity gene family and may have a role in tumor suppression. 24,25 As with the case of rs1333049, the classic risk factors appear not to be related to the increased MI risks associated with rs17465637.…”

Section: Discussionmentioning

confidence: 99%

Validation of the Association of Genetic Variants on Chromosome 9p21 and 1q41 With Myocardial Infarction in a Japanese Population

Hiura¹,

Fukushima²,

Yuno³

et al. 2008

Circ J

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Section: Discussionmentioning

confidence: 99%

Validation of the Association of Genetic Variants on Chromosome 9p21 and 1q41 With Myocardial Infarction in a Japanese Population

Hiura¹,

Fukushima²,

Yuno³

et al. 2008

Circ J

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“…SNP rs17465637 on chromosome 1q41 is located in the MIA3 gene, which encodes melanoma inhibitor protein 3 required for export of collagen VII (COL7A1) from the endoplasmic reticulum (Saito et al, 2009), and appears to be a tumor suppressor of malignant melanoma (Arndt & Bosserhoff, 2007). MIA3 may be involved in facilitating the migration of monocytic cells through fibrinogene or human microvascular endothelial cells (Arndt et al, 2007), which may increase the risk of plaque formation.…”

Section: Discussionmentioning

confidence: 99%

Association of SNP rs17465637 on Chromosome 1q41 and rs599839 on 1p13.3 with Myocardial Infarction in an American Caucasian Population

Wang

Zhou

et al. 2011

Annals of Human Genetics

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SummaryRecent genome-wide single nucleotide polymorphism (SNP) association studies (GWAS) have identified a number of SNPs that were significantly associated with coronary artery disease and myocardial infarction (MI). However, many independent replication studies in other populations are needed to unequivocally confirm the GWAS association. To assess GWAS association, we have established a case-control cohort consisting of 1231 well-characterised MI patients and 560 controls without detectable coronary stenosis, all selected from the Cleveland Genebank population. The Genebank cohort has sufficient power to detect the association between MI and four GWAS SNPs, including rs17465637 within the MIA3 gene, rs2943634 (intergenic), rs6922269 in MTHFD1L, and rs599839 near SORT1. SNPs were genotyped by TaqMan assays and follow-up multivariate logistic regression analysis with incorporation of significant covariates showed significant association with MI for MIA3 SNP rs17465637 (P-adj = 0.0034) and SORT1 SNP rs599839 (P-adj = 0.009). The minor allele G of rs599839 was also associated with a decreased LDL-C level of 5-9 mg/dL per allele, but not with HDL-C or triglyceride levels. No association for MI or lipid levels was found for SNPs rs2943634 and rs6922269 (P-adj > 0.05). Our results establish two SNPs, rs17465637 in MIA3 and rs599839 near SORT1 as significant risk factors for MI in the American Genebank Caucasian population.

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“…Additionally, these studies also identified O-glycans on mammalian Tango1/Mia3 (26,27), suggesting that O-glycans may perform similar protective functions to control secretion in mammalian systems. Indeed, alterations in both Tango1/Mia3 and O-glycosylation have been associated with diseases of the mammalian gastrointestinal tract (5,6,28,29), which are typically characterized by loss of secretion, loss of mucous membrane formation, and increased diffusion barrier permeability. Interestingly, PGANT4 is most similar to the mammalian ppGalNAc-T10 (8), which is abundantly expressed in the digestive system (30).…”

Section: Resultsmentioning

confidence: 99%

O-Glycosylation regulates polarized secretion by modulating Tango1 stability

Zhang

Syed

Härd

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Polarized secretion is crucial in many tissues. The conserved protein modification, O-glycosylation, plays a role in regulating secretion. However, the mechanisms by which this occurs are unknown. Here, we demonstrate that an O-glycosyltransferase functions as a novel regulator of secretion and secretory vesicle formation in vivo by glycosylating the essential Golgi/endoplasmic reticulum protein, Tango1 (Transport and Golgi organization 1), and conferring protection from furin-mediated proteolysis. Loss of the O-glycosyltransferase PGANT4 resulted in Tango1 cleavage, loss of secretory granules, and disrupted apical secretion. The secretory defects seen upon loss of pgant4 could be rescued either by overexpression of Tango1 or by knockdown of a specific furin (Dfur2) in vivo. Our studies elucidate a novel regulatory mechanism whereby secretion is influenced by the yin/yang of O-glycosylation and proteolytic cleavage. Moreover, our data have broader implications for the potential treatment of diseases resulting from the loss of O-glycosylation by modulating the activity of specific proteases.R egulation of secretory vesicle formation and polarized secretion in vivo is crucial to ensure the proper deposition of signaling molecules, morphogens, and matrix components that mediate growth and differentiation. Polarized secretion is also required in many differentiated tissues, such as the digestive tract, where secreted components along the apical surface form the mucous membrane that confers protection from mechanical and microbial insults (1) and provides immunoregulatory signals (2). Indeed, disruptions in the secreted mucous membrane are associated with diseases of the digestive tract, such as colitis and colon cancer (3-6).Recent studies aimed at identifying the factors that influence secretion have elucidated novel proteins that function in unique aspects of secretion, including the enzymes responsible for the addition of sugars to mucins and other proteins (mucin-type O-glycosylation) (7). O-glycosylation is an essential, evolutionarily conserved protein modification (8, 9) that has direct medical relevance, as aberrations are responsible for the human diseases familial tumoral calcinosis (10, 11) and Tn syndrome (12). Loss of this protein modification affected constitutive secretion and Golgi apparatus structure in Drosophila cell culture (7, 13) and secretion in the developing respiratory system in vivo (14). Additionally, loss of O-glycosylation also disrupted secretion of an extracellular matrix protein (Tiggrin) in the developing wing, resulting in aberrant basement membrane formation and disrupted integrin-mediated cell adhesion (15). Mammalian studies have confirmed the effects of O-glycosylation on secretion, as loss of a glycosyltransferase (ppGalNAcT-1) disrupted secretion of laminin and collagen during mammalian organogenesis, altering the composition of the basement membrane and disrupting proper FGF signaling and organ growth (16). Although these studies all point to a role for O-glycosylation in se...

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Reduced expression of TANGO in colon and hepatocellular carcinomas

Cited by 23 publications

References 19 publications

Validation of the Association of Genetic Variants on Chromosome 9p21 and 1q41 With Myocardial Infarction in a Japanese Population

Validation of the Association of Genetic Variants on Chromosome 9p21 and 1q41 With Myocardial Infarction in a Japanese Population

Association of SNP rs17465637 on Chromosome 1q41 and rs599839 on 1p13.3 with Myocardial Infarction in an American Caucasian Population

O-Glycosylation regulates polarized secretion by modulating Tango1 stability

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