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A missense variant in aryl hydrocarbon receptor-interacting protein (AIP (Montrer AIP Protéines)) gene and a truncating mutation in multiple endocrine neoplasia I protein (MEN1) gene were both detected in the proband and his father, showing limited co-segregation with phenotype.
menin is regulated by extracellular signaling factors and has a role in nuclear receptor activation and hepatobiliary pathology in various hepatic cell types [review]
Each of these autosomal dominant syndromes results from a specific germline mutation in unique genes: MEN1 is due to pathogenic MEN1 variants (11q13), MEN2A (Montrer RET Protéines) and MEN2B (Montrer RET Protéines) are due to pathogenic RET (Montrer RET Protéines) variants (10q11.21), MEN4 (Montrer CDKN1B Protéines) is due to pathogenic CDKN1B (Montrer CDKN1B Protéines) variants (12p13.1), and the HPT-JT syndrome is due to pathogenic CDC73 (Montrer CDC73 Protéines) variants (1q25).
Menin deficiency is the consequence of a MEN1 mutation in most menin-negative primary hyperparathyroidism tissues
Data demonstrate an essential role for MLL1 and menin in mediating tumor maintenance and posterior HOXD gene activation in Ewing sarcoma.
Data suggest that a novel germline missense mutation in MEN1 (p.Gly42Val) accounts for type 1 multiple endocrine neoplasia in a family; this mutation was found in the patient and his mother. [CASE REPORT]
Our study provides important insights into the role of menin in DNA methylation (Montrer HELLS Protéines) and its impact on the pathogenesis of Multiple endocrine neoplasia type 1 syndrome tumor development.
MEN1 exerts an anti-proliferative function by regulating a distinct expression signature.
expression increa (Montrer MLXIP Protéines)sed in late-stage primary scleros (Montrer TGFB1 Protéines)ing cholangitis
The results provide novel molecular insights into the tumor suppressor activity of menin, which is partly mediated by proteasomal degradation of beta-catenin (Montrer CTNNB1 Protéines) and inhibition of Wnt (Montrer WNT2 Protéines)/beta-catenin (Montrer CTNNB1 Protéines) signaling.
Men1-deficient osteocytes was expressed numerous soluble mediators such as C-X-C motif chemokine 10 (CXCL10 (Montrer CXCL10 Protéines) and a novel role for Men1 in osteocyte-osteoclast crosstalk by controlling osteoclastogenesis through the action of soluble factors.
Gastrin induces nuclear export and proteasome degradation of menin in duodenal glial cells.
gene expression analysis revealed that Menin was involved in the maintenance of the high expression of the previously identified Th2-specific genes rather than the induction of these genes. This result suggests that Menin plays a role in the maintenance of Th2 cell identity.This study confirmed the critical role of Menin in Th2 cell-mediated immune responses.
Inhibition of miR (Montrer MLXIP Protéines)-24 increases menin and TGF-beta1 (Montrer TGFB1 Protéines) expression, subsequently increasing hepatic fibrosis in FVB/NJ WT and Mdr2 (Montrer ABCB4 Protéines)(-/-) mice.
Menin and PRMT5 (Montrer PRMT5 Protéines) suppress GLP1R (Montrer GLP1R Protéines) transcript levels and PKA-mediated phosphorylation of FOXO1 (Montrer FOXO1 Protéines) and CREB (Montrer CREB1 Protéines).
Inactivation of Kmt2a in Men1-deficient mice accelerated pancreatic islet tumorigenesis and shortened the average life span. Increases in cell proliferation were observed in mouse pancreatic islet tumors upon inactivation of both Kmt2a and Men1.
Data suggest that menin inhibits differentiation into terminal effectors and positively controls proliferation and survival of Ag-specific CD8 (Montrer CD8A Protéines)(+) T cells that are activated upon infection; study uncovered an important role for menin in the immune response of CD8 (Montrer CD8A Protéines)(+) T cells to infection
Our data further confirms that deletion of Men1 alone does not favour carcinoid development, but rather cooperates with additional loci.
Menin binds on the promoter of Inhbb (Montrer INHBB Protéines) gene where it favours the recruitment of Ezh2 (Montrer EZH2 Protéines) via an indirect mechanism involving Akt (Montrer AKT1 Protéines)-phosphorylation.
Results indicate that fasted male Men1(+/-) mice, in the early stage of development of MEN1, display glucose metabolic disorders. These disorders are caused not by direct induction of insulin (Montrer INS Protéines) resistance, but via increased glucagon (Montrer GCG Protéines) secretion and the consequent stimulation of hepatic glucose production.
This gene encodes menin, a putative tumor suppressor associated with a syndrome known as multiple endocrine neoplasia type 1. In vitro studies have shown menin is localized to the nucleus, possesses two functional nuclear localization signals, and inhibits transcriptional activation by JunD, however, the function of this protein is not known. Two messages have been detected on northern blots but the larger message has not been characterized. Alternative splicing results in multiple transcript variants.
, multiple endocrine neoplasia protein
, multiple endocrine neoplasia 1
, multiple endocrine neoplasia I