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[PMID]: 29408622
[Au] Autor:Zeng Y; Shen Z; Gu W; Wu M
[Ad] Address:Department of Medical Oncology, Jiangsu Cancer Hospital, Jiangsu Institute of Cancer Research, The Affiliated Cancer Hospital of Nanjing Medical University, Nanjing, Jiangsu 210009, China; The First Clinical Medical College, Nanjing University of Chinese Medicine, Nanjing, Jiangsu 210023, China. Ele
[Ti] Title:Inhibition of hepatocellular carcinoma tumorigenesis by curcumin may be associated with CDKN1A and CTGF.
[So] Source:Gene;651:183-193, 2018 Apr 20.
[Is] ISSN:1879-0038
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:This study aimed to explore crucial genes, transcription factors (TFs), and microRNAs (miRNAs) associated with the effects of curcumin against hepatocellular carcinoma (HCC). We downloaded data (GSE59713) from Gene Expression Omnibus to analyze differentially expressed genes (DEGs) between curcumin-treated and untreated HCC cell lines. Then, we identified the disease ontology (DO) and functional enrichment analysis of these DEGs and analyzed their protein-protein interactions (PPIs). Additionally, we constructed TF-target gene and miRNA-target gene regulatory networks and explored the potential functions of these DEGs. Finally, we detected the expression of CDKN1A, CTGF, LEF1 TF and MIR-19A regulated by curcumin in PLC/PRF/5 cells using RT-PCR. In total, 345 upregulated and 212 downregulated genes were identified. The main enriched pathway of upregulated genes was the TNF signaling pathway. The downregulated genes were significantly enriched in TGF-beta signaling pathway. In addition, most DEGs were significantly enriched in DO terms such as liver cirrhosis, hepatitis, hepatitis C and cholestasis (eg., CTGF). In the constructed PPI network, CDKN1A and CTGF were the key proteins. Moreover, LEF1, CDKN1A, and miR-19A that regulated CTGF were highlighted in the regulatory networks. Furthermore, the expression of CDKN1A, CTGF, LEF1 TF and miR-19A regulated by curcumin in PLC/PRF/5 cells was consistent with the aforementioned bioinformatics analysis results. To conclude, curcumin might exert its protective effects against HCC tumorigenesis by downregulating LEF1 and downregulating CTGF regulated by MIR-19A and upregulating CDKN1A expression.
[Mh] MeSH terms primary: Carcinogenesis/drug effects
Carcinoma, Hepatocellular/drug therapy
Connective Tissue Growth Factor/genetics
Curcumin/therapeutic use
Cyclin-Dependent Kinase Inhibitor p21/genetics
[Mh] MeSH terms secundary: Carcinoma, Hepatocellular/genetics
Cell Line, Tumor
Databases, Genetic
Gene Expression Regulation, Neoplastic/drug effects
Humans
Liver Neoplasms/genetics
Lymphoid Enhancer-Binding Factor 1/genetics
MicroRNAs/genetics
Neoplasm Proteins/genetics
Protein Interaction Maps
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (CDKN1A protein, human); 0 (CTGF protein, human); 0 (Cyclin-Dependent Kinase Inhibitor p21); 0 (LEF1 protein, human); 0 (Lymphoid Enhancer-Binding Factor 1); 0 (MIRN19 microRNA, human); 0 (MicroRNAs); 0 (Neoplasm Proteins); 139568-91-5 (Connective Tissue Growth Factor); IT942ZTH98 (Curcumin)
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[Js] Journal subset:IM
[Da] Date of entry for processing:180207
[St] Status:MEDLINE

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[PMID]: 29028222
[Au] Autor:Choi HJ; Joo HS; Won HY; Min KW; Kim HY; Son T; Oh YH; Lee JY; Kong G
[Ad] Address:Department of Pathology, College of Medicine, Hanyang University, Seoul, Republic of Korea; Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Republic of Korea; Institute for Bioengineering and Biopharmaceutical Research (IBBR), Hanyang University,
[Ti] Title:Role of RBP2-Induced ER and IGF1R-ErbB Signaling in Tamoxifen Resistance in Breast Cancer.
[So] Source:J Natl Cancer Inst;110(4), 2018 Apr 01.
[Is] ISSN:1460-2105
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Background: Despite the benefit of endocrine therapy, acquired resistance during or after treatment still remains a major challenge in estrogen receptor (ER)-positive breast cancer. We investigated the potential role of histone demethylase retinoblastoma-binding protein 2 (RBP2) in endocrine therapy resistance of breast cancer. Methods: Survival of breast cancer patients according to RBP2 expression was analyzed in three different breast cancer cohorts including METABRIC (n = 1980) and KM plotter (n = 1764). RBP2-mediated tamoxifen resistance was confirmed by invitro sulforhodamine B (SRB) colorimetric, colony-forming assays, and invivo xenograft models (n = 8 per group). RNA-seq analysis and receptor tyrosine kinase assay were performed to identify the tamoxifen resistance mechanism by RBP2. All statistical tests were two-sided. Results: RBP2 was associated with poor prognosis to tamoxifen therapy in ER-positive breast cancer (P = .04 in HYU cohort, P = .02 in KM plotter, P = .007 in METABRIC, log-rank test). Furthermore, RBP2 expression was elevated in patients with tamoxifen-resistant breast cancer (P = .04, chi-square test). Knockdown of RBP2 conferred tamoxifen sensitivity, whereas overexpression of RBP2 induced tamoxifen resistance invitro and invivo (MCF7 xenograft: tamoxifen-treated control, mean [SD] tumor volume = 70.8 [27.9] mm3, vs tamoxifen-treated RBP2, mean [SD] tumor volume = 387.9 [85.1] mm3, P < .001). Mechanistically, RBP2 cooperated with ER co-activators and corepressors and regulated several tamoxifen resistance-associated genes, including NRIP1, CCND1, and IGFBP4 and IGFBP5. Furthermore, epigenetic silencing of IGFBP4/5 by RBP2-ER-NRIP1-HDAC1 complex led to insulin-like growth factor-1 receptor (IGF1R) activation. RBP2 also increased IGF1R-ErbB crosstalk and subsequent PI3K-AKT activation via demethylase activity-independent ErbB protein stabilization. Combinational treatment with tamoxifen and PI3K inhibitor could overcome RBP2-mediated tamoxifen resistance (RBP2-overexpressing cells: % cell viability [SD], tamoxifen = 89.0 [3.8]%, vs tamoxifen with BKM120 = 41.3 [5.6]%, P < .001). Conclusions: RBP2 activates ER-IGF1R-ErbB signaling cascade in multiple ways to induce tamoxifen resistance, suggesting that RBP2 is a potential therapeutic target for ER-driven cancer.
[Mh] MeSH terms primary: Breast Neoplasms/metabolism
Carcinoma, Ductal, Breast/metabolism
Drug Resistance, Neoplasm
Neoplasm Proteins/physiology
Receptors, Estrogen/metabolism
Retinoblastoma-Binding Protein 2/physiology
[Mh] MeSH terms secundary: Adaptor Proteins, Signal Transducing/metabolism
Analysis of Variance
Animals
Antineoplastic Agents, Hormonal/therapeutic use
Breast Neoplasms/chemistry
Breast Neoplasms/drug therapy
Breast Neoplasms/pathology
Carcinoma, Ductal, Breast/chemistry
Carcinoma, Ductal, Breast/drug therapy
Carcinoma, Ductal, Breast/pathology
Carrier Proteins/metabolism
Cohort Studies
Colorimetry
Disease-Free Survival
Drug Resistance, Neoplasm/genetics
Female
Heterografts
Humans
Kaplan-Meier Estimate
MCF-7 Cells
Mice
Mice, Inbred NOD
Mice, SCID
Neoplasm Proteins/metabolism
Neoplastic Stem Cells
Nuclear Proteins/metabolism
Phosphatidylinositol 3-Kinases/antagonists & inhibitors
Phosphatidylinositol 3-Kinases/metabolism
Receptor, ErbB-2/metabolism
Receptor, IGF Type 1/metabolism
Retinoblastoma-Binding Protein 2/metabolism
Tamoxifen/therapeutic use
Tumor Burden
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Adaptor Proteins, Signal Transducing); 0 (Antineoplastic Agents, Hormonal); 0 (Carrier Proteins); 0 (IGFBP5-interacting protein, human); 0 (Neoplasm Proteins); 0 (Nuclear Proteins); 0 (Receptors, Estrogen); 0 (nuclear receptor interacting protein 1); 094ZI81Y45 (Tamoxifen); EC 1.14.11.27 (Retinoblastoma-Binding Protein 2); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.10.1 (Receptor, ErbB-2); EC 2.7.10.1 (Receptor, IGF Type 1)
[Em] Entry month:1710
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[Js] Journal subset:IM
[Da] Date of entry for processing:171014
[St] Status:MEDLINE
[do] DOI:10.1093/jnci/djx207

  3 / 13547 MEDLINE  
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[PMID]: 29249623
[Au] Autor:Nambam B; Schatz D
[Ad] Address:Pediatric Endocrinology, Louisiana State University Health, Shreveport, United States.
[Ti] Title:Growth hormone and insulin-like growth factor-I axis in type 1 diabetes.
[So] Source:Growth Horm IGF Res;38:49-52, 2018 02.
[Is] ISSN:1532-2238
[Cp] Country of publication:Scotland
[La] Language:eng
[Ab] Abstract:The precise mechanisms relating type 1 diabetes (T1D) and poor glycemic control to the axis of growth hormone (GH), insulin like growth factor- I (IGF-I), and IGF binding protein-3 (IGFBP-3) remain to be definitively determined. GH resistance with low IGF-I as is frequently seen in patients with T1D is often related to portal hypoinsulization, and lack of upregulation of GH receptors. There are conflicting reports of the effect of a dysregulated GH/IGF-I axis on height in children and adolescents with T1D, as well as on chronic complications. This brief review discusses some of the interactions between the GH/IGF-I axis and T1D pathology, and vice-versa.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[St] Status:In-Process

  4 / 13547 MEDLINE  
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[PMID]: 29189343
[Au] Autor:Ostermann M; McCullough PA; Forni LG; Bagshaw SM; Joannidis M; Shi J; Kashani K; Honore PM; Chawla LS; Kellum JA; all SAPPHIRE Investigators
[Ad] Address:Department of Critical Care, King's College London, Guy's & St Thomas' Hospital, London, United Kingdom.
[Ti] Title:Kinetics of Urinary Cell Cycle Arrest Markers for Acute Kidney Injury Following Exposure to Potential Renal Insults.
[So] Source:Crit Care Med;46(3):375-383, 2018 03.
[Is] ISSN:1530-0293
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:OBJECTIVES: Urinary tissue inhibitor of metalloproteinase-2 and insulin-like growth factor binding protein 7 predict the development of acute kidney injury following renal insults of varied aetiology. To aid clinical interpretation, we describe the kinetics of biomarker elevations around an exposure. DESIGN: In an ancillary analysis of the multicenter SAPPHIRE study, we examined the kinetics of the urinary [tissue inhibitor of metalloproteinase-2]•[insulin-like growth factor binding protein 7] in association with exposure to common renal insults (major surgery, IV radiocontrast, vancomycin, nonsteroidal anti-inflammatory drugs, and piperacillin/tazobactam). SETTING: Thirty-five sites in North America and Europe between September 2010 and June 2012. PATIENTS: Seven hundred twenty-three critically ill adult patients admitted to the ICU. INTERVENTIONS: None. MEASUREMENTS AND MAIN RESULTS: We compared the urinary [tissue metalloproteinase-2]•[insulin growth factor binding protein 7] kinetics from the day prior to exposure up to 5 days after exposure in patients developing acute kidney injury stage 2-3, stage 1, or no acute kidney injury by Kidney Disease Improving Global Outcome criteria. Among the 723 patients, 679 (94%) had at least one, 70% had more than one, and 35% had three or more exposures to a known renal insult. There was a significant association between cumulative number of exposures up to study day 3 and risk of acute kidney injury (p = 0.02) but no association between the specific type of exposure and acute kidney injury (p = 0.22). With the exception of radiocontrast, patients who developed acute kidney injury stage 2-3 after one of the five exposures, had a clear rise and fall of urinary [tissue inhibitor of metalloproteinase-2]•[insulin-like growth factor binding protein 7] from the day of exposure to 24-48 hours later. In patients without acute kidney injury, there was no significant elevation in urinary [tissue inhibitor of metalloproteinase-2]•[insulin-like growth factor binding protein 7]. CONCLUSIONS: Exposure to potential renal insults is common. In patients developing acute kidney injury stage 2-3, the kinetics of urinary [tissue inhibitor of metalloproteinase-2]•[insulin-like growth factor binding protein 7] matched the exposure except in the case of radiocontrast.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[St] Status:In-Data-Review
[do] DOI:10.1097/CCM.0000000000002847

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[PMID]: 29505681
[Au] Autor:Schmitt FCF; Salgado E; Friebe J; Schmoch T; Uhle F; Fleming T; Zemva J; Kihm L; Nusshag C; Morath C; Zeier M; Bruckner T; Mehrabi A; Nawroth PP; Weigand MA; Hofer S; Brenner T
[Ad] Address:Department of Anesthesiology, Heidelberg University Hospital, Heidelberg, Germany.
[Ti] Title:Cell cycle arrest and cell death correlate with the extent of ischemia and reperfusion injury in patients following kidney transplantation - Results of an observational pilot study.
[So] Source:Transpl Int;, 2018 Mar 05.
[Is] ISSN:1432-2277
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:BACKGROUND: A prolonged cold ischemia time (CIT) is suspected to be associated with an increased ischemia and reperfusion injury (IRI) resulting in an increased damage to the graft. METHODS: In total, 91 patients were evaluated for a delayed graft function within 7 days after kidney transplantation (48 deceased, 43 living donors). Blood and urine samples were collected before, immediately after the operation, and 1, 3, 5, 7 and 10 days later. Plasma and/or urine levels of total keratin 18 (total K18), caspase-cleaved keratin 18 (cc K18), the soluble receptor for advanced glycation end-products (sRAGE), tissue inhibitor of metalloproteinase-2 and insulin-like growth factor-binding protein-7 ([TIMP-2][IGFBP7]) were measured. RESULTS: As a result of prolonged CIT and increased IRI, deceased donor transplantations were shown to suffer from a more distinct cell cycle arrest and necrotic cell death. Plasmatic total K18 and urinary [TIMP-2][IGFBP7] were therefore demonstrated to be of value for the detection of a delayed graft function (DGF), since they improved the diagnostic performance of a routinely used clinical scoring system. CONCLUSIONS: Plasmatic total K18 and urinary [TIMP-2][IGFBP7] measurements are potentially suitable for early identification of patients at high risk for a DGF following kidney transplantation from deceased or living donors. This article is protected by copyright. All rights reserved.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180305
[Lr] Last revision date:180305
[St] Status:Publisher
[do] DOI:10.1111/tri.13148

  6 / 13547 MEDLINE  
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[PMID]: 28460483
[Au] Autor:Guo XF; Zhu XF; Cao HY; Zhong GS; Li L; Deng BG; Chen P; Wang PZ; Miao QF; Zhen YS
[Ad] Address:Department of Microbiology, School of Basic Medical Sciences, Xinxiang Medical University, Xinxiang, China.
[Ti] Title:A bispecific enediyne-energized fusion protein targeting both epidermal growth factor receptor and insulin-like growth factor 1 receptor showing enhanced antitumor efficacy against non-small cell lung cancer.
[So] Source:Oncotarget;8(16):27286-27299, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Epidermal growth factor receptor (EGFR) and insulin-like growth factor 1 receptor (IGF-1R) both overexpressed on non-small cell lung cancer (NSCLC) and are known cooperatively to promote tumor progression and drug resistance. This study was to construct a novel bispecific fusion protein EGF-IGF-LDP-AE consisting of EGFR and IGF-IR specific ligands (EGF and IGF-1) and lidamycin, an enediyne antibiotic with potent antitumor activity, and investigate its antitumor efficacy against NSCLC. Binding and internalization assays showed that EGF-IGF-LDP protein could bind to NSCLC cells with high affinity and then internalized into cells with higher efficiency than that of monospecific proteins. In vitro, the enediyne-energized analogue of bispecific fusion protein (EGF-IGF-LDP-AE) displayed extremely potent cytotoxicity to NSCLC cell lines with IC50<10-11 mol/L. Moreover, the bispecific protein EGF-IGF-LDP-AE was more cytotoxic than monospecific proteins (EGF-LDP-AE and LDP-IGF-AE) and lidamycin. In vivo, EGF-IGF-LDP-AE markedly inhibited the growth of A549 xenografts, and the efficacy was more potent than that of lidamycin and monospecific counterparts. EGF-IGF-LDP-AE caused significant cell cycle arrest and it also induced cell apoptosis in a dosage-dependent manner. Pretreatment with EGF-IGF-LDP-AE inhibited EGF-, IGF-stimulated EGFR and IGF-1R phosphorylation, and blocked two main downstream signaling molecules AKT and ERK activation. These data suggested that EGF-LDP-IGF-AE protein would be a promising targeted agent for NSCLC patients with EGFR and/or IGF-1R overexpression.
[Mh] MeSH terms primary: Carcinoma, Non-Small-Cell Lung/metabolism
Enediynes
Insulin-Like Growth Factor I/antagonists & inhibitors
Lung Neoplasms/metabolism
Receptor, Epidermal Growth Factor/antagonists & inhibitors
Recombinant Fusion Proteins/pharmacology
[Mh] MeSH terms secundary: Animals
Apoptosis/drug effects
Carcinoma, Non-Small-Cell Lung/drug therapy
Carcinoma, Non-Small-Cell Lung/pathology
Cell Cycle/drug effects
Cell Line, Tumor
Cell Survival/drug effects
Disease Models, Animal
Enediynes/chemistry
Female
Humans
Insulin-Like Growth Factor I/metabolism
Lung Neoplasms/drug therapy
Lung Neoplasms/pathology
Mice
Protein Binding
Receptor, Epidermal Growth Factor/metabolism
Recombinant Fusion Proteins/chemistry
Recombinant Fusion Proteins/metabolism
Signal Transduction/drug effects
Xenograft Model Antitumor Assays
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Enediynes); 0 (Recombinant Fusion Proteins); 67763-96-6 (Insulin-Like Growth Factor I); EC 2.7.10.1 (Receptor, Epidermal Growth Factor)
[Em] Entry month:1803
[Cu] Class update date: 180305
[Lr] Last revision date:180305
[Js] Journal subset:IM
[Da] Date of entry for processing:170503
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15933

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[PMID]: 28460437
[Au] Autor:Li C; Zeng M; Chi H; Shen J; Ng TB; Jin G; Lu D; Fan X; Xiong B; Xiao Z; Sha O
[Ad] Address:Department of Anatomy, Histology and Developmental Biology, School of Basic Medical Sciences, Shenzhen University Health Science Centre, Shenzhen, Guangdong, China.
[Ti] Title:Trichosanthin increases Granzyme B penetration into tumor cells by upregulation of CI-MPR on the cell surface.
[So] Source:Oncotarget;8(16):26460-26470, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Trichosanthin is a plant toxin belonging to the family of ribosome-inactivating proteins. It has various biological and pharmacological activities, including anti-tumor and immunoregulatory effects. In this study, we explored the potential medicinal applications of trichosanthin in cancer immunotherapy. We found that trichosanthin and cation-independent mannose-6-phosphate receptor competitively bind to the Golgi-localized, γ-ear containing and Arf-binding proteins. It in turn promotes the translocation of cation-independent mannose-6-phosphate receptor from the cytosol to the plasma membrane, which is a receptor of Granzyme B. The upregulation of this receptor on the tumor cell surface increased the cell permeability to Granzyme B, and the latter is one of the major factors of cytotoxic T lymphocyte-mediated tumor cell apoptosis. These results suggest a novel potential application of trichosanthin and shed light on its anti-tumor immunotherapy.
[Mh] MeSH terms primary: Cell Membrane/metabolism
Granzymes/metabolism
Receptor, IGF Type 2/metabolism
Trichosanthin/metabolism
[Mh] MeSH terms secundary: Amino Acid Sequence
Animals
Apoptosis
Cell Line, Tumor
Cell Membrane Permeability
Disease Models, Animal
Humans
Male
Mice
Protein Binding
Protein Interaction Domains and Motifs
Trichosanthin/chemistry
Xenograft Model Antitumor Assays
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Receptor, IGF Type 2); 60318-52-7 (Trichosanthin); EC 3.4.21.- (GZMB protein, human); EC 3.4.21.- (Granzymes)
[Em] Entry month:1803
[Cu] Class update date: 180305
[Lr] Last revision date:180305
[Js] Journal subset:IM
[Da] Date of entry for processing:170503
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15518

  8 / 13547 MEDLINE  
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[PMID]: 29483580
[Au] Autor:Xu Y; Kong GK; Menting JG; Margetts MB; Delaine CA; Jenkin LM; Kiselyov VV; De Meyts P; Forbes BE; Lawrence MC
[Ad] Address:The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, VIC, 3052, Australia.
[Ti] Title:How ligand binds to the type 1 insulin-like growth factor receptor.
[So] Source:Nat Commun;9(1):821, 2018 Feb 26.
[Is] ISSN:2041-1723
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Human type 1 insulin-like growth factor receptor is a homodimeric receptor tyrosine kinase that signals into pathways directing normal cellular growth, differentiation and proliferation, with aberrant signalling implicated in cancer. Insulin-like growth factor binding is understood to relax conformational restraints within the homodimer, initiating transphosphorylation of the tyrosine kinase domains. However, no three-dimensional structures exist for the receptor ectodomain to inform atomic-level understanding of these events. Here, we present crystal structures of the ectodomain in apo form and in complex with insulin-like growth factor I, the latter obtained by crystal soaking. These structures not onlyprovide a wealth of detail of the growth factor interaction with the receptor's primary ligand-binding site but also indicate that ligand binding separates receptor domains by a mechanism of induced fit. Our findings are of importance to the design of agents targeting IGF-1R and its partner protein, the human insulin receptor.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180304
[Lr] Last revision date:180304
[St] Status:In-Data-Review
[do] DOI:10.1038/s41467-018-03219-7

  9 / 13547 MEDLINE  
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[PMID]: 29496979
[Au] Autor:McCarthy JM; McCann-Crosby BM; Rech ME; Yin J; Chen CA; Ali MA; Nguyen HN; Miller JL; Schaaf CP
[Ad] Address:Jan and Dan Duncan Neurological Research Institute at Texas Children's Hospital, Houston, Texas, USA.
[Ti] Title:Hormonal, metabolic and skeletal phenotype of Schaaf-Yang syndrome: a comparison to Prader-Willi syndrome.
[So] Source:J Med Genet;, 2018 Mar 01.
[Is] ISSN:1468-6244
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:BACKGROUND: Nonsense and frameshift mutations in the maternally imprinted, paternally expressed gene located in the Prader-Willi critical region 15q11-15q13, have been reported to cause Schaaf-Yang syndrome (SYS), a genetic disorder that manifests as developmental delay/intellectual disability, hypotonia, feeding difficulties and autism spectrum disorder. Prader-Willi syndrome (PWS) is a genetic disorder characterised by severe infantile hypotonia, hypogonadotrophic hypogonadism, early childhood onset obesity/hyperphagia, developmental delay/intellectual disability and short stature. Scoliosis and growth hormone insufficiency are also prevalent in PWS.There is extensive documentation of the endocrine and metabolic phenotypes for PWS, but not for SYS. This study served to investigate the hormonal, metabolic and body composition phenotype of SYS and its potential overlap with PWS. METHODS: In nine individuals with SYS (5 female/4 male; aged 5-17 years), we measured serum ghrelin, glucose, insulin-like growth factor 1 (IGF-1), insulin-like growth factor binding protein 3, follicle-stimulating hormone, luteinising hormone, thyroid-stimulating hormone, free T4, uric acid and testosterone, and performed a comprehensive lipid panel. Patients also underwent X-ray and dual-energy X-ray absorptiometry analyses to assess for scoliosis and bone mineral density. RESULTS: Low IGF-1 levels despite normal weight/adequate nutrition were observed in six patients, suggesting growth hormone deficiency similar to PWS. Fasting ghrelin levels were elevated, as seen in individuals with PWS. X-rays revealed scoliosis >10 in three patients, and abnormal bone mineral density in six patients, indicated by Z-scores of below -2 SDs. CONCLUSION: This is the first analysis of the hormonal, metabolic and body composition phenotype of SYS. Our findings suggest that there is marked, but not complete overlap between PWS and SYS.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180302
[Lr] Last revision date:180302
[St] Status:Publisher

  10 / 13547 MEDLINE  
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[PMID]: 29369405
[Au] Autor:Kim T; Havighurst T; Kim K; Albertini M; Xu YG; Spiegelman VS
[Ad] Address:Department of Dermatology, University of Wisconsin School of Medicine and Public Health, Madison, Wisconsin.
[Ti] Title:Targeting insulin-like growth factor 2 mRNA-binding protein 1 (IGF2BP1) in metastatic melanoma to increase efficacy of BRAF inhibitors.
[So] Source:Mol Carcinog;, 2018 Jan 25.
[Is] ISSN:1098-2744
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Melanoma is one of the deadliest forms of skin cancer. Although BRAF inhibitors significantly enhance survival of metastatic melanoma patients, most patients relapse after less than a year of treatment. We previously reported that mRNA binding protein Insulin-like growth factor 2 mRNA-binding protein 1 (IGF2BP1) is overexpressed in metastatic melanoma and that expression of IGF2BP1 confers resistance to chemotherapeutic agents. Here we demonstrate that IGF2BP1 plays an important role in the sensitivity of melanoma to targeted therapy. Inhibition of IGF2BP1 enhances the effects of BRAF-inhibitor and BRAF-MEK inhibitors in BRAF melanoma. Also, knockdown of IGF2BP1 alone is sufficient to reduce tumorigenic characteristics in vemurafenib-resistant melanoma. These findings suggest that IGF2BP1 can be a novel therapeutic target for melanoma.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180302
[Lr] Last revision date:180302
[St] Status:Publisher
[do] DOI:10.1002/mc.22786


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