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[PMID]:29505529
[Au] Autor:Yue H; Xu Q; Xie S
[Ad] Endereço:Department of Neurosurgery, Jinan Central Hospital Affiliated to Shandong University, Jinan.
[Ti] Título:High EMP3 expression might independently predict poor overall survival in glioblastoma and its expression is related to DNA methylation.
[So] Source:Medicine (Baltimore);97(1):e9538, 2018 Jan.
[Is] ISSN:1536-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this study, we analyzed the prognostic value of epithelial membrane protein 3 (EMP3) in terms of overall survival (OS) in glioblastoma multiforme (GBM) and the association between its expression and DNA methylation.Bioinformatic analysis was performed by using data from the Cancer Genome Atlas (TCGA) database.EMP3 expression was markedly higher in GBM tissues than in normal brain tissues. High EMP3 expression was associated with significantly worse OS in patients with GBM. Univariate and multivariate analysis showed that EMP3 expression was an independent prognostic factor of poor OS no matter converting its expression into categorical variables (Hazard Ratio [HR] = 1.359, 95%CI: 1.118-1.652, P = .002) or setting it as a continuous variable (HR = 1.178, 95%CI: 1.101-1.260, P < .001). Among different subtypes of GBM, proneural subtype had the lowest EMP3 expression. The lowest EMP3 expression was observed in cluster 5 DNA methylation, which all belong to G-CIMP phenotype. Regression analysis confirmed a moderate negative correlation between EMP3 expression and its DNA methylation (Pearson's r = -0.61).Based on these findings, we infer that high EMP3 expression might be an independent indicator of unfavorable OS in GBM. EMP3 expression might be repressed by DNA methylation.
[Mh] Termos MeSH primário: Neoplasias Encefálicas/metabolismo
Glioblastoma/metabolismo
Glicoproteínas de Membrana/metabolismo
[Mh] Termos MeSH secundário: Idoso
Neoplasias Encefálicas/mortalidade
Estudos de Casos e Controles
China/epidemiologia
Ilhas de CpG
Metilação de DNA
Feminino
Glioblastoma/mortalidade
Seres Humanos
Masculino
Meia-Idade
[Pt] Tipo de publicação:JOURNAL ARTICLE; OBSERVATIONAL STUDY
[Nm] Nome de substância:
0 (EMP3 protein, human); 0 (Membrane Glycoproteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:180306
[St] Status:MEDLINE
[do] DOI:10.1097/MD.0000000000009538


  2 / 63804 MEDLINE  
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[PMID]:28470789
[Au] Autor:Kulkarni SS; Vasantha K; Gogri H; Parchure D; Madkaikar M; Férec C; Fichou Y
[Ad] Endereço:National Institute of Immunohaematology, Indian Council of Medical Research (NIIH-ICMR), Mumbai, India.
[Ti] Título:First report of Rh individuals in the Indian population and characterization of the underlying molecular mechanisms.
[So] Source:Transfusion;57(8):1944-1948, 2017 08.
[Is] ISSN:1537-2995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Rh phenotype is an extremely rare condition characterized by no expression of Rh antigens at the surface of red blood cells. Although rare, genetic bases of this phenotype are well known and include mutations within either the RH (RHD and RHCE) genes or the RHAG gene. So far Rh has been reported in individuals of Caucasian, African, and Asian origin. Here, we report individuals from two families of Indian origin representing such a rare phenotype. STUDY DESIGN AND METHODS: Serologic analysis was carried out by testing with anti-D, -C, -c, -E, and -e in Rh individuals and their family members. RH genes were analyzed by standard molecular approaches, including Sanger sequencing and quantitative multiplex polymerase chain reaction (PCR) of short fluorescent fragments. RHAG gene was investigated by exon-specific PCR amplification and Sanger sequencing. RESULTS: In one family, RHAG gene was found to be deleted at the homozygous state in the propositus, suggesting Rh of the regulator type. In the other family, a novel splice site variant in RHCE in cis with whole RHD gene deletion was identified at the homozygous state. Further functional analysis by minigene splicing assay showed that this variation, that is, c.801 + 1G>A, completely impairs normal splicing, then inactivating the expression of RhCE protein. Contrary to the former case, these data suggest Rh of the amorph type. CONCLUSION: Overall, we report for the first time the molecular mechanisms responsible for Rh phenotype in individuals of Indian origin. This study contributes to extend the molecular spectrum of variations in Rh individuals.
[Mh] Termos MeSH primário: Grupo com Ancestrais do Continente Asiático/genética
Linhagem
Sistema do Grupo Sanguíneo Rh-Hr/genética
[Mh] Termos MeSH secundário: Proteínas Sanguíneas/genética
Família
Feminino
Deleção de Genes
Seres Humanos
Índia/epidemiologia
Masculino
Glicoproteínas de Membrana/genética
Processamento de RNA/genética
Testes Sorológicos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Blood Proteins); 0 (Membrane Glycoproteins); 0 (RHAG protein, human); 0 (RHCE protein, human); 0 (Rh-Hr Blood-Group System)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1111/trf.14150


  3 / 63804 MEDLINE  
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[PMID]:29441921
[Au] Autor:Zhuo H; Zhou L
[Ti] Título:Gpnmb/osteoactivin: an indicator and therapeutic target in tumor and nontumorous lesions.
[So] Source:Pharmazie;71(10):555-561, 2016 Oct 01.
[Is] ISSN:0031-7144
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Non-metastatic melanoma glycoprotein B (Gpnmb), a type I transmembrane glycoprotein, was first cloned and described in low-metastatic human melanoma and xenografts in 1995. Up to now a growing number of studies have confirmed that Gpnmb is expressed not only in numerous normal tissues but also at pathological sites and malignant tissues and often connected with the invasive and metastatic phenotypes, including breast cancer. Nowadays, immunotherapeutic approaches for cancer therapy, by which monoclonal antibodies (Mabs) target tumor specific antigens, have shown great potential. Glembatumumabvedotin, also called CR011-vcMMAE, is a Mab-drug conjugate which was developed for the treatment of Gpnmb-expressing cancers. Several phase I/II studies have confirmed the safety and activity of glembatumumabvedotin in patients with advanced/metastatic breast cancer and unresectable cutaneous melanoma. Moreover, increasing numbers of studies have supported the potential roles of targeting Gpnmb with glembatumumabvedotin in patients with recurrent osteosarcoma, uveal melanoma, ALS, Gaucher disease, pancreatic ductal adenocarcinoma etc. This review will summarize the latest understanding of Gpnmb in the aspects of diagnosis, progression and prognosis of pathological disorders and neoplasms, emphasizing the clinical advances in targeting Gpnmb-expressing malignancies.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Biomarcadores Tumorais/análise
Biomarcadores/análise
Glicoproteínas de Membrana/efeitos dos fármacos
Glicoproteínas de Membrana/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Biomarkers); 0 (Biomarkers, Tumor); 0 (GPNMB protein, human); 0 (Membrane Glycoproteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180215
[St] Status:MEDLINE
[do] DOI:10.1691/ph.2016.6683


  4 / 63804 MEDLINE  
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[PMID]:29329339
[Au] Autor:Granger BL
[Ad] Endereço:Department of Microbiology and Immunology, Montana State University, Bozeman, Montana, United States of America.
[Ti] Título:Accessibility and contribution to glucan masking of natural and genetically tagged versions of yeast wall protein 1 of Candida albicans.
[So] Source:PLoS One;13(1):e0191194, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Yeast wall protein 1 (Ywp1) is an abundant glycoprotein of the cell wall of the yeast form of Candida albicans, the most prevalent fungal pathogen of humans. Antibodies that bind to the polypeptide backbone of isolated Ywp1 show little binding to intact yeast cells, presumably because the Ywp1 epitopes are masked by the polysaccharides of the mannoproteins that form the outer layer of the cell wall. Rare cells do exhibit much greater anti-Ywp1 binding, however, and one of these was isolated and characterized. No differences were seen in its Ywp1, but it exhibited greater adhesiveness, sensitivity to wall perturbing agents, and exposure of its underlying ß-1,3-glucan layer to external antibodies. The molecular basis for this greater epitope accessibility has not been determined, but has facilitated exploration of how these properties change as a function of cell growth and morphology. In addition, previously engineered strains with reduced quantities of Ywp1 in their cell walls were also found to have greater ß-1,3-glucan exposure, indicating that Ywp1 itself contributes to the masking of wall epitopes, which may be important for understanding the anti-adhesive effect of Ywp1. Ectopic production of Ywp1 by hyphae, which reduces the adhesivity of these filamentous forms of C. albicans, was similarly found to reduce exposure of the ß-1,3-glucan in their walls. To monitor Ywp1 in the cell wall irrespective of its accessibility, green fluorescent protein (Gfp) was genetically inserted into wall-anchored Ywp1 using a bifunctional cassette that also allowed production from a single transfection of a soluble, anchor-free version. The wall-anchored Ywp1-Gfp-Ywp1 accumulated in the wall of the yeast forms but not hyphae, and appeared to have properties similar to native Ywp1, including its adhesion-inhibiting effect. Some pseudohyphal walls also detectably accumulated this probe. Strains of C. albicans with tandem hemagglutinin (HA) epitopes inserted into wall-anchored Ywp1 were previously created by others, and were further explored here. As above, rare cells with much greater accessibility of the HA epitopes were isolated, and also found to exhibit greater exposure of Ywp1 and ß-1,3-glucan. The placement of the HA cassette inhibited the normal N-glycosylation and propeptide cleavage of Ywp1, but the wall-anchored Ywp1-HA-Ywp1 still accumulated in the cell wall of yeast forms. Bifunctional transformation cassettes were used to additionally tag these molecules with Gfp, generating soluble Ywp1-HA-Gfp and wall-anchored Ywp1-HA-Gfp-Ywp1 molecules. The former revealed unexpected electrophoretic properties caused by the HA insertion, while the latter further highlighted differences between the presence of a tagged Ywp1 molecule (as revealed by Gfp fluorescence) and its accessibility in the cell wall to externally applied antibodies specific for HA, Gfp and Ywp1, with accessibility being greatest in the rapidly expanding walls of budding daughter cells. These strains and results increase our understanding of cell wall properties and how C. albicans masks itself from recognition by the human immune system.
[Mh] Termos MeSH primário: Candida albicans/genética
Candida albicans/metabolismo
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
beta-Glucanas/metabolismo
[Mh] Termos MeSH secundário: Anticorpos Antifúngicos
Antígenos de Fungos/química
Antígenos de Fungos/genética
Antígenos de Fungos/metabolismo
Candida albicans/imunologia
Parede Celular/genética
Parede Celular/imunologia
Parede Celular/metabolismo
Epitopos/química
Epitopos/genética
Epitopos/metabolismo
Proteínas Fúngicas/imunologia
Glicosilação
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/imunologia
Proteínas de Fluorescência Verde/metabolismo
Hemaglutininas/genética
Hemaglutininas/imunologia
Hemaglutininas/metabolismo
Seres Humanos
Glicoproteínas de Membrana/genética
Glicoproteínas de Membrana/imunologia
Glicoproteínas de Membrana/metabolismo
Engenharia de Proteínas
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/imunologia
Proteínas Recombinantes de Fusão/metabolismo
beta-Glucanas/química
beta-Glucanas/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Fungal); 0 (Antigens, Fungal); 0 (Epitopes); 0 (Fungal Proteins); 0 (Hemagglutinins); 0 (Membrane Glycoproteins); 0 (Recombinant Fusion Proteins); 0 (beta-Glucans); 0 (mannoproteins); 147336-22-9 (Green Fluorescent Proteins); 9051-97-2 (beta-1,3-glucan)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191194


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[PMID]:29317664
[Au] Autor:Choi HJ; Park A; Kang S; Lee E; Lee TA; Ra EA; Lee J; Lee S; Park B
[Ad] Endereço:Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, 03722, South Korea.
[Ti] Título:Human cytomegalovirus-encoded US9 targets MAVS and STING signaling to evade type I interferon immune responses.
[So] Source:Nat Commun;9(1):125, 2018 01 09.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Human cytomegalovirus (HCMV) has evolved sophisticated immune evasion mechanisms that target both the innate and adaptive immune responses. However, how HCMV encoded proteins are involved in this immune escape is not clear. Here, we show that HCMV glycoprotein US9 inhibits the IFN-ß response by targeting the mitochondrial antiviral-signaling protein (MAVS) and stimulator of interferon genes (STING)-mediated signaling pathways. US9 accumulation in mitochondria attenuates the mitochondrial membrane potential, leading to promotion of MAVS leakage from the mitochondria. Furthermore, US9 disrupts STING oligomerization and STING-TBK1 association through competitive interaction. Intriguingly, US9 blocks interferon regulatory factor 3 (IRF3) nuclear translocation and its cytoplasmic domain is essential for inhibiting IRF3 activation. Mutant HCMV lacking US7-16 is impaired in antagonism of MAVS/STING-mediated IFN-ß expression, an effect that is reversible by the introduction of US9. Our findings indicate that HCMV US9 is an antagonist of IFN signaling to persistently evade host innate antiviral responses.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/imunologia
Interferon Tipo I/imunologia
Glicoproteínas de Membrana/imunologia
Proteínas de Membrana/imunologia
Proteínas Virais/imunologia
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Células Cultivadas
Células HEK293
Células HeLa
Interações Hospedeiro-Patógeno/imunologia
Seres Humanos
Evasão da Resposta Imune/imunologia
Fator Regulador 3 de Interferon/imunologia
Fator Regulador 3 de Interferon/metabolismo
Interferon Tipo I/metabolismo
Glicoproteínas de Membrana/fisiologia
Proteínas de Membrana/metabolismo
Mitocôndrias/imunologia
Mitocôndrias/metabolismo
Mitocôndrias/virologia
Transdução de Sinais/imunologia
Células U937
Proteínas Virais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (IRF3 protein, human); 0 (Interferon Regulatory Factor-3); 0 (Interferon Type I); 0 (MPYS protein, human); 0 (Membrane Glycoproteins); 0 (Membrane Proteins); 0 (US9 protein, Human herpesvirus 5); 0 (VISA protein, human); 0 (Viral Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180111
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02624-8


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[PMID]:28457753
[Au] Autor:Sadovnik I; Herrmann H; Eisenwort G; Blatt K; Hoermann G; Mueller N; Sperr WR; Valent P
[Ad] Endereço:Department of Internal Medicine I, Division of Hematology & Hemostaseology, Medical University of Vienna, Vienna, Austria.
[Ti] Título:Expression of CD25 on leukemic stem cells in BCR-ABL1 CML: Potential diagnostic value and functional implications.
[So] Source:Exp Hematol;51:17-24, 2017 07.
[Is] ISSN:1873-2399
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Chronic myeloid leukemia (CML) is a stem cell-derived leukemia in which neoplastic cells exhibit the Philadelphia chromosome and the related oncoprotein BCR-ABL1. The disease is characterized by an accumulation of myeloid precursor cells in the peripheral blood and bone marrow (BM). A small fraction of neoplastic cells in the CML clone supposedly exhibits self-renewal and thus long-term disease-propagating ability. However, so far, little is known about the phenotype, function, and target expression profiles of these leukemic stem cells (LSCs). Recent data suggest that CML LSCs aberrantly express the interleukin-2 receptor alpha chain CD25. Whereas normal CD34 /CD38 BM stem cells display only low amounts of CD25 or lack CD25 altogether, CD34 /CD38 LSCs express CD25 strongly in more than 90% of all patients with untreated CML. As a result, CD25 can be used to identify and quantify CML LSCs. In addition, it has been shown that CD25 serves as a negative growth regulator of CML LSCs. Here, we review the value of CD25 as a novel marker and potential drug target in CML LSCs.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/biossíntese
Proteínas de Fusão bcr-abl/metabolismo
Regulação Leucêmica da Expressão Gênica
Subunidade alfa de Receptor de Interleucina-2/biossíntese
Leucemia Mielogênica Crônica BCR-ABL Positiva/diagnóstico
Leucemia Mielogênica Crônica BCR-ABL Positiva/metabolismo
Proteínas de Neoplasias/metabolismo
Células-Tronco Neoplásicas/metabolismo
[Mh] Termos MeSH secundário: ADP-Ribosil Ciclase 1/metabolismo
Antígenos CD34/metabolismo
Células da Medula Óssea/metabolismo
Seres Humanos
Glicoproteínas de Membrana/metabolismo
Células-Tronco Neoplásicas/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, CD34); 0 (BCR-ABL1 fusion protein, human); 0 (Biomarkers, Tumor); 0 (IL2RA protein, human); 0 (Interleukin-2 Receptor alpha Subunit); 0 (Membrane Glycoproteins); 0 (Neoplasm Proteins); EC 2.7.10.2 (Fusion Proteins, bcr-abl); EC 3.2.2.5 (CD38 protein, human); EC 3.2.2.6 (ADP-ribosyl Cyclase 1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180224
[Lr] Data última revisão:
180224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE


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[PMID]:29272356
[Au] Autor:Kim DS; Song L; Wang J; Wu H; Gu G; Sugi Y; Li Z; Wang H
[Ad] Endereço:Department of Surgery, Medical University of South Carolina, Charleston, South Carolina.
[Ti] Título:GRP94 Is an Essential Regulator of Pancreatic ß-Cell Development, Mass, and Function in Male Mice.
[So] Source:Endocrinology;159(2):1062-1073, 2018 02 01.
[Is] ISSN:1945-7170
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Deficiencies in pancreatic ß-cell mass contribute to both type 1 and type 2 diabetes. We investigated the role of the glucose-regulated protein (GRP) 94, an endoplasmic reticulum protein abundantly expressed in the pancreatic acini and islets, in ß-cell development, survival, and function. We used a conditional knockout (KO) mouse in which the GRP94 gene, Hsp90b1, was specifically deleted in pancreatic and duodenal homeobox 1 (Pdx1)-expressing cells. These Hsp90b1 flox/flox;Pdx1Cre KO mice exhibited pancreatic hypoplasia at embryonic day (E) 16.5 to E18.5 and had significantly reduced ß-cell mass at 4 weeks after birth. Further mechanistic studies showed that deletion of GRP94 reduced ß-cell proliferation with increased cell apoptosis in both Pdx1+ endocrine progenitor cells and differentiated ß cells. Although Hsp90b1 flox/flox;Pdx1Cre KO mice remained euglycemic at 8 weeks of age, they exhibited impaired glucose tolerance. In aggregate, these findings indicate that GRP94 is an essential regulator of pancreatic ß-cell development, mass, and function.
[Mh] Termos MeSH primário: Células Secretoras de Insulina/citologia
Células Secretoras de Insulina/fisiologia
Glicoproteínas de Membrana/fisiologia
Pâncreas/embriologia
[Mh] Termos MeSH secundário: Animais
Contagem de Células
Diferenciação Celular/genética
Proliferação Celular/genética
Células Cultivadas
Embrião não Mamífero
Intolerância à Glucose/genética
Intolerância à Glucose/metabolismo
Células HEK293
Seres Humanos
Masculino
Glicoproteínas de Membrana/genética
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Tamanho do Órgão/genética
Pâncreas/crescimento & desenvolvimento
Pâncreas/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Membrane Glycoproteins); 0 (endoplasmin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171223
[St] Status:MEDLINE
[do] DOI:10.1210/en.2017-00685


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[PMID]:29259037
[Au] Autor:Falch CM; Sundaram AYM; Øystese KA; Normann KR; Lekva T; Silamikelis I; Eieland AK; Andersen M; Bollerslev J; Olarescu NC
[Ad] Endereço:Section of Specialized EndocrinologyDepartment of Endocrinology cafal14@student.sdu.dk.
[Ti] Título:Gene expression profiling of fast- and slow-growing non-functioning gonadotroph pituitary adenomas.
[So] Source:Eur J Endocrinol;178(3):295-307, 2018 Mar.
[Is] ISSN:1479-683X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Reliable biomarkers associated with aggressiveness of non-functioning gonadotroph adenomas (GAs) are lacking. As the growth of tumor remnants is highly variable, molecular markers for growth potential prediction are necessary. We hypothesized that fast- and slow-growing GAs present different gene expression profiles and reliable biomarkers for tumor growth potential could be identified, focusing on the specific role of epithelial-mesenchymal transition (EMT). DESIGN AND METHODS: Eight GAs selected for RNA sequencing were equally divided into fast- and slow-growing group by the tumor volume doubling time (TVDT) median (27.75 months). Data were analyzed by tophat2, cufflinks and cummeRbund pipeline. 40 genes were selected for RT-qPCR validation in 20 GAs based on significance, fold-change and pathway analyses. The effect of silencing (metadherin) and (endomucin) on migration of human adenoma cells was evaluated. RESULTS: 350 genes were significantly differentially expressed (282 genes upregulated and 68 downregulated in the fast group, -adjusted <0.05). Among 40 selected genes, 11 showed associations with TVDT (-0.669< <-0.46, < 0.05). These were and six EMT-related genes ( and ). , but not , demonstrated involvement in cell migration and association with EMT markers. CONCLUSIONS: Fast- and slow-growing GAs present different gene expression profiles, and genes related to EMT have higher expression in fast-growing tumors. In addition to , identified as an important contributor to aggressiveness, the other genes might represent markers for tumor growth potential and possible targets for drug therapy.
[Mh] Termos MeSH primário: Adenoma/genética
Transição Epitelial-Mesenquimal/genética
Neoplasias Hipofisárias/genética
RNA Mensageiro/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/genética
Adenoma/metabolismo
Adulto
Idoso
Caderinas/genética
Moléculas de Adesão Celular/genética
Movimento Celular/genética
Subunidades Catalíticas da Proteína Quinase Dependente de AMP Cíclico/genética
Feminino
Hormônio Foliculoestimulante/metabolismo
Perfilação da Expressão Gênica
Regulação Neoplásica da Expressão Gênica
Inativação Gênica
Seres Humanos
Técnicas In Vitro
Peptídeos e Proteínas de Sinalização Intracelular/genética
Hormônio Luteinizante/metabolismo
Masculino
Glicoproteínas de Membrana/genética
Proteínas Associadas aos Microtúbulos/genética
Meia-Idade
Miosina Tipo I/genética
Proteínas do Tecido Nervoso/genética
Neoplasias Hipofisárias/metabolismo
Proteínas Proto-Oncogênicas/genética
Receptores de Superfície Celular/genética
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Ribonucleases/genética
Sialoglicoproteínas/genética
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Cadherins); 0 (Cell Adhesion Molecules); 0 (EMCN protein, human); 0 (GPM6A protein, human); 0 (Intracellular Signaling Peptides and Proteins); 0 (MTDH protein, human); 0 (MYO1B protein, human); 0 (Membrane Glycoproteins); 0 (Microtubule-Associated Proteins); 0 (Nerve Tissue Proteins); 0 (PCDH18 protein, human); 0 (Proto-Oncogene Proteins); 0 (RNA, Messenger); 0 (Receptors, Cell Surface); 0 (SKIL protein, human); 0 (SPAG9 protein, human); 0 (Sialoglycoproteins); 0 (UNC5H4 protein, human); 0 (hook1 protein, human); 9002-67-9 (Luteinizing Hormone); 9002-68-0 (Follicle Stimulating Hormone); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinase Catalytic Subunits); EC 2.7.11.11 (PRKACB protein, human); EC 3.1.- (CNOT6L protein, human); EC 3.1.- (Ribonucleases); EC 3.6.1.- (Myosin Type I)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171221
[St] Status:MEDLINE
[do] DOI:10.1530/EJE-17-0702


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[PMID]:29293625
[Au] Autor:Kell MJ; Riccio RE; Baumgartner EA; Compton ZJ; Pecorin PJ; Mitchell TA; Topczewski J; LeClair EE
[Ad] Endereço:Department of Pediatrics, Northwestern University Feinberg School of Medicine / Stanley Manne Children's Research Center, Chicago, Illinois, United States of America.
[Ti] Título:Targeted deletion of the zebrafish actin-bundling protein L-plastin (lcp1).
[So] Source:PLoS One;13(1):e0190353, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Regulation of the cytoskeleton is essential for cell migration in health and disease. Lymphocyte cytosolic protein 1 (lcp1, also called L-plastin) is a hematopoietic-specific actin-bundling protein that is highly conserved in zebrafish, mice and humans. In addition, L-plastin expression is documented as both a genetic marker and a cellular mechanism contributing to the invasiveness of tumors and transformed cell lines. Despite L-plastin's role in both immunity and cancer, in zebrafish there are no direct studies of its function, and no mutant, knockout or reporter lines available. Using CRISPR-Cas9 genome editing, we generated null alleles of zebrafish lcp1 and examined the phenotypes of these fish throughout the life cycle. Our editing strategy used gRNA to target the second exon of lcp1, producing F0 mosaic fish that were outcrossed to wild types to confirm germline transmission. F1 heterozygotes were then sequenced to identify three unique null alleles, here called 'Charlie', 'Foxtrot' and 'Lima'. In silico, each allele truncates the endogenous protein to less than 5% normal size and removes both essential actin-binding domains (ABD1 and ABD2). Although none of the null lines express detectable LCP1 protein, homozygous mutant zebrafish (-/-) can develop and reproduce normally, a finding consistent with that of the L-plastin null mouse (LPL -/-). However, such mice do have a profound immune defect when challenged by lung bacteria. Interestingly, we observed reduced long-term survival of zebrafish lcp1 -/- homozygotes (~30% below the expected numbers) in all three of our knockout lines, with greatest mortality corresponding to the period (4-6 weeks post-fertilization) when the innate immune system is functional, but the adaptive immune system is not yet mature. This suggests that null zebrafish may have reduced capacity to combat opportunistic infections, which are more easily transmissible in the aquatic environment. Overall, our novel mutant lines establish a sound genetic model and an enhanced platform for further studies of L-plastin gene function in hematopoiesis and cancer.
[Mh] Termos MeSH primário: Deleção de Genes
Glicoproteínas de Membrana/genética
Proteínas dos Microfilamentos/genética
Proteínas de Peixe-Zebra/genética
Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Alelos
Sequência de Aminoácidos
Animais
Clonagem Molecular
Repetições Palindrômicas Curtas Agrupadas e Regularmente Espaçadas
Seres Humanos
Camundongos
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Glycoproteins); 0 (Microfilament Proteins); 0 (Zebrafish Proteins); 0 (plastin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190353


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[PMID]:29266546
[Au] Autor:Zhao X; Pan Y; Ren W; Shen F; Xu M; Yu M; Fu J; Xia L; Ruan C; Zhao Y
[Ad] Endereço:Jiangsu Institute of Hematology, Key Laboratory of Thrombosis and Hemostasis of the Ministry of Health, The First Affiliated Hospital of Soochow University, Suzhou, China.
[Ti] Título:Plasma soluble podoplanin is a novel marker for the diagnosis of tumor occurrence and metastasis.
[So] Source:Cancer Sci;109(2):403-411, 2018 Feb.
[Is] ISSN:1349-7006
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Podoplanin (PDPN) is expressed on many tumors and is involved in tumor metastasis. The objective of the present study was to develop an ELISA for determining soluble PDPN (sPDPN) levels as a potential novel tumor marker in plasma of patients with cancers for detection of tumor occurrence and metastasis. Mouse monoclonal antibodies (mAb) against human PDPN were developed and characterized. Two anti-PDPN mAb, SZ-163 and SZ-168, were used in a sandwich ELISA to detect plasma sPDPN in patients with cancers and in normal individuals. The levels of sPDPN were detected in patients with adenocarcinoma (87 cases, 31.09 ± 5.48 ng/ml), squamous cell carcinoma (86 cases, 6.91 ± 0.59 ng/ml), lung cancer (45 cases, 26.10 ± 7.62 ng/ml), gastric cancer (38 cases, 23.71 ± 6.90 ng/ml) and rectal cancer (27 cases, 32.98 ± 9.88 ng/ml), which were significantly higher than those in normal individuals (99 cases, 1.31 ± 0.13 ng/ml) (P < .0001). Moreover, the sPDPN levels in patients with metastatic cancers were higher (192 cases, 30.35 ± 3.63 ng/ml) than those in non-metastatic cancer patients (92 cases, 6.28 ± 0.77 ng/ml) (P < .0001). The post-treatment sPDPN levels of cancer patients (n = 156) (4.47 ± 0.35 ng/ml) were significantly lower compared with those seen pre-treatment (n = 128) (43.74 ± 4.97 ng/ml) (P < .0001). These results showed that an ELISA method was successfully established for quantitation of plasma sPDPN and plasma sPDPN levels correlate significantly with tumor occurrence and metastasis.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/sangue
Glicoproteínas de Membrana/sangue
Neoplasias/diagnóstico
[Mh] Termos MeSH secundário: Animais
Anticorpos Monoclonais/metabolismo
Células CHO
Linhagem Celular Tumoral
Cricetulus
Regulação Neoplásica da Expressão Gênica
Masculino
Camundongos
Metástase Neoplásica
Neoplasias/sangue
Neoplasias/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Biomarkers, Tumor); 0 (Membrane Glycoproteins); 0 (PDPN protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171222
[St] Status:MEDLINE
[do] DOI:10.1111/cas.13475



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