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[PMID]:28460335
[Au] Autor:Feng Y; Li Q; Wu D; Niu Y; Yang C; Dong L; Wang C
[Ad] Endereço:State Key Laboratory of Quality Research in Chinese Medicine, Institute of Chinese Medical Sciences, University of Macau, Macau SAR, China.
[Ti] Título:A macrophage-activating, injectable hydrogel to sequester endogenous growth factors for in situ angiogenesis.
[So] Source:Biomaterials;134:128-142, 2017 Jul.
[Is] ISSN:1878-5905
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Biomaterials scaffolds designed for many regenerative applications are expected to support neo-vascularisation, which is now being hampered by two limitations - the instability of exogenous growth factors (GFs) that are delivered to promote angiogenesis; and the loss of extracellular matrix components that bind and stabilise GFs. Here, we report the design and evaluation of an injectable hydrogel system aimed at restoring a GF-binding microenvironment to enhance the pro-angiogenic functions of endogenous GFs. This gel comprises two polysaccharides with their unique bioactivities: Konjac glucomannan (KGM) as the building block of the gel scaffold, for its demonstrated capacity to activate macrophages/monocytes to secrete pro-angiogenic/-mitogenic GFs; and heparin (Hep), a representative glycosaminoglycan molecule that binds numerous pro-angiogenic GFs, as functional moieties to sequester the macrophage-produced GFs. Modified with tyramine (TA) groups, the two polysaccharides can be co-polymerised and rapidly form into hydrogel upon enzyme catalysis. The designed KGM-TA/Hep-TA hydrogel successfully preserves the macrophage-activating function and GF-binding affinity of the two components, respectively, and, once subcutaneously implanted, effectively sequestered the locally-produced GFs in situ and promote the formation and maturation of blood vessels in mice. In summary, the designed hydrogel system demonstrates a feasible approach to stimulate the production and harness the function of endogenous GFs for inducing blood vessel formation in vivo, without the addition of any exogenous proteins. This design may provide an innovative, open platform to promote vascularisation for various regenerative purposes.
[Mh] Termos MeSH primário: Materiais Biocompatíveis/química
Materiais Biocompatíveis/farmacologia
Hidrogel de Polietilenoglicol-Dimetacrilato/química
Hidrogel de Polietilenoglicol-Dimetacrilato/farmacologia
Peptídeos e Proteínas de Sinalização Intercelular/metabolismo
Macrófagos/metabolismo
[Mh] Termos MeSH secundário: Indutores da Angiogênese/química
Indutores da Angiogênese/farmacologia
Animais
Glicosaminoglicanos/metabolismo
Seres Humanos
Integrina beta1/metabolismo
Lectinas Tipo C/metabolismo
Masculino
Mananas/metabolismo
Lectinas de Ligação a Manose/metabolismo
Camundongos
Neovascularização Fisiológica/efeitos dos fármacos
Polissacarídeos/metabolismo
Células RAW 264.7
Receptores de Superfície Celular/metabolismo
Células THP-1
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Angiogenesis Inducing Agents); 0 (Biocompatible Materials); 0 (Glycosaminoglycans); 0 (Integrin beta1); 0 (Intercellular Signaling Peptides and Proteins); 0 (Lectins, C-Type); 0 (Mannans); 0 (Mannose-Binding Lectins); 0 (Polysaccharides); 0 (Receptors, Cell Surface); 0 (mannose receptor); 25852-47-5 (Hydrogel, Polyethylene Glycol Dimethacrylate); 36W3E5TAMG ((1-6)-alpha-glucomannan)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE


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[PMID]:29288363
[Au] Autor:Hamurcu Z; Delibasi N; Geçene S; Sener EF; Dönmez-Altuntas H; Özkul Y; Canatan H; Ozpolat B
[Ad] Endereço:Department of Medical Biology, Faculty of Medicine, Erciyes University, Kayseri, Turkey.
[Ti] Título:Targeting LC3 and Beclin-1 autophagy genes suppresses proliferation, survival, migration and invasion by inhibition of Cyclin-D1 and uPAR/Integrin ß1/ Src signaling in triple negative breast cancer cells.
[So] Source:J Cancer Res Clin Oncol;144(3):415-430, 2018 Mar.
[Is] ISSN:1432-1335
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Autophagy is a catabolic process for degrading dysfunctional proteins and organelles, and closely associated with cancer cell survival under therapeutic, metabolic stress, hypoxia, starvation and lack of growth factors, contributing to resistance to therapies. However, the role of autophagy in breast cancer cells is not well understood. In the present study, we investigated the role of autophagy in highly aggressive and metastatic triple negative breast cancer (TNBC) and non-metastatic breast cancer cells and demonstrated that the knockdown of autophagy-related genes (LC3 and Beclin-1) inhibited autophagy and significantly suppressed cell proliferation, colony formation, migration/invasion and induced apoptosis in MDA-MB-231 and BT-549 TNBC cells. Knockdown of LC3 and Beclin-1 led to inhibition of multiple proto-oncogenic signaling pathways, including cyclin D1, uPAR/integrin-ß1/Src, and PARP1. In conclusion, our study suggests that LC3 and Beclin-1 are required for cell proliferation, survival, migration and invasion, and may contribute to tumor growth and progression of highly aggressive and metastatic TNBC cells and therapeutic targeting of autophagy genes may be a potential therapeutic strategy for TNBC in breast cancer.
[Mh] Termos MeSH primário: Beclina-1/antagonistas & inibidores
Movimento Celular/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Proteínas Associadas aos Microtúbulos/antagonistas & inibidores
Terapia de Alvo Molecular/métodos
RNA Interferente Pequeno/farmacologia
Neoplasias de Mama Triplo Negativas/patologia
[Mh] Termos MeSH secundário: Autofagia/genética
Beclina-1/genética
Linhagem Celular Tumoral
Movimento Celular/genética
Proliferação Celular/genética
Sobrevivência Celular/efeitos dos fármacos
Sobrevivência Celular/genética
Ciclina D1/antagonistas & inibidores
Ciclina D1/metabolismo
Feminino
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Integrina beta1/metabolismo
Células MCF-7
Proteínas Associadas aos Microtúbulos/genética
Receptores de Ativador de Plasminogênio Tipo Uroquinase/antagonistas & inibidores
Receptores de Ativador de Plasminogênio Tipo Uroquinase/metabolismo
Transdução de Sinais/efeitos dos fármacos
Transdução de Sinais/genética
Neoplasias de Mama Triplo Negativas/genética
Quinases da Família src/antagonistas & inibidores
Quinases da Família src/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Beclin-1); 0 (CCND1 protein, human); 0 (Integrin beta1); 0 (Microtubule-Associated Proteins); 0 (RNA, Small Interfering); 0 (Receptors, Urokinase Plasminogen Activator); 0 (light chain 3, human); 136601-57-5 (Cyclin D1); EC 2.7.10.2 (src-Family Kinases)
[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:171231
[St] Status:MEDLINE
[do] DOI:10.1007/s00432-017-2557-5


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[PMID]:29335551
[Au] Autor:Fang T; Lv H; Lv G; Li T; Wang C; Han Q; Yu L; Su B; Guo L; Huang S; Cao D; Tang L; Tang S; Wu M; Yang W; Wang H
[Ad] Endereço:International Co-operation Laboratory on Signal Transduction, Eastern Hepatobiliary Surgery Institute, Second Military Medical University, Shanghai, 200438, China.
[Ti] Título:Tumor-derived exosomal miR-1247-3p induces cancer-associated fibroblast activation to foster lung metastasis of liver cancer.
[So] Source:Nat Commun;9(1):191, 2018 01 15.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The communication between tumor-derived elements and stroma in the metastatic niche has a critical role in facilitating cancer metastasis. Yet, the mechanisms tumor cells use to control metastatic niche formation are not fully understood. Here we report that in the lung metastatic niche, high-metastatic hepatocellular carcinoma (HCC) cells exhibit a greater capacity to convert normal fibroblasts to cancer-associated fibroblasts (CAFs) than low-metastatic HCC cells. We show high-metastatic HCC cells secrete exosomal miR-1247-3p that directly targets B4GALT3, leading to activation of ß1-integrin-NF-κB signaling in fibroblasts. Activated CAFs further promote cancer progression by secreting pro-inflammatory cytokines, including IL-6 and IL-8. Clinical data show high serum exosomal miR-1247-3p levels correlate with lung metastasis in HCC patients. These results demonstrate intercellular crosstalk between tumor cells and fibroblasts is mediated by tumor-derived exosomes that control lung metastasis of HCC, providing potential targets for prevention and treatment of cancer metastasis.
[Mh] Termos MeSH primário: Fibroblastos Associados a Câncer/metabolismo
Carcinoma Hepatocelular/metabolismo
Exossomos/metabolismo
Regulação Neoplásica da Expressão Gênica
Neoplasias Hepáticas/metabolismo
Neoplasias Pulmonares/metabolismo
MicroRNAs/genética
N-Acetil-Lactosamina Sintase/genética
[Mh] Termos MeSH secundário: Animais
Fibroblastos Associados a Câncer/patologia
Carcinoma Hepatocelular/genética
Carcinoma Hepatocelular/secundário
Comunicação Celular
Linhagem Celular Tumoral
Transformação Celular Neoplásica/genética
Transformação Celular Neoplásica/patologia
Exossomos/química
Seres Humanos
Integrina beta1/genética
Integrina beta1/metabolismo
Interleucina-6/genética
Interleucina-6/metabolismo
Interleucina-8/genética
Interleucina-8/metabolismo
Neoplasias Hepáticas/genética
Neoplasias Hepáticas/patologia
Neoplasias Pulmonares/genética
Neoplasias Pulmonares/secundário
Masculino
Camundongos
Camundongos Nus
MicroRNAs/secreção
N-Acetil-Lactosamina Sintase/metabolismo
Invasividade Neoplásica
Transplante de Neoplasias
Células Neoplásicas Circulantes/metabolismo
Células Neoplásicas Circulantes/patologia
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (IL6 protein, human); 0 (Integrin beta1); 0 (Interleukin-6); 0 (Interleukin-8); 0 (MIRN1247 microRNA, human); 0 (MicroRNAs); EC 2.4.1.90 (N-Acetyllactosamine Synthase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180117
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02583-0


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[PMID]:29203246
[Au] Autor:Popielarski M; Ponamarczuk H; Stasiak M; Michalec L; Bednarek R; Studzian M; Pulaski L; Swiatkowska M
[Ad] Endereço:Department of Cytobiology and Proteomics, Medical University of Lodz, 6/8 Mazowiecka St., 92-215 Lodz, Poland. Electronic address: marcin.popielarski@umed.lodz.pl.
[Ti] Título:The role of Protein Disulfide Isomerase and thiol bonds modifications in activation of integrin subunit alpha11.
[So] Source:Biochem Biophys Res Commun;495(2):1635-1641, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Integrins belong to a family of transmembrane receptors that mediate cell migration and adhesion to ECM. Extracellular domains of integrin heterodimers contain cysteine-rich regions, which are potential sites of thiol-disulfide exchanges. Rearrangements of extracellular disulfide bonds regulate activation of integrin receptors by promoting transition from an inactive state into a ligand-binding competent state. Modifications of integrin disulfide bonds dependent on oxidation-reduction can be mediated by Protein Disulfide Isomerse (PDI). This paper provides evidences that binding to integrin ligands initiate changes in free thiol pattern on cell surface and that thiol-disulfide exchange mediated by PDI leads to activation of integrin subunit α11. By employing co-immunoprecipitation and confocal microscopy analysis we showed that α11ß1 and PDI create complexes bounded by disulfide bonds. Using surface plasmon resonance we provide biochemical evidence that PDI can interact directly with integrin subunit α11.
[Mh] Termos MeSH primário: Cadeias alfa de Integrinas/química
Cadeias alfa de Integrinas/metabolismo
Isomerases de Dissulfetos de Proteínas/metabolismo
[Mh] Termos MeSH secundário: Adesão Celular
Movimento Celular
Células Cultivadas
Seres Humanos
Imunoprecipitação
Integrina beta1/química
Integrina beta1/metabolismo
Microscopia Confocal
Domínios e Motivos de Interação entre Proteínas
Compostos de Sulfidrila/química
Compostos de Sulfidrila/metabolismo
Ressonância de Plasmônio de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ITGA11 protein, human); 0 (Integrin alpha Chains); 0 (Integrin beta1); 0 (Sulfhydryl Compounds); EC 5.3.4.1 (Protein Disulfide-Isomerases)
[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:171206
[St] Status:MEDLINE


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[PMID]:29040328
[Au] Autor:Peuhu E; Salomaa SI; De Franceschi N; Potter CS; Sundberg JP; Pouwels J
[Ad] Endereço:Turku Centre for Biotechnology, University of Turku, Turku, Finland.
[Ti] Título:Integrin beta 1 inhibition alleviates the chronic hyperproliferative dermatitis phenotype of SHARPIN-deficient mice.
[So] Source:PLoS One;12(10):e0186628, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:SHARPIN (Shank-Associated RH Domain-Interacting Protein) is a component of the linear ubiquitin chain assembly complex (LUBAC), which enhances TNF-induced NF-κB activity. SHARPIN-deficient (Sharpincpdm/cpdm) mice display multi-organ inflammation and chronic proliferative dermatitis (cpdm) due to TNF-induced keratinocyte apoptosis. In cells, SHARPIN also inhibits integrins independently of LUBAC, but it has remained enigmatic whether elevated integrin activity levels in the dermis of Sharpincpdm/cpdm mice is due to increased integrin activity or is secondary to inflammation. In addition, the functional contribution of increased integrin activation to the Sharpincpdm/cpdm phenotype has not been investigated. Here, we find increased integrin activity in keratinocytes from Tnfr1-/- Sharpincpdm/cpdm double knockout mice, which do not display chronic inflammation or proliferative dermatitis, thus suggesting that SHARPIN indeed acts as an integrin inhibitor in vivo. In addition, we present evidence for a functional contribution of integrin activity to the Sharpincpdm/cpdm skin phenotype. Treatment with an integrin beta 1 function blocking antibody reduced epidermal hyperproliferation and epidermal thickness in Sharpincpdm/cpdm mice. Our data indicate that, while TNF-induced cell death triggers the chronic inflammation and proliferative dermatitis, absence of SHARPIN-dependent integrin inhibition exacerbates the epidermal hyperproliferation in Sharpincpdm/cpdm mice.
[Mh] Termos MeSH primário: Proteínas de Transporte/genética
Dermatite/tratamento farmacológico
Epiderme/efeitos dos fármacos
Integrina beta1/genética
Queratinócitos/efeitos dos fármacos
Receptores Tipo I de Fatores de Necrose Tumoral/genética
[Mh] Termos MeSH secundário: Animais
Anticorpos Neutralizantes/farmacologia
Apoptose
Proteínas de Transporte/imunologia
Proliferação Celular
Doença Crônica
Dermatite/genética
Dermatite/imunologia
Dermatite/patologia
Epiderme/imunologia
Epiderme/patologia
Feminino
Deleção de Genes
Regulação da Expressão Gênica
Inflamação
Integrina beta1/imunologia
Queratinócitos/imunologia
Queratinócitos/patologia
Masculino
Camundongos
Camundongos Knockout
NF-kappa B/genética
NF-kappa B/imunologia
Fenótipo
Receptores Tipo I de Fatores de Necrose Tumoral/deficiência
Receptores Tipo I de Fatores de Necrose Tumoral/imunologia
Transdução de Sinais
Ubiquitina/genética
Ubiquitina/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Carrier Proteins); 0 (Integrin beta1); 0 (NF-kappa B); 0 (Receptors, Tumor Necrosis Factor, Type I); 0 (Sipl1 protein, mouse); 0 (Tnfrsf1a protein, mouse); 0 (Ubiquitin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171018
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186628


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[PMID]:29016654
[Au] Autor:Jasinska-Konior K; Pochylczuk K; Czajka E; Michalik M; Romanowska-Dixon B; Swakon J; Urbanska K; Elas M
[Ad] Endereço:Department of Biophysics, Faculty of Biochemistry, Biophysics and Biotechnology, Cracow, Poland.
[Ti] Título:Proton beam irradiation inhibits the migration of melanoma cells.
[So] Source:PLoS One;12(10):e0186002, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE: In recent years experimental data have indicated that low-energy proton beam radiation might induce a difference in cellular migration in comparison to photons. We therefore set out to compare the effect of proton beam irradiation and X-rays on the survival and long-term migratory properties of two cell lines: uveal melanoma Mel270 and skin melanoma BLM. MATERIALS AND METHODS: Cells treated with either proton beam or X-rays were analyzed for their survival using clonogenic assay and MTT test. Long-term migratory properties were assessed with time-lapse monitoring of individual cell movements, wound test and transpore migration, while the expression of the related proteins was measured with western blot. RESULTS: Exposure to proton beam and X-rays led to similar survival but the quality of the cell colonies was markedly different. More paraclones with a low proliferative activity and fewer highly-proliferative holoclones were found after proton beam irradiation in comparison to X-rays. At 20 or 40 days post-irradiation, migratory capacity was decreased more by proton beam than by X-rays. The beta-1-integrin level was decreased in Mel270 cells after both types of radiation, while vimentin, a marker of EMT, was increased in BLM cells only. CONCLUSIONS: We conclude that proton beam irradiation induced long-term inhibition of cellular motility, as well as changes in the level of beta-1 integrin and vimentin. If confirmed, the change in the quality, but not in the number of colonies after proton beam irradiation might favor tumor growth inhibition after fractionated proton therapy.
[Mh] Termos MeSH primário: Movimento Celular/efeitos da radiação
Integrina beta1/genética
Melanócitos/efeitos da radiação
Prótons/uso terapêutico
Vimentina/genética
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Sobrevivência Celular/efeitos da radiação
Células Clonais
Expressão Gênica/efeitos da radiação
Seres Humanos
Integrina beta1/metabolismo
Melanócitos/metabolismo
Melanócitos/patologia
Especificidade de Órgãos
Imagem com Lapso de Tempo
Vimentina/metabolismo
Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Integrin beta1); 0 (Protons); 0 (Vimentin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171011
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186002


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[PMID]:28882889
[Au] Autor:Rohrbeck A; Höltje M; Adolf A; Oms E; Hagemann S; Ahnert-Hilger G; Just I
[Ad] Endereço:From the Institute of Toxicology, Hannover Medical School, Carl-Neuberg-Strasse 1, D-30625 Hannover and rohrbeck.astrid@mh-hannover.de.
[Ti] Título:The Rho ADP-ribosylating C3 exoenzyme binds cells via an Arg-Gly-Asp motif.
[So] Source:J Biol Chem;292(43):17668-17680, 2017 Oct 27.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Rho ADP-ribosylating C3 exoenzyme (C3bot) is a bacterial protein toxin devoid of a cell-binding or -translocation domain. Nevertheless, C3 can efficiently enter intact cells, including neurons, but the mechanism of C3 binding and uptake is not yet understood. Previously, we identified the intermediate filament vimentin as an extracellular membranous interaction partner of C3. However, uptake of C3 into cells still occurs (although reduced) in the absence of vimentin, indicating involvement of an additional host cell receptor. C3 harbors an Arg-Gly-Asp (RGD) motif, which is the major integrin-binding site, present in a variety of integrin ligands. To check whether the RGD motif of C3 is involved in binding to cells, we performed a competition assay with C3 and RGD peptide or with a monoclonal antibody binding to ß1-integrin subunit and binding assays in different cell lines, primary neurons, and synaptosomes with C3-RGD mutants. Here, we report that preincubation of cells with the GRGDNP peptide strongly reduced C3 binding to cells. Moreover, mutation of the RGD motif reduced C3 binding to intact cells and also to recombinant vimentin. Anti-integrin antibodies also lowered the C3 binding to cells. Our results indicate that the RGD motif of C3 is at least one essential C3 motif for binding to host cells and that integrin is an additional receptor for C3 besides vimentin.
[Mh] Termos MeSH primário: ADP Ribose Transferases
Toxinas Botulínicas
Integrina beta1
Neurônios/metabolismo
Oligopeptídeos
Sinaptossomos/metabolismo
[Mh] Termos MeSH secundário: ADP Ribose Transferases/química
ADP Ribose Transferases/farmacocinética
ADP Ribose Transferases/farmacologia
Motivos de Aminoácidos
Animais
Toxinas Botulínicas/química
Toxinas Botulínicas/farmacocinética
Toxinas Botulínicas/farmacologia
Linhagem Celular
Integrina beta1/química
Integrina beta1/genética
Integrina beta1/metabolismo
Camundongos
Vimentina/química
Vimentina/genética
Vimentina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Integrin beta1); 0 (Oligopeptides); 0 (Vimentin); 78VO7F77PN (arginyl-glycyl-aspartic acid); EC 2.4.2.- (ADP Ribose Transferases); EC 2.4.2.- (exoenzyme C3, Clostridium botulinum); EC 3.4.24.69 (Botulinum Toxins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170909
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.798231


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[PMID]:28778796
[Au] Autor:Wieczorek K; Wiktorska M; Sacewicz-Hofman I; Boncela J; Lewinski A; Kowalska MA; Niewiarowska J
[Ad] Endereço:Department of Molecular Cell Mechanisms, Medical University of Lodz, Lodz, Poland; Department of Endocrinology and Metabolic Diseases, Medical University of Lodz, Lodz, Poland.
[Ti] Título:Filamin A upregulation correlates with Snail-induced epithelial to mesenchymal transition (EMT) and cell adhesion but its inhibition increases the migration of colon adenocarcinoma HT29 cells.
[So] Source:Exp Cell Res;359(1):163-170, 2017 Oct 01.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Filamin A (FLNA) is actin filament cross-linking protein involved in cancer progression. Its importance in regulating cell motility is directly related to the epithelial to mesenchymal transition (EMT) of tumor cells. However, little is known about the mechanism of action of FLNA at this early stage of cancer invasion. Using immunochemical methods, we evaluated the levels and localization of FLNA, pFLNA[Ser2152], ß1 integrin, pß1 integrin[Thr788/9], FAK, pFAK[Y379], and talin in stably transfected HT29 adenocarcinoma cells overexpressing Snail and looked for the effect of Snail in adhesion and migration assays on fibronectin-coated surfaces before and after FLNA silencing. Our findings indicate that FLNA upregulation correlates with Snail-induced EMT in colorectal carcinoma. FLNA localizes in the cytoplasm and at the sites of focal adhesion (FA) of invasive cells. Silencing of FLNA inhibits Snail-induced cell adhesion, reduces the size of FA sites, induces the relocalization of talin from the cytoplasm to the membrane area and augments cell migratory properties. Our findings suggest that FLNA may not act as a classic integrin inhibitor in invasive carcinoma cells, but is involved in other pro-invasive pathways. FLNA upregulation, which correlates with cell metastatic properties, maybe an additional target for combination therapy in colorectal carcinoma tumor progression.
[Mh] Termos MeSH primário: Adenocarcinoma/patologia
Movimento Celular
Neoplasias do Colo/patologia
Transição Epitelial-Mesenquimal
Filaminas/metabolismo
Fatores de Transcrição da Família Snail/metabolismo
Regulação para Cima
[Mh] Termos MeSH secundário: Adenocarcinoma/metabolismo
Adesão Celular
Células Clonais
Neoplasias do Colo/metabolismo
Proteína-Tirosina Quinases de Adesão Focal/metabolismo
Adesões Focais
Inativação Gênica
Células HT29
Seres Humanos
Integrina beta1/metabolismo
Invasividade Neoplásica
Fosforilação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Filamins); 0 (Integrin beta1); 0 (Snail Family Transcription Factors); EC 2.7.10.2 (Focal Adhesion Protein-Tyrosine Kinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170806
[St] Status:MEDLINE


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[PMID]:28763805
[Au] Autor:Wang Y; Terrell AM; Riggio BA; Anand D; Lachke SA; Duncan MK
[Ad] Endereço:Department of Biological Sciences, University of Delaware, Newark, Delaware, United States.
[Ti] Título:ß1-Integrin Deletion From the Lens Activates Cellular Stress Responses Leading to Apoptosis and Fibrosis.
[So] Source:Invest Ophthalmol Vis Sci;58(10):3896-3922, 2017 Aug 01.
[Is] ISSN:1552-5783
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Purpose: Previous research showed that the absence of ß1-integrin from the mouse lens after embryonic day (E) 13.5 (ß1MLR10) leads to the perinatal apoptosis of lens epithelial cells (LECs) resulting in severe microphthalmia. This study focuses on elucidating the molecular connections between ß1-integrin deletion and this phenotype. Methods: RNA sequencing was performed to identify differentially regulated genes (DRGs) in ß1MLR10 lenses at E15.5. By using bioinformatics analysis and literature searching, Egr1 (early growth response 1) was selected for further study. The activation status of certain signaling pathways (focal adhesion kinase [FAK]/Erk, TGF-ß, and Akt signaling) was studied via Western blot and immunohistochemistry. Mice lacking both ß1-integrin and Egr1 genes from the lenses were created (ß1MLR10/Egr1-/-) to study their relationship. Results: RNA sequencing identified 120 DRGs that include candidates involved in the cellular stress response, fibrosis, and/or apoptosis. Egr1 was investigated in detail, as it mediates cellular stress responses in various cell types, and is recognized as an upstream regulator of numerous other ß1MLR10 lens DRGs. In ß1MLR10 mice, Egr1 levels are elevated shortly after ß1-integrin loss from the lens. Further, pErk1/2 and pAkt are elevated in ß1MLR10 LECs, thus providing the potential signaling mechanism that causes Egr1 upregulation in the mutant. Indeed, deletion of Egr1 from ß1MLR10 lenses partially rescues the microphthalmia phenotype. Conclusions: ß1-integrin regulates the appropriate levels of Erk1/2 and Akt phosphorylation in LECs, whereas its deficiency results in the overexpression of Egr1, culminating in reduced cell survival. These findings provide insight into the molecular mechanism underlying the microphthalmia observed in ß1MLR10 mice.
[Mh] Termos MeSH primário: Apoptose/fisiologia
Integrina beta1/fisiologia
Cristalino/metabolismo
Cristalino/patologia
Transdução de Sinais/fisiologia
[Mh] Termos MeSH secundário: Animais
Western Blotting
Modelos Animais de Doenças
Proteínas do Olho/metabolismo
Fibrose
Imuno-Histoquímica
Camundongos
Camundongos Transgênicos
Análise de Sequência de RNA
Estresse Fisiológico/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Eye Proteins); 0 (Integrin beta1)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170802
[St] Status:MEDLINE
[do] DOI:10.1167/iovs.17-21721


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[PMID]:28760342
[Au] Autor:Shin HC; Park JY; Lim HD; Namgung U
[Ad] Endereço:Department of Oriental Medicine, Daejeon University, Daejeon 34520, Republic of Korea. Electronic address: hcshin2507@naver.com.
[Ti] Título:Induction of α6 and ß1 integrins by acupuncture stimulation in rats.
[So] Source:Biochem Biophys Res Commun;491(3):629-635, 2017 Sep 23.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acupuncture therapy is performed by applying the needle insertion at discrete cutaneous locations and used for the treatments of diverse symptoms and disorders. In order to elucidate mechanistic basis on how acupuncture stimulation (AS) produces therapeutic effects, it is primarily important to understand tissue responses locally at the acupuncture site (acupoint). Here, we investigated integrin protein as molecular target responding to and integrating AS. Signals of α6 and ß1 integrins were clearly induced at zusanli acupoint 24 h after AS in areas of nuclear clusters around the needle track. Induction levels of integrin were largely reduced by needle insertion at non-acupuncture point or without needle rotation. Phospho-Erk1/2 was initially decreased below the basal level after AS but increased 24 h later. Induction pattern of phospho-Erk1/2 was as similar as that of α6 integrin in its selectivity to needling procedure and tissue distribution. We further found that mRNA expression of P2X3 purinergic receptor was upregulated in the dorsal root ganglion (DRG) after AS, but decreased by the inhibition of Erk1/2 activity at the acupuncture area. Moreover, AS-mediated integrin activation was required for Erk1/2 activation at the acupuncture site and regulation of pain sensitivity in the hind paw. The present results provide a new evidence on acupuncture-specific tissue response in terms of integrin induction, and further suggest that integrin activation may be involved in transmitting mechanosensory signals from the acupoint to afferent nerve fiber.
[Mh] Termos MeSH primário: Terapia por Acupuntura/métodos
Integrina alfa6/imunologia
Integrina beta1/imunologia
Sistema de Sinalização das MAP Quinases/imunologia
Neuralgia/imunologia
Neuralgia/terapia
[Mh] Termos MeSH secundário: Pontos de Acupuntura
Animais
Masculino
Mecanotransdução Celular/imunologia
Neuralgia/diagnóstico
Estimulação Física/métodos
Ratos
Ratos Sprague-Dawley
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Integrin alpha6); 0 (Integrin beta1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170802
[St] Status:MEDLINE



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