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[PMID]:28348485
[Au] Autor:Hou XF; Xu LP; Song HY; Li S; Wu C; Wang JF
[Ad] Endereço:Xin-Fang Hou, Shuai Li, Chen Wu, Ju-Feng Wang, Department of Medical Oncology, Affiliated Cancer Hospital of Zhengzhou University, Henan Cancer Hospital, Zhengzhou 450008, Henan Province, China.
[Ti] Título: enhances the anti-cancer effects of cisplatin in cisplatin-resistant esophageal cancer cells upregulation of and downregulation of .
[So] Source:World J Gastroenterol;23(10):1796-1803, 2017 Mar 14.
[Is] ISSN:2219-2840
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:AIM: To explore the anti-tumor effects of esophageal cancer-related gene 2 (ECRG2) in combination with cisplatin (DDP) in DDP-resistant esophageal cancer cells (EC9706/DDP). METHODS: A drug-resistant cell model was established, with EC9706/DDP cells being treated with ECRG2 and/or DDP. Cell viability was examined by MTT assay. The rate of cell apoptosis was determined by flow cytometry. The mRNA expression levels of proliferating cell nuclear antigen (PCNA), metallothionein (MT), and p53 were determined by RT-PCR and PCNA, while MT and p53 protein expression levels were determined by western blotting. RESULTS: The anti-proliferative effect of ECRG2 in combination with DDP was superior when compared to ECRG2 or DDP alone. The inhibition rate for the combination reached its peak (51.33%) at 96 h. The early apoptotic rates of the control, ECRG2 alone, DDP alone, and ECRG2 plus DDP groups were 5.71% ± 0.27%, 12.68% ± 0.61%, 14.15% ± 0.87%, and 27.96% ± 0.36%, respectively. Although all treatment groups were significantly different from the control group ( < 0.05), the combination treatment of ECRG2 plus DDP performed significantly better when compared to either ECRG2 or DDP alone ( < 0.05). The combination of ECRG2 and DDP significantly upregulated p53 mRNA and protein levels and downregulated PCNA mRNA and protein levels compared to ECRG2 or DDP alone ( < 0.05). However, no changes were seen in the expression of MT mRNA or protein. CONCLUSION: in combination with DDP can inhibit viability and induce apoptosis in esophageal cancer DDP-resistant cells, possibly upregulation of expression and downregulation of expression. These findings suggest that the combination of ECRG2 and DDP may be a promising strategy for the clinical treatment of esophageal cancers that are resistant to DDP.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Cisplatino/farmacologia
Resistência a Medicamentos Antineoplásicos/efeitos dos fármacos
Neoplasias Esofágicas/tratamento farmacológico
Antígeno Nuclear de Célula em Proliferação/metabolismo
Proteínas Secretadas Inibidoras de Proteinases/uso terapêutico
Proteína Supressora de Tumor p53/metabolismo
[Mh] Termos MeSH secundário: Antineoplásicos/uso terapêutico
Apoptose/efeitos dos fármacos
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Cisplatino/uso terapêutico
Regulação para Baixo
Quimioterapia Combinada
Neoplasias Esofágicas/fisiopatologia
Citometria de Fluxo
Seres Humanos
Metalotioneína/metabolismo
Proteínas Secretadas Inibidoras de Proteinases/farmacologia
RNA Mensageiro/metabolismo
Proteínas Recombinantes/farmacologia
Proteínas Recombinantes/uso terapêutico
Inibidores de Serinopeptidase do Tipo Kazal
Ativação Transcricional
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Proliferating Cell Nuclear Antigen); 0 (Proteinase Inhibitory Proteins, Secretory); 0 (RNA, Messenger); 0 (Recombinant Proteins); 0 (SPINK7 protein, human); 0 (Serine Peptidase Inhibitors, Kazal Type); 0 (TP53 protein, human); 0 (Tumor Suppressor Protein p53); 9038-94-2 (Metallothionein); Q20Q21Q62J (Cisplatin)
[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:170329
[St] Status:MEDLINE
[do] DOI:10.3748/wjg.v23.i10.1796


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[PMID]:27671677
[Au] Autor:Zheng LS; Yang JP; Cao Y; Peng LX; Sun R; Xie P; Wang MY; Meng DF; Luo DH; Zou X; Chen MY; Mai HQ; Guo L; Guo X; Shao JY; Huang BJ; Zhang W; Qian CN
[Ad] Endereço:State Key Laboratory of Oncology in South China and Collaborative Innovation Center for Cancer Medicine, Sun Yat-Sen University Cancer Center, Guangzhou, China.
[Ti] Título:SPINK6 Promotes Metastasis of Nasopharyngeal Carcinoma via Binding and Activation of Epithelial Growth Factor Receptor.
[So] Source:Cancer Res;77(2):579-589, 2017 Jan 15.
[Is] ISSN:1538-7445
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nasopharyngeal carcinoma has the highest rate of metastasis among head and neck cancers, and distant metastasis is the major reason for treatment failure. The underlying molecular mechanisms of nasopharyngeal carcinoma metastasis are not fully understood. Here, we report the identification of serine protease inhibitor Kazal-type 6 (SPINK6) as a functional regulator of nasopharyngeal carcinoma metastasis via EGFR signaling. SPINK6 mRNA was upregulated in tumor and highly metastatic nasopharyngeal carcinoma cells. Immunohistochemical staining of 534 nasopharyngeal carcinomas revealed elevated SPINK6 expression as an independent unfavorable prognostic factor for overall, disease-free, and distant metastasis-free survival. Ectopic SPINK6 expression promoted in vitro migration and invasion as well as in vivo lymph node metastasis and liver metastasis of nasopharyngeal carcinoma cells, whereas silencing SPINK6 exhibited opposing effects. SPINK6 enhanced epithelial-mesenchymal transition by activating EGFR and the downstream AKT pathway. Inhibition of EGFR with a neutralizing antibody or erlotinib reversed SPINK6-induced nasopharyngeal carcinoma cell migration and invasion. Erlotinib also inhibited SPINK6-induced metastasis in vivo Notably, SPINK6 bound to the EGFR extracellular domain independent of serine protease-inhibitory activity. Overall, our results identified a novel EGFR-activating mechanism in which SPINK6 has a critical role in promoting nasopharyngeal carcinoma metastasis, with possible implications as a prognostic indicator in nasopharyngeal carcinoma patients. Cancer Res; 77(2); 579-89. ©2016 AACR.
[Mh] Termos MeSH primário: Carcinoma/patologia
Neoplasias Nasofaríngeas/patologia
Proteínas Secretadas Inibidoras de Proteinases/metabolismo
Receptor do Fator de Crescimento Epidérmico/metabolismo
[Mh] Termos MeSH secundário: Carcinoma/metabolismo
Carcinoma/mortalidade
Movimento Celular/fisiologia
Intervalo Livre de Doença
Transição Epitelial-Mesenquimal/fisiologia
Feminino
Xenoenxertos
Seres Humanos
Immunoblotting
Imuno-Histoquímica
Imunoprecipitação
Estimativa de Kaplan-Meier
Metástase Linfática/patologia
Masculino
Neoplasias Nasofaríngeas/metabolismo
Neoplasias Nasofaríngeas/mortalidade
Invasividade Neoplásica/patologia
Prognóstico
Modelos de Riscos Proporcionais
Inibidores de Serinopeptidase do Tipo Kazal
Análise Serial de Tecidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteinase Inhibitory Proteins, Secretory); 0 (SPINK6 protein, human); 0 (Serine Peptidase Inhibitors, Kazal Type); EC 2.7.10.1 (EGFR protein, human); EC 2.7.10.1 (Receptor, Epidermal Growth Factor)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160928
[St] Status:MEDLINE
[do] DOI:10.1158/0008-5472.CAN-16-1281


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[PMID]:27354280
[Au] Autor:Plaza K; Kalinska M; Bochenska O; Meyer-Hoffert U; Wu Z; Fischer J; Falkowski K; Sasiadek L; Bielecka E; Potempa B; Kozik A; Potempa J; Kantyka T
[Ad] Endereço:From the Departments of Microbiology and.
[Ti] Título:Gingipains of Porphyromonas gingivalis Affect the Stability and Function of Serine Protease Inhibitor of Kazal-type 6 (SPINK6), a Tissue Inhibitor of Human Kallikreins.
[So] Source:J Biol Chem;291(36):18753-64, 2016 09 02.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Periodontitis, a chronic inflammation driven by dysbiotic subgingival bacterial flora, is linked on clinical levels to the development of a number of systemic diseases and to the development of oral and gastric tract tumors. A key pathogen, Porphyromonas gingivalis, secretes gingipains, cysteine proteases implicated as the main factors in the development of periodontitis. Here we hypothesize that gingipains may be linked to systemic pathologies through the deregulation of kallikrein-like proteinase (KLK) family members. KLKs are implicated in cancer development and are clinically utilized as tumor progression markers. In tissues, KLK activity is strictly controlled by a limited number of tissue-specific inhibitors, including SPINK6, an inhibitor of these proteases in skin and oral epithelium. Here we identify gingipains as the only P. gingivalis proteases responsible for SPINK6 degradation. We further show that gingipains, even at low nanomolar concentrations, cleaved SPINK6 in concentration- and time-dependent manner. The proteolysis was accompanied by loss of inhibition against KLK13. We also mapped the cleavage by Arg-specific gingipains to the reactive site loop of the SPINK6 inhibitor. Moreover, we identified a significant fraction of SPINK6-sensitive proteases in healthy saliva and confirmed the ability of gingipains to inactivate SPINK6 under ex vivo conditions. Finally, we demonstrate the double-edge action of gingipains, which, in addition, can activate KLKs because of gingipain K-mediated proteolytic processing of the zymogenic proform of KLK13. Altogether, the results indicate the potential of P. gingivalis to disrupt the control system of KLKs, providing a possible mechanistic link between periodontal disease and tumor development.
[Mh] Termos MeSH primário: Adesinas Bacterianas/metabolismo
Cisteína Endopeptidases/metabolismo
Porphyromonas gingivalis/enzimologia
Proteínas Secretadas Inibidoras de Proteinases/metabolismo
Saliva/metabolismo
Proteínas e Peptídeos Salivares/metabolismo
[Mh] Termos MeSH secundário: Adesinas Bacterianas/química
Cisteína Endopeptidases/química
Seres Humanos
Calicreínas/antagonistas & inibidores
Calicreínas/química
Calicreínas/metabolismo
Estabilidade Proteica
Proteínas Secretadas Inibidoras de Proteinases/química
Saliva/química
Proteínas e Peptídeos Salivares/antagonistas & inibidores
Proteínas e Peptídeos Salivares/química
Inibidores de Serinopeptidase do Tipo Kazal
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Proteinase Inhibitory Proteins, Secretory); 0 (SPINK6 protein, human); 0 (Salivary Proteins and Peptides); 0 (Serine Peptidase Inhibitors, Kazal Type); EC 3.4.21.- (KLK13 protein, human); EC 3.4.21.- (Kallikreins); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.37 (argingipain, Porphyromonas gingivalis)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171124
[Lr] Data última revisão:
171124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160630
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.722942


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[PMID]:26828269
[Au] Autor:Jung S; Fischer J; Spudy B; Kerkow T; Sönnichsen FD; Xue L; Bonvin AM; Goettig P; Magdolen V; Meyer-Hoffert U; Grötzinger J
[Ad] Endereço:Institute of Biochemistry, Christian-Albrechts-University, Olshausenstr. 40, 24098 Kiel, Germany.
[Ti] Título:The solution structure of the kallikrein-related peptidases inhibitor SPINK6.
[So] Source:Biochem Biophys Res Commun;471(1):103-8, 2016 Feb 26.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Kallikrein-related peptidases (KLKs) are crucial for epidermal barrier function and are involved in the proteolytic regulation of the desquamation process. Elevated KLK levels were reported in atopic dermatitis. In skin, the proteolytic activity of KLKs is regulated by specific inhibitors of the serine protease inhibitor of Kazal-type (SPINK) family. SPINK6 was shown to be expressed in human stratum corneum and is able to inhibit several KLKs such as KLK4, -5, -12, -13 and -14. In order to understand the structural traits of the specific inhibition we solved the structure of SPINK6 in solution by NMR-spectroscopy and studied its interaction with KLKs. Thereby, beside the conserved binding mode, we identified an alternate binding mode which has so far not been observed for SPINK inhibitors.
[Mh] Termos MeSH primário: Modelos Químicos
Modelos Moleculares
Proteínas Secretadas Inibidoras de Proteinases/química
Proteínas Secretadas Inibidoras de Proteinases/ultraestrutura
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
Simulação por Computador
Ativação Enzimática
Seres Humanos
Espectroscopia de Ressonância Magnética/métodos
Dados de Sequência Molecular
Ligação Proteica
Conformação Proteica
Análise de Sequência de Proteína/métodos
Inibidores de Serinopeptidase do Tipo Kazal
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Proteinase Inhibitory Proteins, Secretory); 0 (SPINK6 protein, human); 0 (Serine Peptidase Inhibitors, Kazal Type)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160202
[St] Status:MEDLINE


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[PMID]:26746658
[Au] Autor:Redelfs L; Fischer J; Weber C; Wu Z; Meyer-Hoffert U
[Ad] Endereço:Department of Dermatology, University Clinic Schleswig-Holstein, Campus Kiel, Kiel, Germany.
[Ti] Título:The serine protease inhibitor of Kazal-type 9 (SPINK9) is expressed in lichen simplex chronicus, actinic keratosis and squamous cell carcinoma.
[So] Source:Arch Dermatol Res;308(2):133-7, 2016 Mar.
[Is] ISSN:1432-069X
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The serine protease inhibitor of Kazal-type (SPINK) 9 was reported to be exclusively expressed in palmoplantar skin. SPINK9 is a specific inhibitor of the serine protease kallikrein-related peptidase 5 (KLK5), which contributes to the desquamation process of the stratum corneum. Herein, we demonstrated that SPINK9 is also expressed in lichen simplex chronicus. Moreover, we observed expression of SPINK9 in 51 % of lesions of actinic keratosis and squamous cell carcinoma. In conclusion, we demonstrate that SPINK9 is not only expressed in healthy palmoplantar skin, but also in dermatologic disorders like lichen simplex chronicus, actinic keratosis and squamous cell carcinoma.
[Mh] Termos MeSH primário: Carcinoma de Células Escamosas/patologia
Epiderme/metabolismo
Ceratose Actínica/patologia
Neurodermatite/patologia
Proteínas Secretadas Inibidoras de Proteinases/metabolismo
[Mh] Termos MeSH secundário: Células Cultivadas
Seres Humanos
Calicreínas/antagonistas & inibidores
Inibidores de Serinopeptidase do Tipo Kazal
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Proteinase Inhibitory Proteins, Secretory); 0 (Serine Peptidase Inhibitors, Kazal Type); 0 (Spink9 protein, human); EC 3.4.21.- (KLK5 protein, human); EC 3.4.21.- (Kallikreins)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160110
[St] Status:MEDLINE
[do] DOI:10.1007/s00403-015-1616-5


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[PMID]:26434587
[Au] Autor:Lucchesi C; Sheikh MS; Huang Y
[Ad] Endereço:Department of Pharmacology, State University of New York, Upstate Medical University, Syracuse, NY, USA.
[Ti] Título:Negative regulation of RNA-binding protein HuR by tumor-suppressor ECRG2.
[So] Source:Oncogene;35(20):2565-73, 2016 May 19.
[Is] ISSN:1476-5594
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Esophageal cancer-related gene 2 (ECRG2) is a newer tumor suppressor whose function in the regulation of cell growth and apoptosis remains to be elucidated. Here we show that ECRG2 expression was upregulated in response to DNA damage, and increased ECRG2 expression induced growth suppression in cancer cells but not in non-cancerous epithelial cells. ECRG2-mediated growth suppression was associated with activation of caspases and marked reduction in the levels of apoptosis inhibitor, X chromosome-linked inhibitor of apoptosis protein (XIAP). ECRG2, via RNA-binding protein human antigen R (HuR), regulated XIAP mRNA stability and expression. Furthermore, ECRG2 increased HuR ubiquitination and degradation but was unable to modulate the non-ubiquitinable mutant form of HuR. We also identified missense and frame-shift ECRG2 mutations in various human malignancies and noted that, unlike wild-type ECRG2, one cancer-derived ECRG2 mutant harboring glutamic acid instead of valine at position 30 (V30E) failed to induce cell death and activation of caspases. This naturally occurring V30E mutant also did not suppress XIAP and HuR. Importantly, the V30E mutant overexpressing cancer cells acquired resistance against multiple anticancer drugs, thus suggesting that ECRG2 mutations appear to have an important role in the acquisition of anticancer drug resistance in a subset of human malignancies.
[Mh] Termos MeSH primário: Proteína Semelhante a ELAV 1/metabolismo
Proteínas Secretadas Inibidoras de Proteinases/metabolismo
[Mh] Termos MeSH secundário: Apoptose
Linhagem Celular Tumoral
Dano ao DNA
Resistência a Medicamentos Antineoplásicos/genética
Seres Humanos
Mutação
Proteínas Secretadas Inibidoras de Proteinases/genética
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Inibidores de Serinopeptidase do Tipo Kazal
Ubiquitinação
Proteínas Inibidoras de Apoptose Ligadas ao Cromossomo X/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ELAV-Like Protein 1); 0 (Proteinase Inhibitory Proteins, Secretory); 0 (RNA, Messenger); 0 (SPINK7 protein, human); 0 (Serine Peptidase Inhibitors, Kazal Type); 0 (X-Linked Inhibitor of Apoptosis Protein)
[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:151006
[St] Status:MEDLINE
[do] DOI:10.1038/onc.2015.339


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[PMID]:24821237
[Au] Autor:Lun YZ; Wang XL; Feng J
[Ad] Endereço:Liaoning Provincial University Key Laboratory of Biophysics, College of Medicine, Dalian University, Dalian, Liaoning 116622, P.R. China.
[Ti] Título:Purification and identification of the Kazal domain of a novel serine protease inhibitor, Hespintor, through a bacterial (Escherichia coli) expression system.
[So] Source:Int J Mol Med;34(1):321-6, 2014 Jul.
[Is] ISSN:1791-244X
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:In this study, Hespintor, a protein with unknown function, was screened and obtained from the hepatoblastoma cell line, HepG2, using suppression subtractive hybridization (SSH). Sequence analysis demonstrated that the protein is a novel secreting member of the Kazal-type serine protease inhibitor (serpin) family, and possesses the basic structure of serpin, which is highly homologous to esophageal cancer-related gene 2 (ECRG2). To further elucidate its biological functions, the Hespintor protein was expressed and purified. The coding sequence of the Hespintor Kazal domain was cloned into the prokaryotic expression vector, pET-40b(+), and was then transformed into host bacteria (Escherichia coli) Rosetta (DE3). The optimally expressed recombinant fusion protein, Hespintor-Kazal, with a molecular weight of 42 kDa was obtained by 0.25 mmol/l isopropyl ß-D-1-thiogalactopyranoside (IPTG) induction at 30˚C for 5 h. Western blot analysis was performed to further confirm the specificity of the recombinant protein, Hespintor-Kazal. The recombinant fusion protein, Hespintor­Kazal, was expressed in the host bacteria in the form of an inclusion body. Two-step metal chelating affinity chromatography and anion exchange chromatography columns were used to purify the recombinant protein. The preliminary activity identification results revealed that the purified recombinant fusion protein, Hespintor-Kazal, specifically inhibited the hydrolysis activity of trypsin, suggesting that Hespintor has potential value as a novel antitumor drug.
[Mh] Termos MeSH primário: Expressão Gênica
Proteínas Recombinantes de Fusão/química
Serpinas/química
Inibidores da Tripsina/química
Tripsina/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sequência de Bases
Clonagem Molecular
Escherichia coli/efeitos dos fármacos
Escherichia coli/genética
Escherichia coli/metabolismo
Células Hep G2
Seres Humanos
Corpos de Inclusão/química
Isopropiltiogalactosídeo/farmacologia
Modelos Moleculares
Dados de Sequência Molecular
Peso Molecular
Fases de Leitura Aberta
Proteínas Secretadas Inibidoras de Proteinases/química
Proteínas Secretadas Inibidoras de Proteinases/genética
Proteínas Secretadas Inibidoras de Proteinases/metabolismo
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/isolamento & purificação
Proteínas Recombinantes de Fusão/metabolismo
Homologia de Sequência de Aminoácidos
Inibidores de Serinopeptidase do Tipo Kazal
Serpinas/genética
Serpinas/isolamento & purificação
Serpinas/metabolismo
Técnicas de Hibridização Subtrativa
Inibidores da Tripsina/isolamento & purificação
Inibidores da Tripsina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteinase Inhibitory Proteins, Secretory); 0 (Recombinant Fusion Proteins); 0 (SPINK7 protein, human); 0 (Serine Peptidase Inhibitors, Kazal Type); 0 (Serpins); 0 (Trypsin Inhibitors); 367-93-1 (Isopropyl Thiogalactoside); EC 3.4.21.4 (Trypsin)
[Em] Mês de entrada:1412
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140514
[St] Status:MEDLINE
[do] DOI:10.3892/ijmm.2014.1778


  8 / 47 MEDLINE  
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[PMID]:24699552
[Au] Autor:Dietz JA; Maes ME; Huang S; Yandell BS; Schlamp CL; Montgomery AD; Allingham RR; Hauser MA; Nickells RW
[Ad] Endereço:Department of Ophthalmology and Visual Sciences, University of Wisconsin, Madison, Wisconsin, United States of America.
[Ti] Título:Spink2 modulates apoptotic susceptibility and is a candidate gene in the Rgcs1 QTL that affects retinal ganglion cell death after optic nerve damage.
[So] Source:PLoS One;9(4):e93564, 2014.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Rgcs1 quantitative trait locus, on mouse chromosome 5, influences susceptibility of retinal ganglion cells to acute damage of the optic nerve. Normally resistant mice (DBA/2J) congenic for the susceptible allele from BALB/cByJ mice exhibit susceptibility to ganglion cells, not only in acute optic nerve crush, but also to chronic inherited glaucoma that is characteristic of the DBA/2J strain as they age. SNP mapping of this QTL has narrowed the region of interest to 1 Mb. In this region, a single gene (Spink2) is the most likely candidate for this effect. Spink2 is expressed in retinal ganglion cells and is increased after optic nerve damage. This gene is also polymorphic between resistant and susceptible strains, containing a single conserved amino acid change (threonine to serine) and a 220 bp deletion in intron 1 that may quantitatively alter endogenous expression levels between strains. Overexpression of the different variants of Spink2 in D407 tissue culture cells also increases their susceptibility to the apoptosis-inducing agent staurosporine in a manner consistent with the differential susceptibility between the DBA/2J and BALB/cByJ strains.
[Mh] Termos MeSH primário: Apoptose/fisiologia
Nervo Óptico/patologia
Locos de Características Quantitativas
Células Ganglionares da Retina/citologia
Serpinas/fisiologia
[Mh] Termos MeSH secundário: Animais
Sequência de Bases
DNA
Camundongos
Camundongos Endogâmicos BALB C
Camundongos Endogâmicos DBA
Dados de Sequência Molecular
Polimorfismo de Nucleotídeo Único
Células Ganglionares da Retina/metabolismo
Inibidores de Serinopeptidase do Tipo Kazal
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (SPINK2 protein, mouse); 0 (Serine Peptidase Inhibitors, Kazal Type); 0 (Serpins); 9007-49-2 (DNA)
[Em] Mês de entrada:1502
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140405
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0093564


  9 / 47 MEDLINE  
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[PMID]:24606472
[Au] Autor:Song HY; Deng XH; Yuan GY; Hou XF; Zhu ZD; Zhou L; Ren MX
[Ad] Endereço:College of Basic Medicine, Xinxiang Medical University; Key Laboratory for Medical Tissue Regeneration of Henan Province, Xinxiang, China E-mail : shy80825@163.com.
[Ti] Título:Expression of bcl-2 and p53 in induction of esophageal cancer cell apoptosis by ECRG2 in combination with cisplatin.
[So] Source:Asian Pac J Cancer Prev;15(3):1397-401, 2014.
[Is] ISSN:2476-762X
[Cp] País de publicação:Thailand
[La] Idioma:eng
[Ab] Resumo:AIM: To investigate the mechanisms of induction of apoptosis of esophageal cancer cells by esophageal cancer-related gene 2 (ECRG2) in combination with cisplatin (DDP). METHODS: Hoechest staining was performed to analyze the effects of single ECRG2 and ECRG2 in combination with DDP on apoptosis of EC9706 cells. The expression levels of p53 and bcl-2 mRNA and protein were determined by RT-PCR and Western blotting, respectively. RESULTS: The number of apoptotic cells after the treatment with ECRG2 in combination with DDP for 24 hours was more than that after the treatment with single ECRG2. RT-PCR and Western blotting showed that the expression levels of bcl-2 mRNA and protein were both down-regulated, while p53 mRNA and protein were both up-regulated in the cells treated with ECRG2 in combination with DDP compared with those given ECRG2 alone. CONCLUSION: ECRG2 in combination with DDP can enhance the apoptosis of EC9706 cells, possibly by down-regulating bcl-2 expression and up-regulating p53.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Neoplasias Esofágicas/tratamento farmacológico
Proteínas Secretadas Inibidoras de Proteinases/farmacologia
Proteínas Proto-Oncogênicas c-bcl-2/biossíntese
Proteína Supressora de Tumor p53/biossíntese
[Mh] Termos MeSH secundário: Antineoplásicos/farmacologia
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Cisplatino/farmacologia
Regulação para Baixo
Resistência a Medicamentos Antineoplásicos
Neoplasias Esofágicas/patologia
Seres Humanos
Proteínas Proto-Oncogênicas c-bcl-2/genética
RNA Mensageiro/biossíntese
Inibidores de Serinopeptidase do Tipo Kazal
Proteína Supressora de Tumor p53/genética
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Proteinase Inhibitory Proteins, Secretory); 0 (Proto-Oncogene Proteins c-bcl-2); 0 (RNA, Messenger); 0 (SPINK7 protein, human); 0 (Serine Peptidase Inhibitors, Kazal Type); 0 (Tumor Suppressor Protein p53); Q20Q21Q62J (Cisplatin)
[Em] Mês de entrada:1411
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140311
[St] Status:MEDLINE


  10 / 47 MEDLINE  
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[PMID]:24441102
[Au] Autor:Sperrhacke M; Fischer J; Wu Z; Klünder S; Sedlacek R; Schroeder JM; Meyer-Hoffert U; Reiss K
[Ad] Endereço:Department of Dermatology, University Hospital Schleswig-Holstein, Christian-Albrecht University Kiel, Kiel, Germany.
[Ti] Título:SPINK9 stimulates metalloprotease/EGFR-dependent keratinocyte migration via purinergic receptor activation.
[So] Source:J Invest Dermatol;134(6):1645-1654, 2014 Jun.
[Is] ISSN:1523-1747
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Serine protease inhibitors of the Kazal-type 9 (SPINK9) is a keratinocyte-derived cationic peptide that is found most abundantly in the upper layers of the palmar-plantar epidermis. In vitro, the peptide displays the capacity to inhibit specifically kallikrein-related peptidase 5 (KLK5). Here, we report that cells expressing SPINK9 secrete the peptide constitutively. Recombinant SPINK9 (rSPINK9) provoked transactivation of the EGFR in human keratinocytes, resulting in efficient downstream triggering of cell migration. Transactivation occurred via functional upregulation of a disintegrin and metalloproteases (ADAMs), as evidenced by suppression with a metalloproteinase inhibitor and an EGFR-blocking antibody. SPINK9 preparations isolated from human skin also displayed EGFR-transactivating capacity. The classical purinergic receptor antagonists oxidized ATP and pyridoxalphosphate-6-azophenyl-2',4',-disulfonic acid effectively suppressed EGFR transactivation by rSPINK9, indicating that in analogy to what has recently been reported for the cationic antimicrobial peptides cathelicidin LL-37 and bee venom melittin, purinergic receptors have an essential bridging role in promoting the upregulation of ADAM function by the cationic peptide. SPINK9 could represent an example of how a cationic peptide may subserve multiple and interrelated functions that contribute to the maintenance of the physical and immunological barrier of the skin.
[Mh] Termos MeSH primário: Movimento Celular
Regulação Enzimológica da Expressão Gênica
Queratinócitos/citologia
Proteínas Secretadas Inibidoras de Proteinases/metabolismo
Receptores Purinérgicos/metabolismo
[Mh] Termos MeSH secundário: Peptídeos Catiônicos Antimicrobianos/metabolismo
Proliferação Celular
Sobrevivência Celular
Clonagem Molecular
Células HEK293
Seres Humanos
Calicreínas/metabolismo
Metaloproteases/metabolismo
Receptor do Fator de Crescimento Epidérmico/metabolismo
Proteínas Recombinantes/metabolismo
Inibidores de Serinopeptidase do Tipo Kazal
Transdução de Sinais
Transfecção
Cicatrização
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antimicrobial Cationic Peptides); 0 (Proteinase Inhibitory Proteins, Secretory); 0 (Receptors, Purinergic); 0 (Recombinant Proteins); 0 (Serine Peptidase Inhibitors, Kazal Type); 0 (Spink9 protein, human); 143108-26-3 (CAP18 lipopolysaccharide-binding protein); EC 2.7.10.1 (Receptor, Epidermal Growth Factor); EC 3.4.- (Metalloproteases); EC 3.4.21.- (KLK5 protein, human); EC 3.4.21.- (Kallikreins)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140121
[St] Status:MEDLINE



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