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Pesquisa : D08.811.913.696.640.025 [Categoria DeCS]
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[PMID]:28031362
[Au] Autor:Xu JD; Jiang HS; Wei TD; Zhang KY; Wang XW; Zhao XF; Wang JX
[Ad] Endereço:Shandong Provincial Key Laboratory of Animal Cells and Developmental Biology, School of Life Sciences, Shandong University, Shandong, China.
[Ti] Título:Interaction of the Small GTPase Cdc42 with Arginine Kinase Restricts White Spot Syndrome Virus in Shrimp.
[So] Source:J Virol;91(5), 2017 Mar 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many types of small GTPases are widely expressed in eukaryotes and have different functions. As a crucial member of the Rho GTPase family, Cdc42 serves a number of functions, such as regulating cell growth, migration, and cell movement. Several RNA viruses employ Cdc42-hijacking tactics in their target cell entry processes. However, the function of Cdc42 in shrimp antiviral immunity is not clear. In this study, we identified a Cdc42 protein in the kuruma shrimp ( ) and named it Cdc42. Cdc42 was upregulated in shrimp challenged by white spot syndrome virus (WSSV). The knockdown of Cdc42 and injection of Cdc42 inhibitors increased the proliferation of WSSV. Further experiments determined that Cdc42 interacted with an arginine kinase ( AK). By analyzing the binding activity and enzyme activity of AK and its mutant, Δ AK, we found that AK could enhance the replication of WSSV in shrimp. AK interacted with the envelope protein VP26 of WSSV. An inhibitor of AK activity, quercetin, could impair the function of AK in WSSV replication. Further study demonstrated that the binding of Cdc42 and AK depends on Cys of AK and suppresses the WSSV replication-promoting effect of AK. By interacting with the active site of AK and suppressing its enzyme activity, Cdc42 inhibits WSSV replication in shrimp. Our results demonstrate a new function of Cdc42 in the cellular defense against viral infection in addition to the regulation of actin and phagocytosis, which has been reported in previous studies. The interaction of Cdc42 with arginine kinase plays a crucial role in the host defense against WSSV infection. This study identifies a new mechanism of Cdc42 in innate immunity and enriches the knowledge of the antiviral innate immunity of invertebrates.
[Mh] Termos MeSH primário: Arginina Quinase/metabolismo
Proteínas de Artrópodes/metabolismo
Penaeidae/virologia
Replicação Viral
Vírus 1 da Síndrome da Mancha Branca/fisiologia
Proteína cdc42 de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Arginina Quinase/química
Proteínas de Artrópodes/química
Sequência Conservada
Indução Enzimática/imunologia
Escherichia coli
Interações Hospedeiro-Patógeno
Imunidade Inata
Simulação de Acoplamento Molecular
Penaeidae/enzimologia
Penaeidae/imunologia
Ligação Proteica
Mapas de Interação de Proteínas
Regulação para Cima
Proteína cdc42 de Ligação ao GTP/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arthropod Proteins); EC 2.7.3.3 (Arginine Kinase); EC 3.6.5.2 (cdc42 GTP-Binding Protein)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161230
[St] Status:MEDLINE


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[PMID]:27859253
[Au] Autor:Bullock N; Oltean S
[Ad] Endereço:School of Physiology, Pharmacology and Neuroscience, University of Bristol, Bristol, UK.
[Ti] Título:The many faces of SRPK1.
[So] Source:J Pathol;241(4):437-440, 2017 03.
[Is] ISSN:1096-9896
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Serine-arginine protein kinase 1 (SRPK1) phosphorylates proteins involved in the regulation of several mRNA-processing pathways, including alternative splicing. SRPK1 has been recently reported to be overexpressed in multiple cancers, including prostate cancer, breast cancer, lung cancer, and glioma. Several studies have shown that inhibition of SRPK1 has anti-tumoural effects, and SRPK1 has therefore become a new candidate for targeted therapies. Interestingly, in terms of molecular mechanism, SRPK1 seems to act heterogeneously, and has been reported to affect several processes in different cancers, e.g. angiogenesis in prostate and colon cancer, apoptosis in breast and colon cancer, and migration in breast cancer. A recent report adds to this puzzle, showing that the main effect of SRPK1 overexpression in non-small-cell lung carcinoma is to stimulate a stem cell-like phenotype. This pleiotropy might be related to preferential activation of different downstream signalling pathways by SRPK1 in various cancers. © 2016 The Authors. The Journal of Pathology published by John Wiley & Sons Ltd on behalf of Pathological Society of Great Britain and Ireland.
[Mh] Termos MeSH primário: Proteínas Quinases/genética
Proteínas Serina-Treonina Quinases/antagonistas & inibidores
[Mh] Termos MeSH secundário: Arginina/genética
Arginina Quinase/genética
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Masculino
Proteínas Serina-Treonina Quinases/fisiologia
Serina/genética
Reino Unido
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
452VLY9402 (Serine); 94ZLA3W45F (Arginine); EC 2.7.- (Protein Kinases); EC 2.7.1.- (SRPK1 protein, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.3.3 (Arginine Kinase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE
[do] DOI:10.1002/path.4846


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[PMID]:27840974
[Au] Autor:Yang H; Chen H; Jin M; Xie H; He S; Wei JF
[Ad] Endereço:Allergy and Clinical Immunology Research Centre, The First Affiliated Hospital of Liaoning Medical University, Jinzhou, Liaoning 121001, P.R. China.
[Ti] Título:Molecular cloning, expression, IgE binding activities and in silico epitope prediction of Per a 9 allergens of the American cockroach.
[So] Source:Int J Mol Med;38(6):1795-1805, 2016 Dec.
[Is] ISSN:1791-244X
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Per a 9 is a major allergen of the American cockroach (CR), which has been recognized as an important cause of imunoglobulin E-mediated type I hypersensitivity worldwide. However, it is not neasy to obtain a substantial quantity of this allergen for use in functional studies. In the present study, the Per a 9 gene was cloned and expressed in Escherichia coli (E. coli) systems. It was found that 13/16 (81.3%) of the sera from patients with allergies caused by the American CR reacted to Per a 9, as assessed by enzyme-linked immunosorbent assay, confirming that Per a 9 is a major allergen of CR. The induction of the expression of CD63 and CCR3 in passively sensitized basophils (from sera of patients with allergies caused by the American CR) by approximately 4.2-fold indicated that recombinant Per a 9 was functionally active. Three immunoinformatics tools, including the DNAStar Protean system, Bioinformatics Predicted Antigenic Peptides (BPAP) system and the BepiPred 1.0 server were used to predict the potential B cell epitopes, while Net-MHCIIpan-2.0 and NetMHCII-2.2 were used to predict the T cell epitopes of Per a 9. As a result, we predicted 11 peptides (23-28, 39-46, 58-64, 91-118, 131-136, 145-154, 159-165, 176-183, 290-299, 309-320 and 338-344) as potential B cell linear epitopes. In T cell prediction, the Per a 9 allergen was predicted to have 5 potential T cell epitope sequences, 119-127, 194-202, 210-218, 239-250 and 279-290. The findings of our study may prove to be useful in the development of peptide-based vaccines to combat CR-induced allergies.
[Mh] Termos MeSH primário: Alérgenos/genética
Alérgenos/imunologia
Arginina Quinase/genética
Arginina Quinase/imunologia
Clonagem Molecular
Epitopos de Linfócito B/imunologia
Expressão Gênica
Imunoglobulina E/imunologia
Periplaneta/genética
Periplaneta/imunologia
[Mh] Termos MeSH secundário: Alérgenos/química
Sequência de Aminoácidos
Animais
Arginina Quinase/química
Sequência de Bases
Basófilos/imunologia
Sítios de Ligação
Epitopos de Linfócito B/química
Seres Humanos
Imunoglobulina E/sangue
Modelos Moleculares
Filogenia
Conformação Proteica
Proteínas Recombinantes
Rinite Alérgica/sangue
Rinite Alérgica/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Allergens); 0 (Epitopes, B-Lymphocyte); 0 (Recombinant Proteins); 37341-29-0 (Immunoglobulin E); EC 2.7.3.3 (Arginine Kinase); EC 2.7.3.3. (Per a 9 allergen, Periplaneta americana)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170314
[Lr] Data última revisão:
170314
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161115
[St] Status:MEDLINE
[do] DOI:10.3892/ijmm.2016.2793


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[PMID]:27594681
[Au] Autor:Godsey MH; Davulcu O; Nix JC; Skalicky JJ; Brüschweiler RP; Chapman MS
[Ad] Endereço:Department of Math/Science, Concordia University, Portland, OR 97211, USA.
[Ti] Título:The Sampling of Conformational Dynamics in Ambient-Temperature Crystal Structures of Arginine Kinase.
[So] Source:Structure;24(10):1658-1667, 2016 Oct 04.
[Is] ISSN:1878-4186
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Arginine kinase provides a model for functional dynamics, studied through crystallography, enzymology, and nuclear magnetic resonance. Structures are now solved, at ambient temperature, for the transition state analog (TSA) complex. Analysis of quasi-rigid sub-domain displacements show that differences between the two TSA structures average about 5% of changes between substrate-free and TSA forms, and they are nearly co-linear. Small backbone hinge rotations map to sites that also flex on substrate binding. Anisotropic atomic displacement parameters (ADPs) are refined using rigid-body TLS constraints. Consistency between crystal forms shows that they reflect intrinsic molecular properties more than crystal lattice effects. In many regions, the favored directions of thermal/static displacement are appreciably correlated with movements on substrate binding. Correlation between ADPs and larger substrate-associated movements implies that the latter approximately follow paths of low-energy intrinsic motions.
[Mh] Termos MeSH primário: Arginina Quinase/química
Caranguejos Ferradura/enzimologia
[Mh] Termos MeSH secundário: Animais
Anisotropia
Cristalografia por Raios X
Caranguejos Ferradura/química
Modelos Moleculares
Ligação Proteica
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.7.3.3 (Arginine Kinase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160906
[St] Status:MEDLINE


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[PMID]:27318110
[Au] Autor:Shi XY; Zhang LL; Wu F; Fu YY; Yin SJ; Si YX; Park YD
[Ad] Endereço:College of Biological and Environmental Sciences, Zhejiang Wanli University, Ningbo 315100, PR China.
[Ti] Título:Kinetics for Cu(2+) induced Sepia pharaonis arginine kinase inactivation and aggregation.
[So] Source:Int J Biol Macromol;91:926-33, 2016 Oct.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Arginine kinase plays an important role in cellular energy metabolism and is closely related to the environmental stress response in marine invertebrates. We studied the Cu(2+)-mediated inhibition and aggregation of Sepia pharaonis arginine kinase (SPAK) and found that Cu(2+) markedly inhibited the SPAK activity along with mixed-type inhibition against the arginine substrate and noncompetitive inhibition against the ATP cofactor. Spectrofluorimetry results showed that Cu(2+) induced a tertiary structure change in SPAK, resulting in exposure of the hydrophobic surface and increased aggregation. Cu(2+)-mediated SPAK aggregation followed first-order kinetics consistent with monophasic and a biphasic processes. Addition of osmolytes, including glycine and proline, effectively blocked SPAK aggregation and restored SPAK activity. Our results demonstrated the effects of Cu(2+) on SPAK catalytic function, conformation, and aggregation, as well as the protective effects of osmolytes on SPAK folding. This study provided important insights into the role of Cu(2+) as a negative effector of the S. pharaonis metabolic enzyme AK and the possible responses of cephalopods to unfavorable environmental conditions.
[Mh] Termos MeSH primário: Arginina Quinase/química
Arginina Quinase/metabolismo
Agregados Proteicos/efeitos dos fármacos
Sepia/enzimologia
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/farmacologia
Animais
Arginina Quinase/antagonistas & inibidores
Dicroísmo Circular
Ativação Enzimática/efeitos dos fármacos
Glicina/farmacologia
Cinética
Prolina/farmacologia
Inibidores de Proteínas Quinases/farmacologia
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Espectrometria de Fluorescência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Aggregates); 0 (Protein Kinase Inhibitors); 8L70Q75FXE (Adenosine Triphosphate); 9DLQ4CIU6V (Proline); EC 2.7.3.3 (Arginine Kinase); TE7660XO1C (Glycine)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170310
[Lr] Data última revisão:
170310
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160619
[St] Status:MEDLINE


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[PMID]:27129461
[Au] Autor:Motomura S; Suzuki T
[Ad] Endereço:Laboratory of Biochemistry, Faculty of Science, Kochi University, Kochi, 780-8520, Japan.
[Ti] Título:Evidence for N-Terminal Myristoylation of Tetrahymena Arginine Kinase Using Peptide Mass Fingerprinting Analysis.
[So] Source:Protein J;35(3):212-7, 2016 06.
[Is] ISSN:1875-8355
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In this study, we confirmed N-terminal myristoylation of Tetrahymena pyriformis arginine kinase (AK1) by identifying a myristoylation signal sequence at the N-terminus. A sufficient amount of modified enzyme was synthesized using an insect cell-free protein synthesis system that contains all of the elements necessary for post-transcriptional modification by fatty acids. Subsequent peptide mass fingerprinting (PMF) analyses were performed after digestion with trypsin. The PMF data covered 39 % (143 residues) of internal peptides. The target N-myristoylated peptide had a theoretical mass of 832.4477 and was clearly observed with an experimental mass (m/z-H(+)) of 832.4747. The difference between the two masses was 0.0271, supporting the accuracy of identification and indicating that the synthesized T. pyriformis AK1 is myristoylated. The fixed specimens of T. pyriformis were reacted with an anti-AK1 peptide antibody followed by a secondary antibody with a fluorescent chromophore and were observed using immunofluorescence microscope. In agreement with previous western blotting analyses, microscopic observations suggested that AK1 is localized in the cilia. The present PMF and microscopic analyses indicate that T. pyriformis AK1 may be localized and anchored to ciliary membranes via N-terminal myristoyl groups.
[Mh] Termos MeSH primário: Arginina Quinase/química
Ácido Mirístico/análise
Tetrahymena pyriformis/citologia
Tetrahymena pyriformis/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Peptídeos/química
Tetrahymena pyriformis/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Peptides); 0I3V7S25AW (Myristic Acid); EC 2.7.3.3 (Arginine Kinase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160501
[St] Status:MEDLINE
[do] DOI:10.1007/s10930-016-9663-0


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[PMID]:27095694
[Au] Autor:Yano D; Mimura S; Uda K; Suzuki T
[Ad] Endereço:Laboratory of Biochemistry, Faculty of Science, Kochi University, Kochi 780-8520, Japan.
[Ti] Título:Arginine kinase from Myzostoma cirriferum, a basal member of annelids.
[So] Source:Comp Biochem Physiol B Biochem Mol Biol;198:73-8, 2016 Aug.
[Is] ISSN:1879-1107
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We assembled a phosphagen kinase gene from the Expressed Sequence Tags database of Myzostoma cirriferum, a basal member of annelids. The assembled gene sequence was synthesized using an overlap extension polymerase chain reaction method and was expressed in Escherichia coli. The recombinant enzyme (355 residues) exhibited monomeric behavior on a gel filtration column and showed strong activity only for l-arginine. Thus, the enzyme was identified as arginine kinase (AK). The two-substrate kinetic parameters were obtained and compared with other AKs. Phylogenetic analysis of amino acid sequences of phosphagen kinases indicated that the Myzostoma AK gene lineage differed from that of the polychaete Sabellastarte spectabilis AK, which is a dimer of creatine kinase (CK) origin. It is likely that the Myzostoma AK gene lineage was lost at an early stage of annelid evolution and that Sabellastarte AK evolved secondarily from the CK gene. This work contributes to our understanding of the evolution of phosphagen kinases of annelids with marked diversity.
[Mh] Termos MeSH primário: Anelídeos/enzimologia
Arginina Quinase/química
Arginina Quinase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Anelídeos/genética
Arginina Quinase/genética
Etiquetas de Sequências Expressas/metabolismo
Cinética
Alinhamento de Sequência
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.7.3.3 (Arginine Kinase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170203
[Lr] Data última revisão:
170203
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160421
[St] Status:MEDLINE


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[PMID]:27072556
[Au] Autor:Lopez-Zavala AA; Sotelo-Mundo RR; Hernandez-Flores JM; Lugo-Sanchez ME; Sugich-Miranda R; Garcia-Orozco KD
[Ad] Endereço:Departamento de Ciencias Químico Biológicas, Universidad de Sonora, Calle Rosales y Blvd. Luis Encinas s/n, Col. Centro, Hermosillo, Sonora, 83000, México.
[Ti] Título:Arginine kinase shows nucleoside diphosphate kinase-like activity toward deoxythymidine diphosphate.
[So] Source:J Bioenerg Biomembr;48(3):301-8, 2016 06.
[Is] ISSN:1573-6881
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Arginine kinase (AK) (ATP: L-arginine phosphotransferase, E.C. 2.7.3.3) catalyzes the reversible transfer of ATP γ-phosphate group to L-arginine to synthetize phospho-arginine as a high-energy storage. Previous studies suggest additional roles for AK in cellular processes. Since AK is found only in invertebrates and it is homologous to creatine kinase from vertebrates, the objective of this work was to demonstrate nucleoside diphosphate kinase-like activity for shrimp AK. For this, AK from marine shrimp Litopenaeus vannamei (LvAK) was purified and its activity was assayed for phosphorylation of TDP using ATP as phosphate donor. Moreover, by using high-pressure liquid chromatography (HPLC) the phosphate transfer reaction was followed. Also, LvAK tryptophan fluorescence emission changes were detected by dTDP titration, suggesting that the hydrophobic environment of Trp 221, which is located in the top of the active site, is perturbed upon dTDP binding. The kinetic constants for both substrates Arg and dTDP were calculated by isothermal titration calorimetry (ITC). Besides, docking calculations suggested that dTDP could bind LvAK in the same cavity where ATP bind, and LvAK basic residues (Arg124, 126 and 309) stabilize the dTDP phosphate groups and the pyrimidine base interact with His284 and Ser122. These results suggest that LvAK bind and phosphorylate dTDP being ATP the phosphate donor, thus describing a novel alternate nucleoside diphosphate kinase-like activity for this enzyme.
[Mh] Termos MeSH primário: Arginina Quinase/metabolismo
Núcleosídeo-Difosfato Quinase/metabolismo
Penaeidae/enzimologia
Nucleotídeos de Timina/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Animais
Simulação de Acoplamento Molecular
Fosforilação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Thymine Nucleotides); 2863-04-9 (thymidine 3',5'-diphosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.3.3 (Arginine Kinase); EC 2.7.4.6 (Nucleoside-Diphosphate Kinase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171021
[Lr] Data última revisão:
171021
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160414
[St] Status:MEDLINE
[do] DOI:10.1007/s10863-016-9660-1


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[PMID]:27033465
[Au] Autor:Jiang S; Jia Z; Chen H; Wang L; Song L
[Ad] Endereço:Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, 266071, China.
[Ti] Título:The modulation of haemolymph arginine kinase on the extracellular ATP induced bactericidal immune responses in the Pacific oyster Crassostrea gigas.
[So] Source:Fish Shellfish Immunol;54:282-93, 2016 Jul.
[Is] ISSN:1095-9947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Arginine kinase is an important phosphagen kinase (PK) which plays an essential role in ATP buffering systems in invertebrates. In the present study, an arginine kinase (designated CgAK) was isolated by the lipopolysaccharide (LPS) affinity chromatography from the haemolymph of Crassostrea gigas. CgAK could directly bind to LPS in a concentration-dependent manner with the dissociation constant (Kd) of 2.46 × 10(-6) M. The interaction with LPS significantly decreased the ATP hydrolytic activity of CgAK, which in turn lead to the accumulation of ATP in vitro. The extracellular ATP stimulation could induce Ca(2+) influx, reactive oxygen species (ROS) production, and the release of lysosomal enzyme in the cellular immune response. In addition, ATP stimulation provoked the bactericidal activity towards Escherichia coli, and the scavenging ROS with N-acetyl-l-cysteine (NAC) abrogated the bactericidal activity, indicating that ATP stimulation could induce ROS-dependent antimicrobial activity in haemocytes. Collectively, the results demonstrated that the haemolymph CgAK could serve as an important purinergic regulator to modulate extracellular ATP, which might further have an important effect on the purinergic signaling-activated innate immune response of oyster.
[Mh] Termos MeSH primário: Arginina Quinase/genética
Crassostrea/genética
Crassostrea/imunologia
Proteínas de Peixes/genética
Imunidade Inata
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Sequência de Aminoácidos
Animais
Arginina Quinase/química
Arginina Quinase/metabolismo
Sequência de Bases
Crassostrea/metabolismo
Crassostrea/microbiologia
Escherichia coli/fisiologia
Proteínas de Peixes/química
Proteínas de Peixes/metabolismo
Hemolinfa/imunologia
Hemolinfa/microbiologia
Modelos Genéticos
Fases de Leitura Aberta
Estrutura Terciária de Proteína
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fish Proteins); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.3.3 (Arginine Kinase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170209
[Lr] Data última revisão:
170209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160402
[St] Status:MEDLINE


  10 / 315 MEDLINE  
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[PMID]:27030550
[Au] Autor:Si YX; Lee J; Cheng JG; Yin SJ; Park YD; Qian GY; Jiang XM
[Ti] Título:Kinetics for Zinc Ion Induced Sepia Pharaonis Arginine Kinase Inactivation and Aggregation.
[So] Source:Protein Pept Lett;23(6):508-17, 2016.
[Is] ISSN:1875-5305
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Arginine kinase is an essential enzyme which is closely related to energy metabolism in marine invertebrates. Arginine kinase provides a significant role in quick response to environmental change and stress. In this study, we simulated a tertiary structure of Sepia pharaonis arginine kinase (SPAK) based on the gene sequence and conducted the molecular dynamics simulations between SPAK and Zn(2+). Using these results, the Zn(2+) binding sites were predicted and the initial effect of Zn(2+) on the SPAK structure was elucidated. Subsequently, the experimental kinetic results were compared with the simulation results. Zn(2+) markedly inhibited the activity of SPAK in a manner of non-competitive inhibitions for both arginine and ATP. We also found that Zn(2+) binding to SPAK resulted in tertiary conformational change accompanying with the hydrophobic residues exposure. These changes caused SPAK aggregation directly. We screened two protectants, glycine and proline, which effectively prevented SPAK aggregation and recovered the structure and activity. Overall, our study suggested the inhibitory effect of Zn(2+) on SPAK and Zn(2+) can trigger SPAK aggregation after exposing large extent of hydrophobic surface. The protective effects of glycine and proline against Zn(2+) on SPAK folding were also demonstrated.
[Mh] Termos MeSH primário: Arginina Quinase/antagonistas & inibidores
Sepia/enzimologia
Zinco/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Arginina Quinase/genética
Arginina Quinase/metabolismo
Sítios de Ligação
Clonagem Molecular
Metabolismo Energético
Interações Hidrofóbicas e Hidrofílicas
Cinética
Simulação de Dinâmica Molecular
Sepia/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.7.3.3 (Arginine Kinase); J41CSQ7QDS (Zinc)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170528
[Lr] Data última revisão:
170528
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160401
[St] Status:MEDLINE



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