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[PMID]: 26980003 [Au] Autor: Park S; Shin YM; Seo J; Song JJ; Yang H [Ad] Endereço: Department of Chemistry and Chemistry Institute for Functional Materials, Pusan National University, Busan 46241, Korea. hyang@pusan.ac.kr. [Ti] Título: A highly sensitive and simply operated protease sensor toward point-of-care testing. [So] Source: Analyst;141(8):2481-6, 2016 Apr 21. [Is] ISSN: 1364-5528 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Protease sensors for point-of-care testing (POCT) require simple operation, a detection period of less than 20 minutes, and a detection limit of less than 1 ng mL(-1). However, it is difficult to meet these requirements with protease sensors that are based on proteolytic cleavage. This paper reports a highly reproducible protease sensor that allows the sensitive and simple electrochemical detection of the botulinum neurotoxin type E light chain (BoNT/E-LC), which is obtained using (i) low nonspecific adsorption, (ii) high signal-to-background ratio, and (iii) one-step solution treatment. The BoNT/E-LC detection is based on two-step proteolytic cleavage using BoNT/E-LC (endopeptidase) and l-leucine-aminopeptidase (LAP, exopeptidase). Indium-tin oxide (ITO) electrodes are modified partially with reduced graphene oxide (rGO) to increase their electrocatalytic activities. Avidin is then adsorbed on the electrodes to minimize the nonspecific adsorption of proteases. Low nonspecific adsorption allows a highly reproducible sensor response. Electrochemical-chemical (EC) redox cycling involving p-aminophenol (AP) and dithiothreitol (DTT) is performed to obtain a high signal-to-background ratio. After adding a C-terminally AP-labeled oligopeptide, DTT, and LAP simultaneously to a sample solution, no further treatment of the solution is necessary during detection. The detection limits of BoNT/E-LC in phosphate-buffered saline are 0.1 ng mL(-1) for an incubation period of 15 min and 5 fg mL(-1) for an incubation period of 4 h. The detection limit in commercial bottled water is 1 ng mL(-1) for an incubation period of 15 min. The developed sensor is selective to BoNT/E-LC among the four types of BoNTs tested. These results indicate that the protease sensor meets the requirements for POCT. [Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos Toxinas Botulínicas/análise Endopeptidases/metabolismo Exopeptidases/metabolismo Testes Imediatos [Mh] Termos MeSH secundário: Adsorção Sequência de Aminoácidos Aminofenóis/química Técnicas Biossensoriais/instrumentação Toxinas Botulínicas/química Toxinas Botulínicas/metabolismo Ditiotreitol/química Eletroquímica Eletrodos Limite de Detecção Proteólise Compostos de Estanho/química [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Aminophenols); 0 (Tin Compounds); 71243-84-0 (indium tin oxide); EC 3.4.- (Endopeptidases); EC 3.4.- (Exopeptidases); EC 3.4.24.69 (Botulinum Toxins); R7P8FRP05V (4-aminophenol); T579M564JY (botulinum toxin type E); T8ID5YZU6Y (Dithiothreitol) [Em] Mês de entrada: 1701 [Cu] Atualização por classe: 170116 [Lr] Data última revisão: 170116 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160317 [St] Status: MEDLINE [do] DOI: 10.1039/c6an00251j

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[PMID]: 26733202 [Au] Autor: Nemoto TK; Ohara-Nemoto Y; Bezerra GA; Shimoyama Y; Kimura S [Ad] Endereço: From the Department of Oral Molecular Biology, Course of Medical and Dental Sciences, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki 852-8588, Japan. [Ti] Título: A Porphyromonas gingivalis Periplasmic Novel Exopeptidase, Acylpeptidyl Oligopeptidase, Releases N-Acylated Di- and Tripeptides from Oligopeptides. [So] Source: J Biol Chem;291(11):5913-25, 2016 Mar 11. [Is] ISSN: 1083-351X [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Exopeptidases, including dipeptidyl- and tripeptidylpeptidase, are crucial for the growth of Porphyromonas gingivalis, a periodontopathic asaccharolytic bacterium that incorporates amino acids mainly as di- and tripeptides. In this study, we identified a novel exopeptidase, designated acylpeptidyl oligopeptidase (AOP), composed of 759 amino acid residues with active Ser(615) and encoded by PGN_1349 in P. gingivalis ATCC 33277. AOP is currently listed as an unassigned S9 family peptidase or prolyl oligopeptidase. Recombinant AOP did not hydrolyze a Pro-Xaa bond. In addition, although sequence similarities to human and archaea-type acylaminoacyl peptidase sequences were observed, its enzymatic properties were apparently distinct from those, because AOP scarcely released an N-acyl-amino acid as compared with di- and tripeptides, especially with N-terminal modification. The kcat/Km value against benzyloxycarbonyl-Val-Lys-Met-4-methycoumaryl-7-amide, the most potent substrate, was 123.3 ± 17.3 µm(-1) s(-1), optimal pH was 7-8.5, and the activity was decreased with increased NaCl concentrations. AOP existed predominantly in the periplasmic fraction as a monomer, whereas equilibrium between monomers and oligomers was observed with a recombinant molecule, suggesting a tendency of oligomerization mediated by the N-terminal region (Met(16)-Glu(101)). Three-dimensional modeling revealed the three domain structures (residues Met(16)-Ala(126), which has no similar homologue with known structure; residues Leu(127)-Met(495) (ß-propeller domain); and residues Ala(496)-Phe(736) (α/ß-hydrolase domain)) and further indicated the hydrophobic S1 site of AOP in accord with its hydrophobic P1 preference. AOP orthologues are widely distributed in bacteria, archaea, and eukaryotes, suggesting its importance for processing of nutritional and/or bioactive oligopeptides. [Mh] Termos MeSH primário: Infecções por Bacteroidaceae/microbiologia Exopeptidases/metabolismo Oligopeptídeos/metabolismo Peptídeo Hidrolases/metabolismo Porphyromonas gingivalis/enzimologia [Mh] Termos MeSH secundário: Acilação Sequência de Aminoácidos Exopeptidases/análise Seres Humanos Modelos Moleculares Dados de Sequência Molecular Oligopeptídeos/química Peptídeo Hidrolases/análise Porphyromonas gingivalis/química Porphyromonas gingivalis/citologia Porphyromonas gingivalis/metabolismo Conformação Proteica Multimerização Proteica [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Oligopeptides); EC 3.4.- (Exopeptidases); EC 3.4.- (Peptide Hydrolases); EC 3.4.- (oligopeptidase); EC 3.4.19.1 (acylaminoacyl-peptidase) [Em] Mês de entrada: 1608 [Cu] Atualização por classe: 170311 [Lr] Data última revisão: 170311 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 160107 [St] Status: MEDLINE [do] DOI: 10.1074/jbc.M115.687566

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[PMID]: 26096504 [Au] Autor: Block H; Maertens B; Spriestersbach A; Kubicek J; Schäfer F [Ad] Endereço: QIAGEN GmbH, Research and Development, Qiagenstrasse 1, 40724 Hilden, Germany. [Ti] Título: Proteolytic Affinity Tag Cleavage. [So] Source: Methods Enzymol;559:71-97, 2015. [Is] ISSN: 1557-7988 [Cp] País de publicação: United States [La] Idioma: eng [Ab] Resumo: Here, we present protocols describing the use of the dipeptidyl-aminopeptidase-1 (DPP1, DAPase) exoprotease-based TAGZyme system and the endoprotease, Factor Xa. Both enable the recovery of proteins free of any amino acids encoded by the vector and/or protease recognition site. They also provide the possibility of removing the proteases from the preparation of the target protein by a simple subtractive chromatography step. TAGZyme enzymes contain an uncleavable His tag for removal by Immobilized Metal Ion Affinity Chromatography (IMAC). Factor Xa can be removed using Xa Removal Resin. [Mh] Termos MeSH primário: Cromatografia de Afinidade/métodos Exopeptidases/química [Mh] Termos MeSH secundário: Animais Produtos Biológicos/química Tampões (Química) Catepsina C/química Cromatografia de Afinidade/instrumentação Fator Xa/química Glutationa Transferase/química Histidina/química Seres Humanos Concentração de Íons de Hidrogênio Íons Metais/química Proteólise Proteínas Recombinantes/química [Pt] Tipo de publicação: JOURNAL ARTICLE [Nm] Nome de substância: 0 (Biological Products); 0 (Buffers); 0 (Ions); 0 (Metals); 0 (Recombinant Proteins); 4QD397987E (Histidine); EC 2.5.1.18 (Glutathione Transferase); EC 3.4.- (Exopeptidases); EC 3.4.14.1 (Cathepsin C); EC 3.4.21.6 (Factor Xa) [Em] Mês de entrada: 1603 [Cu] Atualização por classe: 150623 [Lr] Data última revisão: 150623 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 150623 [St] Status: MEDLINE

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[PMID]: 26094643 [Au] Autor: Derouiche A; Shi L; Bidnenko V; Ventroux M; Pigonneau N; Franz-Wachtel M; Kalantari A; Nessler S; Noirot-Gros MF; Mijakovic I [Ad] Endereço: Systems and Synthetic Biology, Department of Biology and Biological Engineering, Chalmers University of Technology, Gothenburg, 41296, Sweden. [Ti] Título: Bacillus subtilis SalA is a phosphorylation-dependent transcription regulator that represses scoC and activates the production of the exoprotease AprE. [So] Source: Mol Microbiol;97(6):1195-208, 2015 Sep. [Is] ISSN: 1365-2958 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Bacillus subtilis Mrp family protein SalA has been shown to indirectly promote the production of the exoprotease AprE by inhibiting the expression of scoC, which codes for a repressor of aprE. The exact mechanism by which SalA influences scoC expression has not been clarified previously. We demonstrate that SalA possesses a DNA-binding domain (residues 1-60), which binds to the promoter region of scoC. The binding of SalA to its target DNA depends on the presence of ATP and is stimulated by phosphorylation of SalA at tyrosine 327. The B. subtilis protein-tyrosine kinase PtkA interacts specifically with the C-terminal domain of SalA in vivo and in vitro and is responsible for activating its DNA binding via phosphorylation of tyrosine 327. In vivo, a mutant mimicking phosphorylation of SalA (SalA Y327E) exhibited a strong repression of scoC and consequently overproduction of AprE. By contrast, the non-phosphorylatable SalA Y327F and the ΔptkA exhibited the opposite effect, stronger expression of scoC and lower production of the exoprotease. Interestingly, both SalA and PtkA contain the same ATP-binding Walker domain and have thus presumably arisen from the common ancestral protein. Their regulatory interplay seems to be conserved in other bacteria. [Mh] Termos MeSH primário: Bacillus subtilis/metabolismo Proteínas de Bactérias/metabolismo Exopeptidases/metabolismo Proteínas de Membrana Transportadoras/metabolismo Fatores de Transcrição/metabolismo [Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo Proteínas de Ligação a DNA/metabolismo Fosforilação Regiões Promotoras Genéticas Domínios e Motivos de Interação entre Proteínas Proteínas Quinases/metabolismo Tirosina/metabolismo [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (AprE protein, Bacteria); 0 (Bacterial Proteins); 0 (DNA-Binding Proteins); 0 (Membrane Transport Proteins); 0 (ScoC protein, Bacillus subtilis); 0 (Transcription Factors); 42HK56048U (Tyrosine); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.- (Protein Kinases); EC 3.4.- (Exopeptidases) [Em] Mês de entrada: 1606 [Cu] Atualização por classe: 150911 [Lr] Data última revisão: 150911 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 150623 [St] Status: MEDLINE [do] DOI: 10.1111/mmi.13098

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[PMID]: 26006050 [Au] Autor: Lázaro S; Gamarra D; Del Val M [Ad] Endereço: Centro de Biología Molecular Severo Ochoa (CSIC-Universidad Autónoma de Madrid), Madrid, Spain. Electronic address: silvialaz@cbm.csic.es. [Ti] Título: Proteolytic enzymes involved in MHC class I antigen processing: A guerrilla army that partners with the proteasome. [So] Source: Mol Immunol;68(2 Pt A):72-6, 2015 Dec. [Is] ISSN: 1872-9142 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Major histocompatibility complex class I proteins (MHC-I) load short peptides derived from proteolytic cleavage of endogenous proteins in any cell of the body, in a process termed antigen processing and presentation. When the source proteins are altered self or encoded by a pathogen, recognition of peptide/MHC-I complexes at the plasma membrane leads to CD8(+) T-lymphocyte responses that clear infections and probably underlie tumor immune surveillance. On the other hand, presentation of self peptides may cause some types of autoimmunity. The peptides that are presented determine the specificity and efficiency of pathogen clearance or, conversely, of immunopathology. In this review we highlight the growing number of peptidases which, as a by-product of their regular activity, can generate peptide epitopes for immune surveillance. These ∼20 peptidases collectively behave as a guerrilla army partnering with the regular proteasome army in generating a variety of peptides for presentation by MHC-I and thus optimally signaling infection. [Mh] Termos MeSH primário: Aminopeptidases/metabolismo Apresentação do Antígeno/genética Células Dendríticas/enzimologia Endopeptidases/metabolismo Exopeptidases/metabolismo Antígenos de Histocompatibilidade Classe I/imunologia [Mh] Termos MeSH secundário: Aminopeptidases/imunologia Citosol/imunologia Citosol/metabolismo Células Dendríticas/citologia Células Dendríticas/imunologia Endopeptidases/imunologia Epitopos de Linfócito T/genética Epitopos de Linfócito T/imunologia Exopeptidases/imunologia Antígenos de Histocompatibilidade Classe I/metabolismo Seres Humanos Peptídeos/imunologia Peptídeos/metabolismo Fagossomos/genética Fagossomos/imunologia Complexo de Endopeptidases do Proteassoma/imunologia Complexo de Endopeptidases do Proteassoma/metabolismo Proteólise Linfócitos T Citotóxicos/citologia Linfócitos T Citotóxicos/imunologia [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW [Nm] Nome de substância: 0 (Epitopes, T-Lymphocyte); 0 (Histocompatibility Antigens Class I); 0 (Peptides); EC 3.4.- (Endopeptidases); EC 3.4.- (Exopeptidases); EC 3.4.11.- (Aminopeptidases); EC 3.4.25.1 (Proteasome Endopeptidase Complex) [Em] Mês de entrada: 1601 [Cu] Atualização por classe: 151027 [Lr] Data última revisão: 151027 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 150527 [St] Status: MEDLINE

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[PMID]: 25869813 [Au] Autor: Kim JA; Park JH; Lee MA; Lee HJ; Park SJ; Kim KS; Choi SH; Lee KH [Ad] Endereço: Department of Life Science, Sogang University, Seoul, 121-742, South Korea. [Ti] Título: Stationary-phase induction of vvpS expression by three transcription factors: repression by LeuO and activation by SmcR and CRP. [So] Source: Mol Microbiol;97(2):330-46, 2015 Jul. [Is] ISSN: 1365-2958 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: An exoprotease of Vibrio vulnificus, VvpS, exhibits an autolytic function during the stationary phase. To understand how vvpS expression is controlled, the regulators involved in vvpS transcription and their regulatory mechanisms were investigated. LeuO was isolated in a ligand-fishing experiment, and experiments using a leuO-deletion mutant revealed that LeuO represses vvpS transcription. LeuO bound the extended region including LeuO-binding site (LBS)-I and LBS-II. Further screening of additional regulators revealed that SmcR and cyclic adenosine monophosphate-receptor protein (CRP) play activating roles in vvpS transcription. SmcR and CRP bound the regions overlapping LBS-I and -II, respectively. In addition, the LeuO occupancy of LBS-I and LBS-II was competitively exchanged by SmcR and CRP, respectively. To examine the mechanism of stationary-phase induction of vvpS expression, in vivo levels of three transcription factors were monitored. Cellular level of LeuO was maximal at exponential phase, while those of SmcR and CRP were maximal at stationary phase and relatively constant after the early-exponential phase, respectively. Thus, vvpS transcription was not induced during the exponential phase by high cellular content of LeuO. When entering the stationary phase, however, LeuO content was significantly reduced and repression by LeuO was relieved through simultaneous binding of SmcR and CRP to LBS-I and -II, respectively. [Mh] Termos MeSH primário: Exopeptidases/biossíntese Fatores de Transcrição/metabolismo Vibrio vulnificus/metabolismo [Mh] Termos MeSH secundário: Proteínas de Bactérias/metabolismo Indução Enzimática Exopeptidases/genética Exopeptidases/metabolismo Regulação Bacteriana da Expressão Gênica Regulação Enzimológica da Expressão Gênica Ligação Proteica Serina Proteases/biossíntese Serina Proteases/genética Serina Proteases/metabolismo Vibrio vulnificus/enzimologia Vibrio vulnificus/genética Vibrio vulnificus/crescimento & desenvolvimento [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Bacterial Proteins); 0 (Transcription Factors); EC 3.4.- (Exopeptidases); EC 3.4.- (Serine Proteases) [Em] Mês de entrada: 1604 [Cu] Atualização por classe: 150707 [Lr] Data última revisão: 150707 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 150415 [St] Status: MEDLINE [do] DOI: 10.1111/mmi.13028

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[PMID]: 25138068 [Au] Autor: Liang P; He L; Xu Y; Chen X; Huang Y; Ren M; Liang C; Li X; Xu J; Lu G; Yu X [Ad] Endereço: Department of Pathogen Biology, Hainan Medical College, Haikou, Hainan, 571199, China. [Ti] Título: Identification, immunolocalization, and characterization analyses of an exopeptidase of papain superfamily, (cathepsin C) from Clonorchis sinensis. [So] Source: Parasitol Res;113(10):3621-9, 2014 Oct. [Is] ISSN: 1432-1955 [Cp] País de publicação: Germany [La] Idioma: eng [Ab] Resumo: Cathepsin C is an important exopeptidase of papain superfamily and plays a number of great important roles during the parasitic life cycle. The amino acid sequence of cathepsin C from Clonorchis sinensis (C. sinensis) showed 54, 53, and 49% identities to that of Schistosoma japonicum, Schistosoma mansoni, and Homo sapiens, respectively. Phylogenetic analysis utilizing the sequences of papain superfamily of C. sinensis demonstrated that cathepsin C and cathepsin Bs came from a common ancestry. Cathepsin C of C. sinensis (Cscathepsin C) was identified as an excretory/secretory product by Western blot analysis. The results of transcriptional level and translational level of Cscathepsin C at metacercaria stage were higher than that at adult worms. Immunolocalization analysis indicated that Cscathepsin C was specifically distributed in the suckers (oral sucker and ventral sucker), eggs, vitellarium, intestines, and testis of adult worms. In the metacercaria, it was mainly detected on the cyst wall and excretory bladder. Combining with the results mentioned above, it implies that Cscathepsin C may be an essential proteolytic enzyme for proteins digestion of hosts, nutrition assimilation, and immune invasion of C. sinensis. Furthermore, it may be a potential diagnostic antigen and drug target against C. sinensis infection. [Mh] Termos MeSH primário: Catepsina C/genética Clonorquíase/parasitologia Clonorchis sinensis/enzimologia [Mh] Termos MeSH secundário: Motivos de Aminoácidos Sequência de Aminoácidos Animais Anticorpos Anti-Helmínticos/imunologia Catepsina C/química Catepsina C/metabolismo Gatos Clonagem Molecular Clonorchis sinensis/genética Clonorchis sinensis/imunologia Biologia Computacional Cyprinidae/parasitologia Exopeptidases/química Exopeptidases/genética Exopeptidases/metabolismo Feminino Seres Humanos Imuno-Histoquímica Masculino Metacercárias Modelos Estruturais Dados de Sequência Molecular Papaína/química Papaína/genética Papaína/metabolismo Filogenia Ratos Alinhamento de Sequência [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Antibodies, Helminth); EC 3.4.- (Exopeptidases); EC 3.4.14.1 (Cathepsin C); EC 3.4.22.2 (Papain) [Em] Mês de entrada: 1510 [Cu] Atualização por classe: 171007 [Lr] Data última revisão: 171007 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 140821 [St] Status: MEDLINE [do] DOI: 10.1007/s00436-014-4027-1

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[PMID]: 24827749 [Au] Autor: Sakamoto Y; Suzuki Y; Iizuka I; Tateoka C; Roppongi S; Fujimoto M; Inaka K; Tanaka H; Masaki M; Ohta K; Okada H; Nonaka T; Morikawa Y; Nakamura KT; Ogasawara W; Tanaka N [Ad] Endereço: 1] School of Pharmacy, Iwate Medical University, 2-1-1 Nishitokuta, Yahaba, Iwate 028-3694, JAPAN [2]. [Ti] Título: S46 peptidases are the first exopeptidases to be members of clan PA. [So] Source: Sci Rep;4:4977, 2014 May 15. [Is] ISSN: 2045-2322 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: The dipeptidyl aminopeptidase BII (DAP BII) belongs to a serine peptidase family, S46. The amino acid sequence of the catalytic unit of DAP BII exhibits significant similarity to those of clan PA endopeptidases, such as chymotrypsin. However, the molecular mechanism of the exopeptidase activity of family S46 peptidase is unknown. Here, we report crystal structures of DAP BII. DAP BII contains a peptidase domain including a typical double ß-barrel fold and previously unreported α-helical domain. The structures of peptide complexes revealed that the α-helical domain covers the active-site cleft and the side chain of Asn330 in the domain forms hydrogen bonds with the N-terminus of the bound peptide. These observations indicate that the α-helical domain regulates the exopeptidase activity of DAP BII. Because S46 peptidases are not found in mammals, we expect that our study will be useful for the design of specific inhibitors of S46 peptidases from pathogens. [Mh] Termos MeSH primário: Dipeptidil Peptidases e Tripeptidil Peptidases/química Exopeptidases/química [Mh] Termos MeSH secundário: Sequência de Aminoácidos Catálise Domínio Catalítico Cristalografia por Raios X/métodos Ligações de Hidrogênio Dados de Sequência Molecular Estrutura Secundária de Proteína Estrutura Terciária de Proteína Especificidade por Substrato [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: EC 3.4.- (Exopeptidases); EC 3.4.14.- (Dipeptidyl-Peptidases and Tripeptidyl-Peptidases); EC 3.4.14.- (dipeptidyl aminopeptidase B) [Em] Mês de entrada: 1408 [Cu] Atualização por classe: 170220 [Lr] Data última revisão: 170220 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 140516 [St] Status: MEDLINE [do] DOI: 10.1038/srep04977

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[PMID]: 24643449 [Au] Autor: Vilhauer L; Jervis J; Ray WK; Helm RF [Ad] Endereço: Department of Biochemistry, Virginia Tech, 143 Life Sciences 1, Blacksburg, VA, 24061-0910, USA. [Ti] Título: The exo-proteome and exo-metabolome of Nostoc punctiforme (Cyanobacteria) in the presence and absence of nitrate. [So] Source: Arch Microbiol;196(5):357-67, 2014 May. [Is] ISSN: 1432-072X [Cp] País de publicação: Germany [La] Idioma: eng [Ab] Resumo: The ability of nitrogen-fixing filamentous Cyanobacteria to adapt to multiple environments comes in part from assessing and responding to external stimuli, an event that is initiated in the extracellular milieu. While it is known that these organisms produce numerous extracellular substances, little work has been done to characterize both the metabolites and proteins present under standard laboratory growth conditions. We have assessed the extracellular milieu of Nostoc punctiforme when grown in liquid culture in the presence and absence of a nitrogen source (nitrate). The extracellular proteins identified were enriched in integrin ß-propellor domains and calcium-binding sites with sequences unique to N. punctiforme, supporting a role for extracellular proteins in modulating species-specific recognition and behavior processes. Extracellular proteases are present and active under both conditions, with the cells grown with nitrate having a higher activity when normalized to chlorophyll levels. The released metabolites are enriched in peptidoglycan-derived tetrasaccharides, with higher levels in nitrate-free media. [Mh] Termos MeSH primário: Metaboloma Nitratos/metabolismo Nostoc/metabolismo Proteoma/metabolismo [Mh] Termos MeSH secundário: Meios de Cultura Exopeptidases/metabolismo Nostoc/crescimento & desenvolvimento Peptidoglicano/química [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 0 (Culture Media); 0 (Nitrates); 0 (Peptidoglycan); 0 (Proteome); EC 3.4.- (Exopeptidases) [Em] Mês de entrada: 1405 [Cu] Atualização por classe: 140416 [Lr] Data última revisão: 140416 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 140320 [St] Status: MEDLINE [do] DOI: 10.1007/s00203-014-0974-2

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[PMID]: 24157613 [Au] Autor: Zhou J; Xu X; Liu X; Li H; Nie Z; Qing M; Huang Y; Yao S [Ad] Endereço: State Key Laboratory of Chemo/Biosensing and Chemometrics, College of Chemistry and Chemical Engineering, Hunan University, Changsha 410082, PR China. [Ti] Título: A gold nanoparticles colorimetric assay for label-free detection of protein kinase activity based on phosphorylation protection against exopeptidase cleavage. [So] Source: Biosens Bioelectron;53:295-300, 2014 Mar 15. [Is] ISSN: 1873-4235 [Cp] País de publicação: England [La] Idioma: eng [Ab] Resumo: Protein kinases are significant regulators in the cell signaling pathways, and it is still greatly desirable to achieve simple and quick kinase detection. Herein, we present a novel colorimetric gold nanoparticles (AuNPs)/peptide platform for probing the activity and inhibition of protein kinases based on phosphorylation-induced suppression of carboxypeptidase Y (CPY) cleavage. This AuNPs/peptide platform can easily monitor the kinase activity by a UV-vis spectrometer or even by the naked eye. The feasibility of the method has been demonstrated by sensitive measurement of the cAMP-dependent protein kinase (PKA) activity with a low detection limit of 0.232 mU/µL and assessment of kinase inhibition by H-89 with an IC50 value of 18.13 nM. The assay was also successfully put into practice for the detection of kinase activity in cell lysate. Because of its label-free, homogenous and colorimetric merits, the proposed assay presents great potential in high-throughput screening for kinase-targeted drug discovery. [Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos Colorimetria/métodos Proteínas Quinases/isolamento & purificação [Mh] Termos MeSH secundário: Exopeptidases/química Ouro/química Seres Humanos Limite de Detecção Nanopartículas Metálicas/química Fosforilação Proteínas Quinases/química [Pt] Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T [Nm] Nome de substância: 7440-57-5 (Gold); EC 2.7.- (Protein Kinases); EC 3.4.- (Exopeptidases) [Em] Mês de entrada: 1407 [Cu] Atualização por classe: 131126 [Lr] Data última revisão: 131126 [Sb] Subgrupo de revista: IM [Da] Data de entrada para processamento: 131026 [St] Status: MEDLINE

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