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[PMID]:28468828
[Au] Autor:Essalmani R; Susan-Resiga D; Guillemot J; Kim W; Sachan V; Awan Z; Chamberland A; Asselin MC; Ly K; Desjardins R; Day R; Prat A; Seidah NG
[Ad] Endereço:From the Laboratories of Biochemical Neuroendocrinology, Institut de Recherches Cliniques de Montréal, University of Montreal, Montreal, Quebec H2W 1R7, Canada and.
[Ti] Título:Thrombin activation of protein C requires prior processing by a liver proprotein convertase.
[So] Source:J Biol Chem;292(25):10564-10573, 2017 06 23.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein C, a secretory vitamin K-dependent anticoagulant serine protease, inactivates factors Va/VIIIa. It is exclusively synthesized in liver hepatocytes as an inactive zymogen (proprotein C). In humans, thrombin cleavage of the propeptide at PR ↓ results in activated protein C (APC; residues 222-461). However, the propeptide is also cleaved by a furin-like proprotein convertase(s) (PCs) at K SHL ↓ (underlined basic residues critical for the recognition by PCs), but the order of cleavage is unknown. Herein, we present evidence that at the surface of COS-1 cells, mouse proprotein C is first cleaved by the convertases furin, PC5/6A, and PACE4. In mice, this cleavage occurs at the equivalent site, K KIL ↓, and requires the presence of Arg at P1 and a combination of two other basic residues at either P2 (Lys ), P6 (Arg ), or P8 (Lys ) positions. Notably, the thrombin-resistant R221A mutant is still cleaved by these PCs, revealing that convertase cleavage can precede thrombin activation. This conclusion was supported by the fact that the APC-specific activity in the medium of COS-1 cells is exclusively dependent on prior cleavage by the convertases, because both R198A and R221A lack protein C activity. Primary cultures of hepatocytes derived from wild-type or hepatocyte-specific furin, PC5/6, or complete PACE4 knock-out mice suggested that the cleavage of overexpressed proprotein C is predominantly performed by furin intracellularly and by all three proprotein convertases at the cell surface. Indeed, plasma analyses of single-proprotein convertase-knock-out mice showed that loss of the convertase furin or PC5/6 in hepatocytes results in a ∼30% decrease in APC levels, with no significant contribution from PACE4. We conclude that prior convertase cleavage of protein C in hepatocytes is critical for its thrombin activation.
[Mh] Termos MeSH primário: Hepatócitos/enzimologia
Fígado/enzimologia
Pró-Proteína Convertase 5/metabolismo
Proteína C/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Animais
Células COS
Cercopithecus aethiops
Ativação Enzimática/fisiologia
Células Hep G2
Seres Humanos
Camundongos
Camundongos Knockout
Mutação de Sentido Incorreto
Pró-Proteína Convertase 5/genética
Pró-Proteína Convertases/genética
Pró-Proteína Convertases/metabolismo
Proteína C/genética
Serina Endopeptidases/genética
Serina Endopeptidases/metabolismo
Trombina/genética
Trombina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protein C); EC 3.4.21.- (PCSK6 protein, human); EC 3.4.21.- (Pcsk6 protein, mouse); EC 3.4.21.- (Proprotein Convertase 5); EC 3.4.21.- (Proprotein Convertases); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.5 (Thrombin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.770040


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[PMID]:26283733
[Au] Autor:Kim W; Zekas E; Lodge R; Susan-Resiga D; Marcinkiewicz E; Essalmani R; Mihara K; Ramachandran R; Asahchop E; Gelman B; Cohen ÉA; Power C; Hollenberg MD; Seidah NG
[Ad] Endereço:Laboratory of Biochemical Neuroendocrinology, Clinical Research Institute of Montreal, University of Montreal, Montreal, Quebec, Canada.
[Ti] Título:Neuroinflammation-Induced Interactions between Protease-Activated Receptor 1 and Proprotein Convertases in HIV-Associated Neurocognitive Disorder.
[So] Source:Mol Cell Biol;35(21):3684-700, 2015 Nov.
[Is] ISSN:1098-5549
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The proprotein convertases (PCs) furin, PC5, PACE4, and PC7 cleave secretory proteins after basic residues, including the HIV envelope glycoprotein (gp160) and Vpr. We evaluated the abundance of PC mRNAs in postmortem brains of individuals exhibiting HIV-associated neurocognitive disorder (HAND), likely driven by neuroinflammation and neurotoxic HIV proteins (e.g., envelope and Vpr). Concomitant with increased inflammation-related gene expression (interleukin-1ß [IL-1ß]), the mRNA levels of the above PCs are significantly increased, together with those of the proteinase-activated receptor 1 (PAR1), an inflammation-associated receptor that is cleaved by thrombin at ProArg41↓ (where the down arrow indicates the cleavage location), and potentially by PCs at Arg41XXXXArg46↓. The latter motif in PAR1, but not its R46A mutant, drives its interactions with PCs. Indeed, PAR1 upregulation leads to the inhibition of membrane-bound furin, PC5B, and PC7 and inhibits gp160 processing and HIV infectivity. Additionally, a proximity ligation assay revealed that furin and PC7 interact with PAR1. Reciprocally, increased furin expression reduces the plasma membrane abundance of PAR1 by trapping it in the trans-Golgi network. Furthermore, soluble PC5A/PACE4 can target/disarm cell surface PAR1 through cleavage at Arg46↓. PACE4/PC5A decreased calcium mobilization induced by thrombin stimulation. Our data reveal a new PC-PAR1-interaction pathway, which offsets the effects of HIV-induced neuroinflammation, viral infection, and potentially the development of HAND.
[Mh] Termos MeSH primário: Encéfalo/patologia
Infecções por HIV/complicações
Inflamação/complicações
Transtornos Neurocognitivos/complicações
Pró-Proteína Convertases/metabolismo
Mapas de Interação de Proteínas
Receptor PAR-1/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Encéfalo/metabolismo
Linhagem Celular
Furina/genética
Regulação da Expressão Gênica
Proteína gp160 do Envelope de HIV/metabolismo
Infecções por HIV/genética
Infecções por HIV/metabolismo
Infecções por HIV/patologia
HIV-1/fisiologia
Interações Hospedeiro-Patógeno
Seres Humanos
Inflamação/genética
Inflamação/metabolismo
Inflamação/patologia
Camundongos
Dados de Sequência Molecular
Transtornos Neurocognitivos/genética
Transtornos Neurocognitivos/metabolismo
Transtornos Neurocognitivos/patologia
Pró-Proteína Convertase 5/análise
Pró-Proteína Convertase 5/metabolismo
Pró-Proteína Convertases/análise
Pró-Proteína Convertases/genética
RNA Mensageiro/análise
RNA Mensageiro/genética
Receptor PAR-1/análise
Receptor PAR-1/genética
Serina Endopeptidases/análise
Serina Endopeptidases/genética
Serina Endopeptidases/metabolismo
Subtilisinas/análise
Subtilisinas/genética
Subtilisinas/metabolismo
Trombina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (HIV Envelope Protein gp160); 0 (RNA, Messenger); 0 (Receptor, PAR-1); EC 3.4.21.- (PCSK6 protein, human); EC 3.4.21.- (PCSK7 protein, human); EC 3.4.21.- (Proprotein Convertase 5); EC 3.4.21.- (Proprotein Convertases); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.- (Subtilisins); EC 3.4.21.5 (Thrombin); EC 3.4.21.75 (Furin)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:170308
[Lr] Data última revisão:
170308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150819
[St] Status:MEDLINE
[do] DOI:10.1128/MCB.00764-15


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[PMID]:26095298
[Au] Autor:Garten W; Braden C; Arendt A; Peitsch C; Baron J; Lu Y; Pawletko K; Hardes K; Steinmetzer T; Böttcher-Friebertshäuser E
[Ad] Endereço:Institute of Virology, Philipps University Marburg, Hans-Meerwein-Strasse 2, 35043 Marburg, Germany. Electronic address: garten@staff.uni-marburg.de.
[Ti] Título:Influenza virus activating host proteases: Identification, localization and inhibitors as potential therapeutics.
[So] Source:Eur J Cell Biol;94(7-9):375-83, 2015 Jul-Sep.
[Is] ISSN:1618-1298
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Cellular proteases are reponsible for activation of influenza virus hemagglutinin (HA) in epithelial tissues of the respiratory tract. The trans-Golgi network (TGN) is the main subcellular compartment where HA cleavage occurs during its biosynthesis. The proteolytic HA cleavage is an indispensable prerequisite for the fusion of viral with endosomal membrane and the delivery of the virus genome into the cell. Both, the structure and accessibility of the HA cleavage site determine the responsible host protease(s) for cutting. Most influenza virus strains contain a HA sequence with a single arginine at the cleavage site suitable for processing by the trypsin-like serine proteases human airway trypsin-like protease (HAT) and transmembrane protease serine 2 (TMPRSS2), albeit a minority of viruses possesses HA cleavage site motifs that are processed by other proteases. TMPRSS2-deficient mice demonstrated the relevance of TMPRSS2 for pneumotropism and pathogenicity of H1N1 and H7N9 virus infections. In contrast, H3N2 virus infections are promoted by an additional not yet identified protease. Highly pathogenic avian H5 and H7 viruses are characterized by an enlarged cleavage site loop containing a multibasic amino acid motif, where the eukaryotic subtilases furin or PC5/6 cleave. Their ubiquitous presence in the organism allows a systemic virus infection. Peptidomimetic inhibitors derived from the HA cleavage site inhibit the HA-activating proteases and thus virus propagation.
[Mh] Termos MeSH primário: Glicoproteínas de Hemaglutininação de Vírus da Influenza/metabolismo
Vírus da Influenza A Subtipo H1N1/patogenicidade
Vírus da Influenza A Subtipo H7N9/patogenicidade
Serina Endopeptidases/genética
Serina Endopeptidases/metabolismo
Serina Proteases/metabolismo
[Mh] Termos MeSH secundário: Animais
Furina/metabolismo
Glicoproteínas de Hemaglutininação de Vírus da Influenza/biossíntese
Seres Humanos
Vírus da Influenza A Subtipo H3N2/patogenicidade
Influenza Humana/patologia
Influenza Humana/virologia
Camundongos
Infecções por Orthomyxoviridae/patologia
Infecções por Orthomyxoviridae/virologia
Pró-Proteína Convertase 5/metabolismo
Mucosa Respiratória/virologia
Rede trans-Golgi/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Hemagglutinin Glycoproteins, Influenza Virus); EC 3.4.- (Serine Proteases); EC 3.4.21.- (Proprotein Convertase 5); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.- (TMPRSS2 protein, human); EC 3.4.21.- (TMPRSS2 protein, mouse); EC 3.4.21.- (human airway trypsin-like protease); EC 3.4.21.75 (Furin)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:150825
[Lr] Data última revisão:
150825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150623
[St] Status:MEDLINE


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[PMID]:26077903
[Au] Autor:Heng S; Paule SG; Li Y; Rombauts LJ; Vollenhoven B; Salamonsen LA; Nie G
[Ad] Endereço:*Implantation and Placental Development Laboratory, Centre for Reproductive Health, Hudson Institute of Medical Research, Clayton, Victoria, Australia; Department of Molecular and Translational Sciences and Department of Obstetrics and Gynaecology, Monash University, Clayton, Victoria, Australia; Wo
[Ti] Título:Posttranslational removal of α-dystroglycan N terminus by PC5/6 cleavage is important for uterine preparation for embryo implantation in women.
[So] Source:FASEB J;29(9):4011-22, 2015 Sep.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Embryo implantation requires a healthy embryo and a receptive endometrium (inner lining of the uterus); endometrial receptivity acquisition involves considerable epithelial surface remodeling. Dystroglycan (DG), a large cell surface glycoprotein, consists of α- and ß-subunits; ß-DG anchors within the plasma membrane whereas α-DG attaches extracellularly to ß-DG. The glycosylated central α-DG mediates adhesion, but it is obstructed by its large N terminus (α-DG-N); α-DG-N removal enables DG's adhesive function. We demonstrate here that full-length α-DG in the human endometrial epithelium is a barrier for embryo attachment and that removal of α-DG-N by proprotein convertase 5/6 (PC6; a protease critical for implantation) regulates receptivity. This was evidenced by: 1) α-DG contains a PC6-cleavage site near α-DG-N, and PC6 cleaves a peptide harboring such a site; 2) PC6 knockdown reduces α-DG-N removal from endometrial epithelial cell surface and blastocyst adhesion; 3) mutating the PC6-cleavage site prevents α-DG-N removal, causing cell surface retention of full-length α-DG and loss of adhesiveness; 4) α-DG-N is removed from endometrial tissue in vivo for receptivity and uterine fluid α-DG-N reflects tissue removal and receptivity. We thus identified α-DG-N removal as an important posttranslational control of endometrial receptivity and uterine fluid α-DG-N as a potential biomarker for receptivity in women.
[Mh] Termos MeSH primário: Distroglicanas/metabolismo
Implantação do Embrião/fisiologia
Endométrio/metabolismo
Pró-Proteína Convertase 5/metabolismo
Processamento de Proteína Pós-Traducional/fisiologia
Proteólise
[Mh] Termos MeSH secundário: Blastocisto/citologia
Blastocisto/metabolismo
Linhagem Celular
Distroglicanas/genética
Endométrio/citologia
Células Epiteliais/citologia
Células Epiteliais/metabolismo
Epitélio/metabolismo
Feminino
Seres Humanos
Pró-Proteína Convertase 5/genética
Estrutura Terciária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DAG1 protein, human); 146888-27-9 (Dystroglycans); EC 3.4.21.- (Proprotein Convertase 5)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:150902
[Lr] Data última revisão:
150902
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150617
[St] Status:MEDLINE
[do] DOI:10.1096/fj.14-269456


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[PMID]:26055999
[Au] Autor:Nakamura Y; Kikugawa S; Seki S; Takahata M; Iwasaki N; Terai H; Matsubara M; Fujioka F; Inagaki H; Kobayashi T; Kimura T; Kurahashi H; Kato H
[Ad] Endereço:Department of Orthopaedic Surgery, Shinshu University School of Medicine, Matsumoto, Japan. yxn14@aol.jp.
[Ti] Título:PCSK5 mutation in a patient with the VACTERL association.
[So] Source:BMC Res Notes;8:228, 2015 Jun 09.
[Is] ISSN:1756-0500
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The VACTERL association is a typically sporadic, non-random collection of congenital anomalies that includes vertebral defects, anal atresia, cardiac defects, tracheoesophageal fistula with esophageal atresia, renal anomalies, and limb abnormalities. Although several chromosomal aberrations and gene mutations have been reported as disease-causative, these findings have been sparsely replicated to date. CASE PRESENTATION: In the present study, whole exome sequencing of a case with the VACTERL association uncovered a novel frameshift mutation in the PCSK5 gene, which has been reported as one of the causative genes for the VACTERL association. Although this mutation appears potentially pathogenic in its functional aspects, it was also carried by the healthy father. Furthermore, a database survey revealed several other deleterious variants in the PCSK5 gene in the general population. CONCLUSIONS: Further studies are necessary to clarify the etiological role of the PCSK5 mutation in the VACTERL association.
[Mh] Termos MeSH primário: Canal Anal/anormalidades
Esôfago/anormalidades
Mutação da Fase de Leitura
Cardiopatias Congênitas/genética
Rim/anormalidades
Deformidades Congênitas dos Membros/genética
Pró-Proteína Convertase 5/genética
Coluna Vertebral/anormalidades
Traqueia/anormalidades
[Mh] Termos MeSH secundário: Canal Anal/enzimologia
Criança
Análise Mutacional de DNA
Esôfago/enzimologia
Predisposição Genética para Doença
Cardiopatias Congênitas/diagnóstico
Cardiopatias Congênitas/enzimologia
Hereditariedade
Seres Humanos
Rim/enzimologia
Deformidades Congênitas dos Membros/diagnóstico
Deformidades Congênitas dos Membros/enzimologia
Masculino
Linhagem
Fenótipo
Coluna Vertebral/enzimologia
Traqueia/enzimologia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.4.21.- (PCSK5 protein, human); EC 3.4.21.- (Proprotein Convertase 5)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150617
[Lr] Data última revisão:
150617
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150610
[St] Status:MEDLINE
[do] DOI:10.1186/s13104-015-1166-0


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[PMID]:25554488
[Au] Autor:Heng S; Dynon K; Li Y; Edgell T; Walton K; Rombauts LJ; Vollenhoven B; Nie G
[Ad] Endereço:Implantation and Placental Development Laboratory, Centre for Reproductive Health, MIMR-PHI Institute of Medical Research, Clayton, Victoria 3168, Australia; Monash University, Clayton, Victoria 3800, Australia.
[Ti] Título:Development of a high-throughput assay for human proprotein convertase 5/6 for detecting uterine receptivity.
[So] Source:Anal Biochem;475:14-21, 2015 Apr 15.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Embryo implantation requires a healthy embryo and a receptive uterus. In women, the inner lining of the uterus, the endometrium, remains in a hostile state and becomes receptive for embryo implantation for only a short period during each menstrual cycle. Determining endometrial receptivity is vital in in vitro fertilization (IVF) treatment because the timing of embryo transfer needs to be synchronized with endometrial receptivity. We have previously demonstrated that proprotein convertase 5/6A (PC6) is highly expressed in the receptive endometrium and that PC6 is critical for receptivity establishment in women. Furthermore, endometrial PC6 is secreted into the uterine fluid, and levels correlate with receptivity status. Detection of PC6 in uterine fluids, therefore, would provide a nonsurgical assessment of endometrial receptivity. However, to date no assays are available for human PC6. In this study, we produced three PC6 monoclonal antibodies (mAbs) and developed a sandwich enzyme-linked immunosorbent assay (ELISA) for PC6 detection in human uterine fluids. The PC6 mAbs were confirmed to be highly specific to PC6, and the ELISA detected PC6 in human uterine fluids with a significantly higher level during the receptive phase. This newly established PC6 ELISA provides an important tool in the development of noninvasive strategies to detect endometrial receptivity in women.
[Mh] Termos MeSH primário: Anticorpos Monoclonais Murinos/química
Endométrio/enzimologia
Pró-Proteína Convertase 5/metabolismo
[Mh] Termos MeSH secundário: Animais
Implantação do Embrião/fisiologia
Ensaio de Imunoadsorção Enzimática/métodos
Feminino
Seres Humanos
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Monoclonal, Murine-Derived); EC 3.4.21.- (Proprotein Convertase 5)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:150414
[Lr] Data última revisão:
150414
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150103
[St] Status:MEDLINE


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[PMID]:25429785
[Au] Autor:Paule S; Nebl T; Webb AI; Vollenhoven B; Rombauts LJ; Nie G
[Ad] Endereço:Implantation and Placental Development Laboratory, MIMR-PHI Institute of Medical Research, Clayton, Victoria 3168, Australia Monash University, Clayton, Victoria 3168, Australia sarah.paule@mimr-phi.org guiying.nie@mimr-phi.org.
[Ti] Título:Proprotein convertase 5/6 cleaves platelet-derived growth factor A in the human endometrium in preparation for embryo implantation.
[So] Source:Mol Hum Reprod;21(3):262-70, 2015 Mar.
[Is] ISSN:1460-2407
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Establishment of endometrial receptivity is vital for successful embryo implantation. Proprotein convertase 5/6 (referred to as PC6) is up-regulated in the human endometrium specifically at the time of epithelial receptivity. PC6, a serine protease of the proprotein convertase family, plays an important role in converting precursor proteins into their active forms through specific proteolysis. The proform of platelet-derived growth factor A (pro-PDGFA) requires PC cleavage to convert to the active-PDGFA. We investigated the PC6-mediated activation of PDGFA in the human endometrium during the establishment of receptivity. Proteomic analysis identified that the pro-PDGFA was increased in the conditioned medium of HEC1A cells in which PC6 was stably knocked down by small interfering RNA (PC6-siRNA). Western blot analysis demonstrated an accumulation of the pro-PDGFA but a reduction in the active-PDGFA in PC6-siRNA cell lysates and medium compared with control. PC6 cleavage of pro-PDGFA was further confirmed in vitro by incubation of recombinant pro-PDGFA with PC6. Immunohistochemistry revealed cycle-stage-specific localization of the active-PDGFA in the human endometrium. During the non-receptive phase, the active-PDGFA was barely detectable. In contrast, it was localized specifically to the apical surface of the luminal and glandular epithelium in the receptive phase. Furthermore, the active-PDGFA was detected in uterine lavage with levels being significantly higher in the receptive than the non-receptive phase. We thus identified that the secreted PDGFA may serve as a biomarker for endometrial receptivity. This is also the first study demonstrating that the active-PDGFA localizes to the apical surface of the endometrium during receptivity.
[Mh] Termos MeSH primário: Endométrio/metabolismo
Células Epiteliais/metabolismo
Período Fértil/genética
Fator de Crescimento Derivado de Plaquetas/metabolismo
Pró-Proteína Convertase 5/metabolismo
[Mh] Termos MeSH secundário: Adulto
Linhagem Celular Tumoral
Meios de Cultivo Condicionados/farmacologia
Implantação do Embrião/fisiologia
Embrião de Mamíferos
Endométrio/citologia
Células Epiteliais/citologia
Células Epiteliais/efeitos dos fármacos
Feminino
Período Fértil/metabolismo
Fase Folicular/genética
Fase Folicular/metabolismo
Expressão Gênica
Inativação Gênica
Seres Humanos
Fator de Crescimento Derivado de Plaquetas/genética
Pró-Proteína Convertase 5/antagonistas & inibidores
Pró-Proteína Convertase 5/genética
Proteólise
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Culture Media, Conditioned); 0 (Platelet-Derived Growth Factor); 0 (RNA, Small Interfering); 0 (platelet-derived growth factor A); EC 3.4.21.- (Proprotein Convertase 5)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:150225
[Lr] Data última revisão:
150225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141129
[St] Status:MEDLINE
[do] DOI:10.1093/molehr/gau109


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[PMID]:25350918
[Au] Autor:Lee SN; Lee DH; Lee MG; Yoon JH
[Ad] Endereço:1 Research Center for Human Natural Defense System.
[Ti] Título:Proprotein convertase 5/6a is associated with bone morphogenetic protein-2-induced squamous cell differentiation.
[So] Source:Am J Respir Cell Mol Biol;52(6):749-61, 2015 Jun.
[Is] ISSN:1535-4989
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Squamous metaplasia in airway epithelium is a pathological process arising from abnormal remodeling/repair responses to injury. Proteolytic maturation of many growth and differentiation factors involved in tissue remodeling is controlled by proprotein convertases (PCs). However, the role of these convertases in airway remodeling remains poorly understood. Using a retinoic acid deficiency-induced squamous metaplasia model of cultured human nasal epithelial cells (HNECs), we observed a significant increase in the expression of PC5/6A, a PC member, and bone morphogenetic protein-2 (BMP-2), a candidate substrate for PC5/6A. Specific lentiviral short hairpin RNA-mediated PC5/6A knockdown decreased BMP-2 expression and maturation, decreased expression of squamous cell markers, and increased expression of ciliated cell markers. Decanoyl-Arg-Val-Lys-Arg-chloromethylketone (Dec-RVKR-CMK), a PC inhibitor, and LDN-193189, a BMP receptor inhibitor, suppressed squamous differentiation, promoted mucociliary differentiation, and down-regulated the BMP-2/Smad1/5/8/p38 signaling pathways. Dec-RVKR-CMK also decreased expression of PC5/6A, but not furin, another PC member, suggesting the involvement of PC5/6A in squamous differentiation of HNECs. Overexpression of PC5/6A and BMP-2 in the human nasal epithelial cell line RPMI-2650 demonstrated that PC5/6A can activate BMP-2. Under retinoic acid-sufficient culture conditions for mucociliary differentiation of HNECs, short-term expression of PC5/6A by the adenovirus system and addition of exogenous BMP-2 induced squamous differentiation. Furthermore, PC5/6A and BMP-2 were highly expressed in metaplastic squamous epithelium of human nasal polyps. Taken together, PC5/6A is involved in squamous differentiation of HNECs, possibly through up-regulation of the BMP-2/pSmad1/5/8/p38 signaling pathway, pointing to a potential therapeutic target for the prevention of chronic airway diseases that exhibit squamous metaplasia.
[Mh] Termos MeSH primário: Proteína Morfogenética Óssea 2/fisiologia
Diferenciação Celular
Células Epiteliais/fisiologia
Pró-Proteína Convertase 5/fisiologia
[Mh] Termos MeSH secundário: Células Cultivadas
Seres Humanos
Mucosa Nasal/citologia
Proteínas Smad/metabolismo
Tretinoína/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (BMP2 protein, human); 0 (Bone Morphogenetic Protein 2); 0 (Smad Proteins); 5688UTC01R (Tretinoin); EC 3.4.21.- (Proprotein Convertase 5)
[Em] Mês de entrada:1508
[Cu] Atualização por classe:150602
[Lr] Data última revisão:
150602
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141029
[St] Status:MEDLINE
[do] DOI:10.1165/rcmb.2014-0029OC


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[PMID]:25351954
[Au] Autor:Jang HB; Hwang JY; Park JE; Oh JH; Ahn Y; Kang JH; Park KH; Han BG; Kim BJ; Park SI; Lee HJ
[Ad] Endereço:Center for Biomedical Science, Korea National Institute of Health, Cheongwon-gun, Chungcheongbuk-do, South Korea.
[Ti] Título:Intake levels of dietary polyunsaturated fatty acids modify the association between the genetic variation in PCSK5 and HDL cholesterol.
[So] Source:J Med Genet;51(12):782-8, 2014 Dec.
[Is] ISSN:1468-6244
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: A low serum level of high-density lipoprotein cholesterol (HDL-C) is a risk factor for cardiovascular disease. Proprotein convertase subtilisin/kexin type 5 (PCSK5) modulates HDL-C metabolism through the inactivation of endothelial lipase activity. METHODS: Therefore, we analysed the effects of PCSK5 on HDL-C and investigated the association between genetic variation in PCSK5 and dietary polyunsaturated fatty acids (PUFAs) intakes in Korean adults and children. This population-based study which was conducted in South Korea included 4205 adults (43% male) aged 40-69 years and 1548 children (48.6% boys) aged 8-13 years. Dietary intake was assessed using a semiquantitative food frequency questionnaire in adults and modified 3-day food records in children. RESULTS: After adjustments for age and body mass index, we identified a significant association between SNP rs1029035 of the PCSK5 gene and HDL-C concentrations specifically for men in both populations (adults, p=0.004; children, p=0.003; meta, p=7×10(-4)). Additionally, the interaction between the PCSK5 rs1029035 genotype and dietary polyunsaturated fatty acids intake influenced serum HDL-C concentrations in men (adults, p=0.001; children, p=0.008). The deleterious effect of the C allele on serum HDL-C was present only when dietary PUFA intake was less than the dichotomised median level (adults, p=0.011; children, p=0.001). Serum HDL-C concentrations were decreased in men with the C allele genotype and low consumption of dietary PUFA including n-3 and n-6. CONCLUSION: According to these results, men carrying of the C allele were associated with low HDL-C concentrations and might exert beneficial effects on HDL-C concentrations following consumption of a high-PUFA diet.
[Mh] Termos MeSH primário: HDL-Colesterol/genética
Dieta
Ácidos Graxos Insaturados/metabolismo
Variação Genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Criança
Ingestão de Energia
Feminino
Estudos de Associação Genética
Genótipo
Seres Humanos
Masculino
Meia-Idade
Polimorfismo Genético
Pró-Proteína Convertase 5
República da Coreia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cholesterol, HDL); 0 (Fatty Acids, Unsaturated); EC 3.4.21.- (PCSK5 protein, human); EC 3.4.21.- (Proprotein Convertase 5)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:141118
[Lr] Data última revisão:
141118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141030
[St] Status:MEDLINE
[do] DOI:10.1136/jmedgenet-2014-102670


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[PMID]:24856475
[Au] Autor:Ho H; Li Y; Nie G
[Ad] Endereço:Prince Henry's Institute of Medical Research, Clayton, Victoria 3168, Australia; Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3168, Australia.
[Ti] Título:Inhibition of embryo implantation in mice through vaginal administration of a proprotein convertase 6 inhibitor.
[So] Source:Reprod Biol;14(2):155-9, 2014 Apr.
[Is] ISSN:2300-732X
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:Uterine proprotein convertase 6 (PC6) plays a critical role in embryo implantation in both mice and women. It was hypothesized that inhibiting uterine PC6 could prevent pregnancy. Vaginal administration of a PC6 inhibitor presents the ideal route for local drug delivery. A peptide-based PC6 inhibitor, C-30k-PEG Poly R that was previously shown to have properties of increased vaginal absorption and penetration was tested for its contraceptive potential in mice following vaginal administration. The study demonstrated that this approach could inhibit embryo implantation in some mice (24% completely and 47% partially inhibited).
[Mh] Termos MeSH primário: Implantação do Embrião/efeitos dos fármacos
Polirribonucleotídeos/farmacologia
Pró-Proteína Convertase 5/antagonistas & inibidores
Útero/efeitos dos fármacos
[Mh] Termos MeSH secundário: Administração Intravaginal
Animais
Feminino
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Polyribonucleotides); EC 3.4.21.- (Proprotein Convertase 5)
[Em] Mês de entrada:1502
[Cu] Atualização por classe:151029
[Lr] Data última revisão:
151029
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140527
[St] Status:MEDLINE



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