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[PMID]:28859141
[Au] Autor:Maccarana M; Svensson RB; Knutsson A; Giannopoulos A; Pelkonen M; Weis M; Eyre D; Warman M; Kalamajski S
[Ad] Endereço:Department of Experimental Medical Sciences, Lund University, Lund, Sweden.
[Ti] Título:Asporin-deficient mice have tougher skin and altered skin glycosaminoglycan content and structure.
[So] Source:PLoS One;12(8):e0184028, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The main structural component of connective tissues is fibrillar, cross-linked collagen whose fibrillogenesis can be modulated by Small Leucine-Rich Proteins/Proteoglycans (SLRPs). Not all SLRPs' effects on collagen and extracellular matrix in vivo have been elucidated; one of the less investigated SLRPs is asporin. Here we describe the successful generation of an Aspn-/- mouse model and the investigation of the Aspn-/- skin phenotype. Functionally, Aspn-/- mice had an increased skin mechanical toughness, although there were no structural changes present on histology or immunohistochemistry. Electron microscopy analyses showed 7% thinner collagen fibrils in Aspn-/- mice (not statistically significant). Several matrix genes were upregulated, including collagens (Col1a1, Col1a2, Col3a1), matrix metalloproteinases (Mmp2, Mmp3) and lysyl oxidases (Lox, Loxl2), while lysyl hydroxylase (Plod2) was downregulated. Intriguingly no differences were observed in collagen protein content or in collagen cross-linking-related lysine oxidation or hydroxylation. The glycosaminoglycan content and structure in Aspn-/- skin was profoundly altered: chondroitin/dermatan sulfate was more than doubled and had an altered composition, while heparan sulfate was halved and had a decreased sulfation. Also, decorin and biglycan were doubled in Aspn-/- skin. Overall, asporin deficiency changes skin glycosaminoglycan composition, and decorin and biglycan content, which may explain the changes in skin mechanical properties.
[Mh] Termos MeSH primário: Biglicano/genética
Decorina/genética
Proteínas da Matriz Extracelular/deficiência
Efeito Fundador
Regulação da Expressão Gênica
Pele/metabolismo
[Mh] Termos MeSH secundário: Aminoácido Oxirredutases/genética
Aminoácido Oxirredutases/metabolismo
Animais
Biglicano/metabolismo
Sulfatos de Condroitina/genética
Sulfatos de Condroitina/metabolismo
Colágeno Tipo I/genética
Colágeno Tipo I/metabolismo
Colágeno Tipo III/genética
Colágeno Tipo III/metabolismo
Decorina/metabolismo
Dermatan Sulfato/análogos & derivados
Dermatan Sulfato/genética
Dermatan Sulfato/metabolismo
Matriz Extracelular/genética
Matriz Extracelular/metabolismo
Proteínas da Matriz Extracelular/genética
Feminino
Heparitina Sulfato/genética
Heparitina Sulfato/metabolismo
Sulfato de Ceratano/genética
Sulfato de Ceratano/metabolismo
Masculino
Metaloproteinase 2 da Matriz/genética
Metaloproteinase 2 da Matriz/metabolismo
Metaloproteinase 3 da Matriz/genética
Metaloproteinase 3 da Matriz/metabolismo
Camundongos
Camundongos Knockout
Fenótipo
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/genética
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/metabolismo
Pele/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aspn protein, mouse); 0 (Biglycan); 0 (COL3A1 protein, mouse); 0 (Col1a2 protein, mouse); 0 (Collagen Type I); 0 (Collagen Type III); 0 (Dcn protein, mouse); 0 (Decorin); 0 (Extracellular Matrix Proteins); 0 (collagen type I, alpha 1 chain); 0 (dermatan sulfate chondroitin sulfate); 24967-94-0 (Dermatan Sulfate); 9007-28-7 (Chondroitin Sulfates); 9050-30-0 (Heparitin Sulfate); 9056-36-4 (Keratan Sulfate); EC 1.14.11.4 (Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase); EC 1.14.11.4 (lysyl hydroxylase 2, mouse); EC 1.4.- (Amino Acid Oxidoreductases); EC 1.4.3.- (Loxl2 protein, mouse); EC 3.4.24.17 (Matrix Metalloproteinase 3); EC 3.4.24.17 (Mmp3 protein, mouse); EC 3.4.24.24 (Matrix Metalloproteinase 2); EC 3.4.24.24 (Mmp2 protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170901
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184028


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[PMID]:28279775
[Au] Autor:Neyazi B; Tanrikulu L; Wilkens L; Hartmann C; Stein KP; Dumitru CA; Sandalcioglu IE
[Ad] Endereço:Department of Neurosurgery, Nordstadt Hospital Hannover, Hannover, Germany. Electronic address: belal.neyazi@krh.eu.
[Ti] Título:Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase 2 Expression in Brain Arteriovenous Malformations and its Association with Brain Arteriovenous Malformation Size.
[So] Source:World Neurosurg;102:79-84, 2017 Jun.
[Is] ISSN:1878-8769
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND AND OBJECTIVE: Brain arteriovenous malformations (bAVM) are severe conditions that can cause severe neurologic deficits and mortality. The underlying cellular and molecular mechanisms associated with bAVM growth and rupture remain unclear. The objective of this study was to explore the potential role of PLOD2 (procollagen-lysine, 2-oxoglutarate 5-dioxygenase 2) in the pathophysiology of bAVM. METHODS: Expression and localization of PLOD2 were analyzed on tissue microarrays from patients with bAVM (n = 60) by immunohistochemistry. Correlations between PLOD2 levels and clinical parameters were examined with a Pearson test or Spearman rank correlation coefficient. Comparison between different clinical parameters was performed using a t test or nonparametric Mann-Whitney U test. A Fisher exact test was used for categorical data. RESULTS: PLOD2 was mainly expressed within the tunica media of the blood vessels. High levels of PLOD2 expression correlated with bAVM size (linear regression, P = 0.0083, R =0.158). Small bAVM showed a higher frequency of hemorrhage compared with large ones (P = 0.001). Although PLOD2 was not directly associated with bAVM hemorrhage, high PLOD2-expressing bAVM had a lower frequency of hemorrhage compared with low or medium PLOD2-expressing bAVM (25% vs. 63% and 75%, respectively). CONCLUSIONS: This study reports for the first time the expression of PLOD2 in bAVM and suggests a potential role of PLOD2 in bAVM pathophysiology. These findings contribute to an better understanding of the microenvironment of bAVM and may foster the development of improved therapeutic strategies for this disease.
[Mh] Termos MeSH primário: Encéfalo/enzimologia
Encéfalo/patologia
Malformações Arteriovenosas Intracranianas/patologia
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/metabolismo
[Mh] Termos MeSH secundário: Adulto
Embolização Terapêutica
Feminino
Hemorragia/etiologia
Seres Humanos
Malformações Arteriovenosas Intracranianas/complicações
Masculino
Estudos Retrospectivos
Estatísticas não Paramétricas
Análise Serial de Tecidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.14.11.4 (Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170311
[St] Status:MEDLINE


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[PMID]:28216326
[Au] Autor:Guo HF; Cho EJ; Devkota AK; Chen Y; Russell W; Phillips GN; Yamauchi M; Dalby KN; Kurie JM
[Ad] Endereço:Department of Thoracic/Head and Neck Medical Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX, United States.
[Ti] Título:A scalable lysyl hydroxylase 2 expression system and luciferase-based enzymatic activity assay.
[So] Source:Arch Biochem Biophys;618:45-51, 2017 Mar 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hydroxylysine aldehyde-derived collagen cross-links (HLCCs) accumulate in fibrotic tissues and certain types of cancer and are thought to drive the progression of these diseases. HLCC formation is initiated by lysyl hydroxylase 2 (LH2), an Fe(II) and α-ketoglutarate (αKG)-dependent oxygenase that hydroxylates telopeptidyl lysine residues on collagen. Development of LH2 antagonists for the treatment of these diseases will require a reliable source of recombinant LH2 protein and a non-radioactive LH2 enzymatic activity assay that is amenable to high throughput screens of small molecule libraries. However, LH2 protein generated using E coli- or insect-based expression systems is either insoluble or enzymatically unstable, and the LH2 enzymatic activity assays that are currently available measure radioactive CO released from C-labeled αKG during its conversion to succinate. To address these deficiencies, we have developed a scalable process to purify human LH2 protein from Chinese hamster ovary cell-derived conditioned media samples and a luciferase-based assay that quantifies LH2-dependent conversion of αKG to succinate. These methodologies may be applicable to other Fe(II) and αKG-dependent oxygenase systems.
[Mh] Termos MeSH primário: Ácidos Cetoglutáricos/química
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/biossíntese
[Mh] Termos MeSH secundário: Animais
Células CHO
Carbono/química
Dióxido de Carbono/química
Cromatografia Líquida
Colágeno/química
Cricetulus
Meios de Cultivo Condicionados/química
Glicosilação
Seres Humanos
Luciferases/química
Lisina/química
Proteínas Recombinantes/biossíntese
Ácido Succínico/química
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Culture Media, Conditioned); 0 (Ketoglutaric Acids); 0 (Recombinant Proteins); 142M471B3J (Carbon Dioxide); 7440-44-0 (Carbon); 8ID597Z82X (alpha-ketoglutaric acid); 9007-34-5 (Collagen); AB6MNQ6J6L (Succinic Acid); EC 1.13.12.- (Luciferases); EC 1.14.11.4 (PLOD2 protein, human); EC 1.14.11.4 (Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170930
[Lr] Data última revisão:
170930
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170221
[St] Status:MEDLINE


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[PMID]:27234441
[Au] Autor:Villard C; Eriksson P; Hanemaaijer R; Lindeman JH; Hultgren R
[Ad] Endereço:Department of Molecular Medicine and Surgery, Karolinska Institutet, Stockholm, Sweden; Department of Vascular Surgery, Karolinska University Hospital, Stockholm, Sweden. Electronic address: christina.villard@ki.se.
[Ti] Título:The composition of collagen in the aneurysm wall of men and women.
[So] Source:J Vasc Surg;66(2):579-585.e1, 2017 Aug.
[Is] ISSN:1097-6809
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Loss of vessel wall integrity by degradation is essential for the development of abdominal aortic aneurysm (AAA) and ultimately its rupture. The observed greater rupture rate in women with AAA might be related to gender differences in the biomechanical properties of the aneurysm wall. The aim of the study was to compare the biomechanically important structure of collagen between men and women with AAA. METHODS: Biopsies of the aneurysm walls were obtained during elective open repair of men (n = 14) and women (n = 14) treated for AAA. High-performance liquid chromatography (HPLC), Western blot, messenger RNA expression, and histochemical analyses were performed to assess the cross-linking and the amount and the composition of collagen. RESULTS: There was neither a difference in the thickness of the aneurysm wall, nor in the histological evaluation of the collagen composition between the sexes. Relative collagen content in the aneurysm wall was similar in men and women, as assessed by messenger RNA expression and HPLC. Collagen cross-linking differed between the sexes; women had more lysyl pyridinoline (LP) than men (0.140 vs 0.07; P = .005), resulting in a lower hydroxyl pyridinoline (HP):LP ratio (3.28 vs 8.41; P = .003). There was no difference in messenger RNA and protein expressions of lysyl hydroxylase and lysyl oxidase to associate with the lower HP:LP ratio in women. CONCLUSIONS: The composition of collagen in the aneurysm wall of men and women are in several aspects similar, with the exception of collagen cross-linking, suggesting that the difference in rupture rate between the sexes rather depend on the composition of other vessel wall structures.
[Mh] Termos MeSH primário: Aorta Abdominal/química
Aneurisma da Aorta Abdominal/metabolismo
Ruptura Aórtica/metabolismo
Colágeno/análise
[Mh] Termos MeSH secundário: Aorta Abdominal/patologia
Aneurisma da Aorta Abdominal/genética
Aneurisma da Aorta Abdominal/patologia
Ruptura Aórtica/genética
Ruptura Aórtica/patologia
Fenômenos Biomecânicos
Biópsia
Western Blotting
Cromatografia Líquida de Alta Pressão
Colágeno/genética
Feminino
Disparidades nos Níveis de Saúde
Seres Humanos
Masculino
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/análise
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/genética
Proteína-Lisina 6-Oxidase/análise
Proteína-Lisina 6-Oxidase/genética
RNA Mensageiro/genética
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Fatores Sexuais
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 9007-34-5 (Collagen); EC 1.14.11.4 (Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase); EC 1.4.3.13 (Protein-Lysine 6-Oxidase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160529
[St] Status:MEDLINE


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[PMID]:27803159
[Au] Autor:Chen Y; Guo H; Terajima M; Banerjee P; Liu X; Yu J; Momin AA; Katayama H; Hanash SM; Burns AR; Fields GB; Yamauchi M; Kurie JM
[Ad] Endereço:From the Department of Thoracic/Head and Neck Medical Oncology, University of Texas MD Anderson Cancer Center, Houston, Texas 77030.
[Ti] Título:Lysyl Hydroxylase 2 Is Secreted by Tumor Cells and Can Modify Collagen in the Extracellular Space.
[So] Source:J Biol Chem;291(50):25799-25808, 2016 Dec 09.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lysyl hydroxylase 2 (LH2) catalyzes the hydroxylation of lysine residues in the telopeptides of fibrillar collagens, which leads to the formation of stable collagen cross-links. Recently we reported that LH2 enhances the metastatic propensity of lung cancer by increasing the amount of stable hydroxylysine aldehyde-derived collagen cross-links (HLCCs), which generate a stiffer tumor stroma (Chen, Y., et al. (2015) J. Clin. Invest. 125, 125, 1147-1162). It is generally accepted that LH2 modifies procollagen α chains on the endoplasmic reticulum before the formation of triple helical procollagen molecules. Herein, we report that LH2 is also secreted and modifies collagen in the extracellular space. Analyses of lung cancer cell lines demonstrated that LH2 is present in the cell lysates and the conditioned media in a dimeric, active form in both compartments. LH2 co-localized with collagen fibrils in the extracellular space in human lung cancer specimens and in orthotopic lung tumors generated by injection of a LH2-expressing human lung cancer cell line into nude mice. LH2 depletion in MC3T3 osteoblastic cells impaired the formation of HLCCs, resulting in an increase in the unmodified lysine aldehyde-derived collagen cross-link (LCC), and the addition of recombinant LH2 to the media of LH2-deficient MC3T3 cells was sufficient to rescue HLCC formation in the extracellular matrix. The finding that LH2 modifies collagen in the extracellular space challenges the current view that LH2 functions solely on the endoplasmic reticulum and could also have important implications for cancer biology.
[Mh] Termos MeSH primário: Colágeno/metabolismo
Matriz Extracelular/metabolismo
Proteínas de Neoplasias/metabolismo
Neoplasias/metabolismo
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/metabolismo
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Colágeno/genética
Matriz Extracelular/genética
Seres Humanos
Camundongos
Proteínas de Neoplasias/genética
Neoplasias/genética
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neoplasm Proteins); 9007-34-5 (Collagen); EC 1.14.11.4 (PLOD2 protein, human); EC 1.14.11.4 (Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase); EC 1.14.11.4 (lysyl hydroxylase 2, mouse)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161103
[St] Status:MEDLINE


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[PMID]:27310702
[Au] Autor:Miyamoto K; Seki N; Matsushita R; Yonemori M; Yoshino H; Nakagawa M; Enokida H
[Ad] Endereço:Department of Urology, Graduate School of Medical and Dental Sciences, Kagoshima University, 8-35-1 Sakuragaoka, Kagoshima 890-8520, Japan.
[Ti] Título:Tumour-suppressive miRNA-26a-5p and miR-26b-5p inhibit cell aggressiveness by regulating PLOD2 in bladder cancer.
[So] Source:Br J Cancer;115(3):354-63, 2016 Jul 26.
[Is] ISSN:1532-1827
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Previous studies have revealed that miR-26a-5p and miR-26b-5p act as tumour suppressors in various types of cancer tissues. Here, we aimed to investigate the functional roles of these miRNAs and to identify their regulatory targets in bladder cancer (BC). METHODS: We performed functional assays in BC cells using transfection of mature microRNAs (miRNAs). In silico and luciferase reporter analyses were applied to identify target genes of these miRNAs. The overall survival (OS) of patients with BC was evaluated by the Kaplan-Meier method. RESULTS: miR-26a-5p and miR-26b-5p were significantly downregulated in BC tissues. Restoration of these miRNAs inhibited cell migration and invasion in BC. The gene encoding procollagen-lysine, 2-oxoglutarate 5-dioxygenase 2 (PLOD2), a collagen crosslinking enzyme, was directly regulated by miR-26a-5p and miR-26b-5p. Kaplan-Meier analysis revealed that patients with high PLOD2 expression had significantly shorter OS compared with those with low PLOD2 expression (P=0.0153). CONCLUSIONS: PLOD2, which is associated with the stiffness of the extracellular matrix, was directly regulated by miR-26a-5p and miR-26b-5p and may be a good prognostic marker in patients with BC.
[Mh] Termos MeSH primário: Genes Supressores de Tumor
MicroRNAs/genética
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/genética
Neoplasias da Bexiga Urinária/patologia
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Proliferação Celular
Técnicas de Silenciamento de Genes
Seres Humanos
Invasividade Neoplásica
Metástase Neoplásica
Neoplasias da Bexiga Urinária/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MicroRNAs); EC 1.14.11.4 (PLOD2 protein, human); EC 1.14.11.4 (Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160617
[St] Status:MEDLINE
[do] DOI:10.1038/bjc.2016.179


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[PMID]:27298363
[Au] Autor:Gjaltema RA; van der Stoel MM; Boersema M; Bank RA
[Ad] Endereço:Matrix Accumulation, Tissue Repair, and Inflammation Research Group, University Medical Center Groningen, University of Groningen, 9713 GZ Groningen, The Netherlands; Epigenetic Editing Research Group, Department of Pathology and Medical Biology, University Medical Center Groningen, University of Gr
[Ti] Título:Disentangling mechanisms involved in collagen pyridinoline cross-linking: The immunophilin FKBP65 is critical for dimerization of lysyl hydroxylase 2.
[So] Source:Proc Natl Acad Sci U S A;113(26):7142-7, 2016 06 28.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Collagens are subjected to extensive posttranslational modifications, such as lysine hydroxylation. Bruck syndrome (BS) is a connective tissue disorder characterized at the molecular level by a loss of telopeptide lysine hydroxylation, resulting in reduced collagen pyridinoline cross-linking. BS results from mutations in the genes coding for lysyl hydroxylase (LH) 2 or peptidyl-prolyl cis-trans isomerase (PPIase) FKBP65. Given that the immunophilin FKBP65 does not exhibit LH activity, it is likely that LH2 activity is somehow dependent on FKPB65. In this report, we provide insights regarding the interplay between LH2 and FKBP65. We found that FKBP65 forms complexes with LH2 splice variants LH2A and LH2B but not with LH1 and LH3. Ablating the catalytic activity of FKBP65 or LH2 did not affect complex formation. Both depletion of FKBP65 and inhibition of FKBP65 PPIase activity reduced the dimeric (active) form of LH2 but did not affect the binding of monomeric (inactive) LH2 to procollagen Iα1. Furthermore, we show that LH2A and LH2B cannot form heterodimers with each other but are able to form heterodimers with LH1 and LH3. Collectively, our results indicate that FKBP65 is linked to pyridinoline cross-linking by specifically mediating the dimerization of LH2. Moreover, FKBP65 does not interact with LH1 and LH3, explaining why in BS triple-helical hydroxylysines are not affected. Our results provide a mechanistic link between FKBP65 and the loss of pyridinolines and may hold the key to future treatments for diseases related to collagen cross-linking anomalies, such as fibrosis and cancer.
[Mh] Termos MeSH primário: Aminoácidos/química
Artrogripose/metabolismo
Colágeno Tipo I/química
Colágeno/química
Reagentes para Ligações Cruzadas/química
Osteogênese Imperfeita/metabolismo
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/metabolismo
Proteínas de Ligação a Tacrolimo/metabolismo
[Mh] Termos MeSH secundário: Aminoácidos/metabolismo
Artrogripose/enzimologia
Artrogripose/genética
Colágeno/genética
Colágeno/metabolismo
Colágeno Tipo I/genética
Colágeno Tipo I/metabolismo
Dimerização
Seres Humanos
Osteogênese Imperfeita/enzimologia
Osteogênese Imperfeita/genética
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/genética
Ligação Proteica
Processamento de Proteína Pós-Traducional
Proteínas de Ligação a Tacrolimo/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids); 0 (Collagen Type I); 0 (Cross-Linking Reagents); 0 (collagen type I, alpha 1 chain); 63800-01-1 (pyridinoline); 9007-34-5 (Collagen); EC 1.14.11.4 (PLOD2 protein, human); EC 1.14.11.4 (Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase); EC 5.2.1.- (Tacrolimus Binding Proteins); EC 5.2.1.8 (FKBP10 protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160615
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1600074113


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[PMID]:27233793
[Au] Autor:Amodio G; Sasso E; D'Ambrosio C; Scaloni A; Moltedo O; Franceschelli S; Zambrano N; Remondelli P
[Ad] Endereço:Dipartimento di Scienze Farmaceutiche, Università degli Studi di Salerno, 84034, Fisciano, Salerno, Italy.
[Ti] Título:Identification of a microRNA (miR-663a) induced by ER stress and its target gene PLOD3 by a combined microRNome and proteome approach.
[So] Source:Cell Biol Toxicol;32(4):285-303, 2016 Aug.
[Is] ISSN:1573-6822
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: MicroRNAs (miRs) regulate gene expression to support important physiological functions. Significant evidences suggest that miRs play a crucial role in many pathological events and in the cell response to various stresses. METHODS: With the aim to identify new miRs induced by perturbation of intracellular calcium homeostasis, we analysed miR expression profiles of thapsigargin (TG)-treated cells by microarray. In order to identify miR-663a-regulated genes, we evaluated proteomic changes in miR-663a-overexpressing cells by two-dimensional differential in-gel electrophoresis coupled to mass spectrometric identification of the differentially represented proteins. Microarray and proteomic analyses were supported by biochemical validation. RESULTS: Results of microarray revealed 24 differentially expressed miRs; among them, miR-663a turned out to be by ER stress and under the control of the PERK pathway of the unfolded protein response. Proteomic analysis revealed that PLOD3, which is the gene encoding for collagen-modifying lysyl hydroxylase 3 (LH3), is regulated by miR-663a. Luciferase reporter assays demonstrated that miR-663a indeed reduces LH3 expression by targeting to 3'-UTR of PLOD3 mRNA. Interestingly, miR-663a inhibition of LH3 expression generates reduced extracellular accumulation of type IV collagen, thus suggesting the involvement of miR-663a in modulating collagen 4 secretion in physiological conditions and in response to ER stress. CONCLUSION: The finding of the ER stress-induced PERK-miR-663a pathway may have important implications in the understanding of the molecular mechanisms underlying the function of this miR in normal and/or pathological conditions.
[Mh] Termos MeSH primário: Retículo Endoplasmático/genética
MicroRNAs/genética
MicroRNAs/metabolismo
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/genética
[Mh] Termos MeSH secundário: Carcinoma Hepatocelular/enzimologia
Carcinoma Hepatocelular/genética
Linhagem Celular Tumoral
Retículo Endoplasmático/enzimologia
Regulação da Expressão Gênica
Células HEK293
Células HeLa
Seres Humanos
Neoplasias Hepáticas/enzimologia
Neoplasias Hepáticas/genética
MicroRNAs/biossíntese
Análise de Sequência com Séries de Oligonucleotídeos
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/metabolismo
Proteoma/genética
Proteoma/metabolismo
Estresse Fisiológico/genética
Transcriptoma
eIF-2 Quinase/genética
eIF-2 Quinase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MIRN663 microRNA, human); 0 (MicroRNAs); 0 (Proteome); EC 1.14.11.- (lysyl hydroxylase 3, human); EC 1.14.11.4 (Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase); EC 2.7.11.1 (EIF2AK3 protein, human); EC 2.7.11.1 (eIF-2 Kinase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160529
[St] Status:MEDLINE
[do] DOI:10.1007/s10565-016-9335-z


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[PMID]:27119146
[Au] Autor:Heard ME; Besio R; Weis M; Rai J; Hudson DM; Dimori M; Zimmerman SM; Kamykowski JA; Hogue WR; Swain FL; Burdine MS; Mackintosh SG; Tackett AJ; Suva LJ; Eyre DR; Morello R
[Ad] Endereço:Department of Physiology & Biophysics, University of Arkansas for Medical Sciences, Little Rock, Arkansas, United States of America.
[Ti] Título:Sc65-Null Mice Provide Evidence for a Novel Endoplasmic Reticulum Complex Regulating Collagen Lysyl Hydroxylation.
[So] Source:PLoS Genet;12(4):e1006002, 2016 Apr.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Collagen is a major component of the extracellular matrix and its integrity is essential for connective tissue and organ function. The importance of proteins involved in intracellular collagen post-translational modification, folding and transport was recently highlighted from studies on recessive forms of osteogenesis imperfecta (OI). Here we describe the critical role of SC65 (Synaptonemal Complex 65, P3H4), a leprecan-family member, as part of an endoplasmic reticulum (ER) complex with prolyl 3-hydroxylase 3. This complex affects the activity of lysyl-hydroxylase 1 potentially through interactions with the enzyme and/or cyclophilin B. Loss of Sc65 in the mouse results in instability of this complex, altered collagen lysine hydroxylation and cross-linking leading to connective tissue defects that include low bone mass and skin fragility. This is the first indication of a prolyl-hydroxylase complex in the ER controlling lysyl-hydroxylase activity during collagen synthesis.
[Mh] Termos MeSH primário: Autoantígenos/metabolismo
Colágeno/biossíntese
Retículo Endoplasmático/metabolismo
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/metabolismo
Pró-Colágeno-Prolina Dioxigenase/metabolismo
Processamento de Proteína Pós-Traducional/fisiologia
[Mh] Termos MeSH secundário: Animais
Autoantígenos/genética
Osso e Ossos/fisiologia
Linhagem Celular
Colágeno/metabolismo
Ciclofilinas/metabolismo
Matriz Extracelular/metabolismo
Hidroxilação/genética
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Osteogênese Imperfeita/genética
Osteogênese Imperfeita/patologia
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Autoantigens); 0 (SC65 protein, mouse); 137497-17-7 (cyclophilin B); 9007-34-5 (Collagen); EC 1.14.11.2 (Procollagen-Proline Dioxygenase); EC 1.14.11.4 (Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase); EC 1.14.11.7 (proline, 2-oxoglutarate 3-dioxygenase); EC 5.2.1.- (Cyclophilins)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160428
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006002


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[PMID]:27071056
[Au] Autor:Hu YJ; Imbalzano AN
[Ad] Endereço:Department of Cell and Developmental Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA.
[Ti] Título:Global gene expression profiling of JMJD6- and JMJD4-depleted mouse NIH3T3 fibroblasts.
[So] Source:Sci Data;3:160022, 2016 Apr 12.
[Is] ISSN:2052-4463
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Emerging evidence suggests Jumonji domain-containing proteins are epigenetic regulators in diverse biological processes including cellular differentiation and proliferation. RNA interference-based analyses combined with gene expression profiling can effectively characterize the cellular functions of these enzymes. We found that the depletion of Jumonji domain-containing protein 6 (JMJD6) and its paralog protein Jumonji domain-containing protein 4 (JMJD4) individually by small hairpin RNAs (shRNAs) slowed cell proliferation of mouse NIH3T3 fibroblasts. We subsequently performed gene expression profiling on both JMJD6- and JMJD4-depleted mouse NIH3T3 fibroblasts using the Affymetrix GeneChip Mouse Exon 1.0 ST Array. Here we report the gene profiling datasets along with the experimental procedures. The information can be used to further investigate how JMJD6 and JMJD4 affect gene expression and cellular physiology.
[Mh] Termos MeSH primário: Fibroblastos/fisiologia
Perfilação da Expressão Gênica
Histona Desmetilases com o Domínio Jumonji/genética
Células NIH 3T3
Pró-Colágeno-Lisina 2-Oxoglutarato 5-Dioxigenase/genética
Receptores de Superfície Celular/genética
[Mh] Termos MeSH secundário: Animais
Proliferação Celular/genética
Inativação Gênica
Camundongos
RNA Interferente Pequeno
[Pt] Tipo de publicação:DATASET; JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Ptdsr protein, mouse); 0 (RNA, Small Interfering); 0 (Receptors, Cell Surface); EC 1.14.11.- (Jumonji Domain-Containing Histone Demethylases); EC 1.14.11.4 (JMJD4 protein, mouse); EC 1.14.11.4 (Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160413
[St] Status:MEDLINE
[do] DOI:10.1038/sdata.2016.22



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