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[PMID]: 29523681
[Au] Autor:Chia J; Louber J; Glauser I; Taylor S; Bass GT; Dower SK; Gleeson PA; Verhagen AM
[Ad] Address:CSL Limited, Australia.
[Ti] Title:Half-life extended recombinant coagulation factor IX albumin fusion protein is recycled via the FcRn-mediated pathway.
[So] Source:J Biol Chem;, 2018 Mar 09.
[Is] ISSN:1083-351X
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The neonatal Fc receptor (FcRn) has a pivotal role in albumin and IgG homeostasis. Internalized IgG captured by FcRn under acidic endosomal conditions is recycled to the cell surface where exocytosis and a shift to neutral pH promote extracellular IgG release. Although a similar mechanism is proposed for FcRn-mediated albumin intracellular trafficking and recycling, this pathway is less well defined, but is relevant to the development of therapeutics exploiting FcRn to extend the half-life of short-lived plasma proteins. Recently, a long-acting recombinant coagulation factor IX-albumin fusion protein (rIX-FP) has been approved for the management of hemophilia B. Fusion to albumin potentially enables internalized proteins to engage FcRn and escape lysosomal degradation. In this study, we present for the first time, a detailed investigation of the FcRn-mediated recycling of albumin and the albumin fusion protein rIX-FP. We demonstrate that following internalization via FcRn at low pH, rIX-FP, like albumin, is detectable within the early endosome and rapidly (within 10-15 minutes) traffics into the Rab11+ recycling endosomes, from where it is exported from the cell. Similarly, rIX-FP and albumin taken up by fluid-phase endocytosis at physiological pH, traffics into the Rab11+ recycling compartment in FcRn-positive cells but into the lysosomal compartment in FcRn-negative cells. As expected, recombinant factor IX (without albumin fusion) and an FcRn interaction-defective albumin variant localized to the lysosomal compartments of both FcRn-expressing and non-expressing cells. These results indicate that FcRn-mediated recycling via the albumin moiety is a mechanism for the half-life extension of rIX-FP observed in clinical studies.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:Publisher

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[PMID]: 29350259
[Au] Autor:Zhu X; Zhang J; Wang Q; Fu H; Chang Y; Kong Y; Lv M; Xu L; Liu K; Huang X; Zhang X
[Ad] Address:Peking University People's Hospital, Peking University Institute of Hematology, Beijing, 100044, China.
[Ti] Title:Diminished expression of ß2-GPI is associated with a reduced ability to mitigate complement activation in anti-GPIIb/IIIa-mediated immune thrombocytopenia.
[So] Source:Ann Hematol;97(4):641-654, 2018 Apr.
[Is] ISSN:1432-0584
[Cp] Country of publication:Germany
[La] Language:eng
[Ab] Abstract:Anti-GPIIb/IIIa-mediated complement activation has been reported to be important in the pathogenesis of immune thrombocytopenia (ITP). However, the role of the complement system and the involved regulatory mechanism remain equivocal. Beta2-glycoprotein I (ß2-GPI), known as the main target for antiphospholipid autoantibodies, has been demonstrated as a complement regulator. Here, we investigated the complement-regulatory role of ß2-GPI in anti-GPIIb/IIIa-mediated ITP. Plasma complement activation and enhanced complement activation capacity (CAC) were found in ITP patients with anti-GPIIb/IIIa antibodies in vivo and in vitro. Diminished plasma levels of ß2-GPI were shown in patients of this group, which was inversely correlated with C5b-9 deposition. C5b-9 generation was inhibited by approximate physiological concentrations of ß2-GPI, in a dose-dependent manner. Inhibition of C3a generation by ß2-GPI and the existence of ß2-GPI/C3 complexes in plasma indicated a regulation on the level of the C3 convertase. Furthermore, ß2-GPI down-regulated the phosphorylation levels of c-Jun N-terminal kinase (JNK) and cleavage of BH3 interacting domain death agonist (Bid) and ultimately harbored platelet lysis. Our findings may provide a novel link between diminished plasma levels of ß2-GPI and enhanced complement activation, indicating ß2-GPI as a potential diagnostic biomarker and therapeutic target in the treatment of anti-GPIIb/IIIa-mediated ITP.
[Mh] MeSH terms primary: Complement Activation
Down-Regulation
Isoantibodies/metabolism
Platelet Glycoprotein GPIIb-IIIa Complex/antagonists & inhibitors
Purpura, Thrombocytopenic, Idiopathic/metabolism
beta 2-Glycoprotein I/metabolism
[Mh] MeSH terms secundary: Adult
Aged
Biomarkers/blood
Blood Platelets/immunology
Blood Platelets/metabolism
Blood Platelets/pathology
China/epidemiology
Complement C3-C5 Convertases/metabolism
Complement C3a/metabolism
Female
Humans
Male
Middle Aged
Platelet Glycoprotein GPIIb-IIIa Complex/metabolism
Platelet Glycoprotein GPIb-IX Complex/antagonists & inhibitors
Platelet Glycoprotein GPIb-IX Complex/metabolism
Purpura, Thrombocytopenic, Idiopathic/immunology
Purpura, Thrombocytopenic, Idiopathic/pathology
Purpura, Thrombocytopenic, Idiopathic/physiopathology
Risk
Thrombocytopenia/blood
Thrombocytopenia/immunology
Thrombocytopenia/metabolism
Thrombosis/epidemiology
Thrombosis/etiology
Young Adult
beta 2-Glycoprotein I/blood
[Pt] Publication type:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Name of substance:0 (Biomarkers); 0 (Isoantibodies); 0 (Platelet Glycoprotein GPIIb-IIIa Complex); 0 (Platelet Glycoprotein GPIb-IX Complex); 0 (beta 2-Glycoprotein I); 0 (glycoprotein receptor GPIb-IX); 80295-42-7 (Complement C3a); EC 3.4.21.- (Complement C3-C5 Convertases)
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[Js] Journal subset:IM
[Da] Date of entry for processing:180120
[St] Status:MEDLINE
[do] DOI:10.1007/s00277-017-3215-3

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[PMID]: 28471399
[Au] Autor:Wang CC; Wang YX; Yu NQ; Hu D; Wang XY; Chen XG; Liao YW; Yao J; Wang H; He L; Wu L
[Ad] Address:School of Pharmacy, China Pharmaceutical University, Nanjing 210009, China. w940984614@hotmail.com.
[Ti] Title:Brazilian Green Propolis Extract Synergizes with Protoporphyrin IX-mediated Photodynamic Therapy via Enhancement of Intracellular Accumulation of Protoporphyrin IX and Attenuation of NF-κB and COX-2.
[So] Source:Molecules;22(5), 2017 May 04.
[Is] ISSN:1420-3049
[Cp] Country of publication:Switzerland
[La] Language:eng
[Ab] Abstract:Brazilian green propolis (BGP) is noted for its impressive antitumor effects and has been used as a folk medicine in various cultures for many years. It has been demonstrated that BGP could enhance the cytotoxic effect of cytostatic drugs on tumor cells. Photodynamic therapy (PDT) is a therapeutic approach used against malignant cells. To assess the synergistic effect of BGP extract on protoporphyrin IX (PpIX)-mediated photocytotoxicity, MTT assays were performed using A431 and HeLa cells. TUNEL assay and Annexin V-FITC/PI staining were performed to confirm the induction of apoptosis. Western blotting analysis was performed to examine the pro-apoptotic proteins, anti-apoptotic proteins and inflammation related proteins in A431 cells. Intracellular accumulation of PpIX was examined by flow cytometry. The synergistic effect of BGP extract in PpIX-PDT was also evaluated with a xenograft model. Our findings reveal that BGP extract increased PpIX-mediated photocytotoxicity in A431 and HeLa cells. PpIX-PDT with BGP extract treatment resulted in a decrease in Bcl-xL and an increase in NOXA, Bax and caspase-3 cleavage. The protein expression levels of p-IKKα/ß, NF-κB and COX-2 were upregulated by PpIX-PDT but significantly attenuated when in combination with BGP extract. BGP extract was also found to significantly enhance the intracellular accumulation of PpIX in A431 cells. BGP extract increased PpIX-mediated photocytotoxicity in a xenograft model as well. Our findings provide evidence for a synergistic effect of BGP extract in PpIX-PDT both in vitro and in vivo.
[Mh] MeSH terms primary: Cyclooxygenase 2/metabolism
NF-kappa B/metabolism
Photochemotherapy
Propolis
Protoporphyrins/pharmacology
[Mh] MeSH terms secundary: Animals
Apoptosis/drug effects
Brazil
Cell Line, Tumor
Chromatography, High Pressure Liquid
Drug Synergism
Flow Cytometry
Heterografts
Humans
Mice, Inbred BALB C
Mice, Nude
Protoporphyrins/pharmacokinetics
Spectrophotometry, Ultraviolet
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (NF-kappa B); 0 (Protoporphyrins); 9009-62-5 (Propolis); C2K325S808 (protoporphyrin IX); EC 1.14.99.1 (Cyclooxygenase 2)
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[Js] Journal subset:IM
[Da] Date of entry for processing:170505
[St] Status:MEDLINE

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[PMID]: 29519277
[Au] Autor:Jia H; Shi J; Dong S; Zhang Y; Yu J
[Ad] Address:Department of Anesthesiology, Tianjin Nankai Hospital, Nankai Clinical College of Tianjin Medical University, Tianjin 300100, China. Corresponding author: Yu Jianbo, Email: jianboyu99@sina.com.
[Ti] Title:[Effects of heme oxygenase-1/carbon monoxide pathway on the mitochondrial fusion in rat alveolar epithelial type II cells stimulated by lipopolysaccharide].
[So] Source:Zhonghua Wei Zhong Bing Ji Jiu Yi Xue;30(3):209-213, 2018 Mar.
[Is] ISSN:2095-4352
[Cp] Country of publication:China
[La] Language:chi
[Ab] Abstract:OBJECTIVE: To investigate the effects of heme oxygenase-1/carbon monoxide (HO-1/CO) pathway on mitochondrial fusion in rat alveolar epithelial type II cells (AEC II) stimulated by lipopolysaccharide (LPS). METHODS: Once the cultured in vitro rat AEC II cells line RLE-6TN reached confluency of 85%, they were subcultured and randomly divided into seven groups (n = 5 each). RLE-6TN cells were routinely cultured in control group. The cells in LPS group was stimulated with 10 mg/L LPS to reproduce the model of endotoxin challenge in AECII cells. The cells in carbon monoxide-releasing molecule-2 (CORM-2, in vitro CO release agent) + LPS group (CL group) and Hemin (HO-1 inducer) + LPS group (HL group) were pretreated with 100 µmol/L CORM-2 or 20 µmol/L Hemin for 1 hour, respectively, followed by 10 mg/L LPS stimulation. The cells in zinc protoporphyrin-IX (ZnPP-IX, HO-1 inhibitor) + LPS group (ZL group) was pretreated with 10 µmol/L ZnPP-IX for 0.5 hour followed by 10 mg/L LPS stimulation. The cells in CORM-2 + ZnPP-IX + LPS group (CZL group) and Hemin + ZnPP-IX + LPS group (HZL group) were pretreated with 100 µmol/L CORM-2 or 20 µmol/L Hemin respectively for 1 hour, and other treatments were similar to those previously described in ZL group. At 24 hours after LPS stimulation, interleukin-6 (IL-6) and tumor necrosis factor-α (TNF-α) in the supernatant were determined by enzyme linked immunosorbent assay (ELISA), the protein expressions of HO-1, mitochondrial fusion related proteins 1 and 2 (Mfn1, Mfn2) and optic atrophy 1 (OPA1) were determined by Western Blot. RESULTS: Compared with control group, IL-6 and TNF-α contents in the supernatant were increased, HO-1 protein expression was up-regulated, Mfn1, Mfn2 and OPA1 protein expressions were down-regulated in all treatment groups. Compared with LPS group, IL-6 and TNF-α contents were significantly decreased after CORM-2 or Hemin pretreatment [IL-6 (ng/L): 48.6±3.7, 48.4±3.1 vs. 58.7±2.5; TNF-α (ng/L): 40.7±5.3, 39.4±4.3 vs. 51.8±5.1], the protein expressions of HO-1, Mfn1, Mfn2 and OPA1 were significantly up-regulated (HO-1 protein: 0.873±0.051, 0.839±0.061 vs. 0.671±0.044; Mfn1 protein: 0.673±0.037, 0.654±0.025 vs. 0.568±0.021; Mfn2 protein: 0.676±0.044, 0.683±0.035 vs. 0.571±0.043; OPA1 protein: 0.648±0.031, 0.632±0.031 vs. 0.554±0.032; all P < 0.05); while opposite effects were found after ZnPP-IX preincubation, and there were significant differences in IL-6 and TNF-α contents and protein expressions of HO-1, Mfn1, Mfn2 and OPA1 as compared with those of LPS group [IL-6 (ng/L): 69.8±5.1 vs. 58.7±2.5, TNF-α (ng/L): 61.9±3.3 vs. 51.8±5.1, HO-1 protein: 0.545±0.023 vs. 0.671±0.044, Mfn1 protein: 0.406±0.051 vs. 0.568±0.021, Mfn2 protein: 0.393±0.051 vs. 0.571±0.043, OPA1 protein: 0.372±0.050 vs. 0.554±0.032; all P < 0.05]. There were no significant differences in the parameters mentioned above between HL group and CL group, as well as among LPS, CZL and HZL groups. CONCLUSIONS: HO-1/CO pathway promotes mitochondrial fusion and alleviates inflammatory response in LPS-induced rat AEC II cells.
[Pt] Publication type:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:In-Process
[do] DOI:10.3760/cma.j.issn.2095-4352.2018.03.004

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[PMID]: 29517971
[Au] Autor:Franchini M; Mannucci PM
[Ad] Address:Department of Transfusion Medicine and Haematology, "Carlo Poma" Hospital, Mantua, Italy.
[Ti] Title:Non-factor replacement therapy for haemophilia: a current update.
[So] Source:Blood Transfus;:1-5, 2018 Feb 14.
[Is] ISSN:1723-2007
[Cp] Country of publication:Italy
[La] Language:eng
[Ab] Abstract:One of the most challenging issues facing us in the treatment of haemophilia is the development of alloantibodies against infused factor VIII (FVIII) or factor IX (FIX). Inhibitors render factor replacement therapy ineffective, exposing patients to an unacceptably high risk of morbidity and mortality. Besides the well-known bypassing agents (i.e. activated prothrombin complex concentrate and recombinant activated factor VII) used to treat or prevent bleeding in haemophilia patients with inhibitors, there is growing interest in a new class of therapeutic agents which act by enhancing coagulation (i.e. emicizumab) or inhibiting anticoagulant pathways (i.e. fitusiran and concizumab). This review will focus on these innovative therapies, providing an update on their current stage of clinical development.
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Em] Entry month:1803
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:Publisher
[do] DOI:10.2450/2018.0272-17

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[PMID]: 29431281
[Au] Autor:Wang P; Han J; Wei M; Xu Y; Zhang G; Zhang H; Shi L; Liu X; Hamblin MR; Wang X
[Ad] Address:Institute of Photomedicine, Shanghai Skin Disease Hospital, Tongji University School of Medicine, Shanghai, China.
[Ti] Title:Remodeling of dermal collagen in photoaged skin using low-dose 5-aminolevulinic acid photodynamic therapy occurs via the TGF-ß pathway.
[So] Source:J Biophotonics;, 2018 Feb 12.
[Is] ISSN:1864-0648
[Cp] Country of publication:Germany
[La] Language:eng
[Ab] Abstract:5-Aminolevulinic acid photodynamic therapy (ALA-PDT) is known to be effective in the treatment of photoaged skin. However, the molecular mechanisms still remain elusive. Protoporphyrin IX (PpIX) fluorescence is primarily located in the epidermis while ALA-PDT affects the dermal collagen, presumably by an indirect mechanism. This study aimed to investigate the molecular communication in low-dose ALA-PDT occurring between epidermal keratinocytes and dermal fibroblasts. Western blotting and enzyme-linked immunosorbent assays were performed to evaluate collagen expression and transforming growth factor-ß (TGF-ß) signaling in human keratinocytes and dermal fibroblasts. The impact on fibroblast proliferation was assessed by morphology and proliferating cell nuclear antigen immunofluorescence. Skin biopsies from mice were used to analyze the histological changes in dermal collagen and PpIX distribution. When fibroblasts were co-cultured with keratinocytes treated with low-dose ALA-PDT, collagen synthesis and fibroblast proliferation were enhanced. Low-dose ALA-PDT stimulated TGF-ß1 expression in keratinocytes. Fibroblasts co-cultured with low-dose ALA-PDT treated keratinocytes also showed activation of the TGF-ß pathway. In vivo, PpIX fluorescence was densely distributed in photoaged mouse epidermis while collagen in the mouse dermis underwent remodeling. This study suggests that low-dose ALA-PDT can stimulate keratinocytes to release TGF-ß1, activating the TGF-ß pathway in dermal fibroblasts to remodel collagen in the dermis.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:Publisher
[do] DOI:10.1002/jbio.201700357

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[PMID]: 29273498
[Au] Autor:Hung KL; Meitlis I; Hale M; Chen CY; Singh S; Jackson SW; Miao CH; Khan IF; Rawlings DJ; James RG
[Ad] Address:Center for Immunity and Immunotherapies, Seattle Children's Research Institute, Seattle, Washington, USA.
[Ti] Title:Engineering Protein-Secreting Plasma Cells by Homology-Directed Repair in Primary Human B Cells.
[So] Source:Mol Ther;26(2):456-467, 2018 Feb 07.
[Is] ISSN:1525-0024
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The ability to engineer primary human B cells to differentiate into long-lived plasma cells and secrete a de novo protein may allow the creation of novel plasma cell therapies for protein deficiency diseases and other clinical applications. We initially developed methods for efficient genome editing of primary B cells isolated from peripheral blood. By delivering CRISPR/CRISPR-associated protein 9 (Cas9) ribonucleoprotein (RNP) complexes under conditions of rapid B cell expansion, we achieved site-specific gene disruption at multiple loci in primary human B cells (with editing rates of up to 94%). We used this method to alter ex vivo plasma cell differentiation by disrupting developmental regulatory genes. Next, we co-delivered RNPs with either a single-stranded DNA oligonucleotide or adeno-associated viruses containing homologous repair templates. Using either delivery method, we achieved targeted sequence integration at high efficiency (up to 40%) via homology-directed repair. This method enabled us to engineer plasma cells to secrete factor IX (FIX) or B cell activating factor (BAFF) at high levels. Finally, we show that introduction of BAFF into plasma cells promotes their engraftment into immunodeficient mice. Our results highlight the utility of genome editing in studying human B cell biology and demonstrate a novel strategy for modifying human plasma cells to secrete therapeutic proteins.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:In-Data-Review

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[PMID]: 29235571
[Au] Autor:Forker L; Gaunt P; Sioletic S; Shenjere P; Potter R; Roberts D; Irlam J; Valentine H; Hughes D; Hughes A; Billingham L; Grimer R; Seddon B; Choudhury A; Robinson M; West CML
[Ad] Address:Translational Radiobiology Group, Division of Cancer Sciences, University of Manchester, Manchester Academic Health Science Centre, Christie Hospital NHS Foundation Trust, Wilmslow Road, Manchester M20 4BX, UK.
[Ti] Title:The hypoxia marker CAIX is prognostic in the UK phase III VorteX-Biobank cohort: an important resource for translational research in soft tissue sarcoma.
[So] Source:Br J Cancer;118(5):698-704, 2018 Mar 06.
[Is] ISSN:1532-1827
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:BACKGROUND: Despite high metastasis rates, adjuvant/neoadjuvant systemic therapy for localised soft tissue sarcoma (STS) is not used routinely. Progress requires tailoring therapy to features of tumour biology, which need exploration in well-documented cohorts. Hypoxia has been linked to metastasis in STS and is targetable. This study evaluated hypoxia prognostic markers in the phase III adjuvant radiotherapy VorteX trial. METHODS: Formalin-fixed paraffin-embedded tumour biopsies, fresh tumour/normal tissue and blood were collected before radiotherapy. Immunohistochemistry for HIF-1α, CAIX and GLUT1 was performed on tissue microarrays and assessed by two scorers (one pathologist). Prognostic analysis of disease-free survival (DFS) used Kaplan-Meier and Cox regression. RESULTS: Biobank and outcome data were available for 203 out of 216 randomised patients. High CAIX expression was associated with worse DFS (hazard ratio 2.28, 95% confidence interval: 1.44-3.59, P<0.001). Hypoxia-inducible factor-1α and GLUT1 were not prognostic. Carbonic anhydrase IX remained prognostic in multivariable analysis. CONCLUSIONS: The VorteX-Biobank contains tissue with linked outcome data and is an important resource for research. This study confirms hypoxia is linked to poor prognosis in STS and suggests that CAIX may be the best known marker. However, overlap between single marker positivity was poor and future work will develop an STS hypoxia gene signature to account for tumour heterogeneity.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:In-Data-Review
[do] DOI:10.1038/bjc.2017.430

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[PMID]: 29339356
[Au] Autor:Garlo KG; White WB; Bakris GL; Zannad F; Wilson CA; Kupfer S; Vaduganathan M; Morrow DA; Cannon CP; Charytan DM
[Ad] Address:Division of Cardiometabolic Trials, Baim Institute for Clinical Research, Boston, Massachusetts; kgarlo@bwh.harvard.edu.
[Ti] Title:Kidney Biomarkers and Decline in eGFR in Patients with Type 2 Diabetes.
[So] Source:Clin J Am Soc Nephrol;13(3):398-405, 2018 Mar 07.
[Is] ISSN:1555-905X
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:BACKGROUND AND OBJECTIVES: Biomarkers may improve identification of individuals at risk of eGFR decline who may benefit from intervention or dialysis planning. However, available biomarkers remain incompletely validated for risk stratification and prediction modeling. DESIGN, SETTING, PARTICIPANTS, & MEASUREMENTS: We examined serum cystatin C, urinary kidney injury molecule-1 (uKIM-1), and urinary neutrophil gelatinase-associated lipocalin (UNGAL) in 5367 individuals with type 2 diabetes mellitus and recent acute coronary syndromes enrolled in the Examination of Cardiovascular Outcomes with Alogliptin versus Standard of Care (EXAMINE) trial. Baseline concentrations and 6-month changes in biomarkers were also evaluated. Cox proportional regression was used to assess associations with a 50% decrease in eGFR, stage 5 CKD (eGFR<15 ml/min per 1.73 m ), or dialysis. RESULTS: eGFR decline occurred in 98 patients (1.8%) over a median of 1.5 years. All biomarkers individually were associated with higher risk of eGFR decline ( <0.001). However, when adjusting for baseline eGFR, proteinuria, and clinical factors, only baseline cystatin C (adjusted hazard ratio per 1 SD change, 1.66; 95% confidence interval, 1.41 to 1.96; <0.001) and 6-month change in urinary neutrophil gelatinase-associated lipocalin (adjusted hazard ratio per 1 SD change, 1.07; 95% confidence interval, 1.02 to 1.12; =0.004) independently associated with CKD progression. A base model for predicting kidney function decline with nine standard risk factors had strong discriminative ability (C-statistic 0.93). The addition of baseline cystatin C improved discrimination (C-statistic 0.94), but it failed to reclassify risk categories of individuals with and without eGFR decline. CONCLUSIONS: The addition of cystatin C or biomarkers of tubular injury did not meaningfully improve the prediction of eGFR decline beyond common clinical factors and routine laboratory data in a large cohort of patients with type 2 diabetes and recent acute coronary syndrome. PODCAST: This article contains a podcast at https://www.asn-online.org/media/podcast/CJASN/2018_01_16_CJASNPodcast_18_3_G.mp3.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:In-Data-Review
[do] DOI:10.2215/CJN.05280517

  10 / 25367 MEDLINE  
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[PMID]: 28457516
[Au] Autor:Nakata M; Kasuda S; Yuui K; Kudo R; Hatake K
[Ad] Address:Department of Legal Medicine, Nara Medical University, 840 Shijo-cho, Kashihara, Nara 634-8521, Japan. Electronic address: dc112064@naramed-u.ac.jp.
[Ti] Title:Relevance of hemolysis-induced tissue factor expression on monocytes in soft clot formation in alcohol-containing blood.
[So] Source:Leg Med (Tokyo);25:83-88, 2017 Mar.
[Is] ISSN:1873-4162
[Cp] Country of publication:Ireland
[La] Language:eng
[Ab] Abstract:The fluidity of cadaveric blood is an important characteristic in the post-mortem examination of cases of asphyxial death. Although it is empirically known that soft blood clots are present in cadaveric blood containing alcohol, the relationship between such clots and blood alcohol is unclear. We addressed this issue through in vitro studies using blood collected from healthy volunteers. Assessment of global hemostasis by rotational thromboelastometry revealed that ethanol treatment enhanced the procoagulant activity of whole blood. However, ethanol inhibited epinephrine-induced platelet aggregation, whereas plasma levels of von Willebrand factor and the activity of coagulation factors VIII and IX were unaffected. In contrast, tissue factor (TF) activity was higher in plasma obtained from ethanol-treated whole blood than that in plasma from untreated blood. Ethanol induced hemolysis of red blood cells, and the consequent hemoglobin (Hb) release promoted de novo synthesis of TF in isolated monocytes, as determined by real-time reverse transcription PCR, western blotting, and flow cytometry. However, ethanol itself did not induce TF expression in monocytes. Given that TF activates the extrinsic coagulation pathway and amplifies hemostatic reactions, Hb-induced TF expression in monocytes might contribute to soft blood clot formation.
[Mh] MeSH terms primary: Blood Coagulation/drug effects
Ethanol/blood
Hemolysis
Monocytes/drug effects
Thromboplastin/drug effects
[Mh] MeSH terms secundary: Autopsy
Cadaver
Flow Cytometry
Forensic Medicine
Humans
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:3K9958V90M (Ethanol); 9035-58-9 (Thromboplastin)
[Em] Entry month:1803
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[Js] Journal subset:IM
[Da] Date of entry for processing:170502
[St] Status:MEDLINE


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