Role of monocyte chemoattractant protein-1, tumor necrosis factor-α and interleukin-6 in the control of malignant pleural effusion and survival in patients with primary lung adenocarcinoma

2012 ◽  
Vol 27 (2) ◽  
pp. 118-124 ◽  
Author(s):  
Qian Qian ◽  
Wen-Kui Sun ◽  
Ping Zhan ◽  
Yu Zhang ◽  
Yong Song ◽  
...  
Keyword(s):  
Pleural Effusion ◽  
Lung Adenocarcinoma ◽  
Malignant Pleural Effusion ◽  
Monocyte Chemoattractant Protein 1 ◽  
Monocyte Chemoattractant ◽  
Primary Lung Adenocarcinoma ◽  
Tnf Α ◽  
Factor Α ◽  
Necrosis Factor

This study aimed at assessing the role of monocyte chemoattractant protein-1 (MCP-1), tumor necrosis factor-α (TNF-α) and interleukin-6 (IL-6) in the control of pleural effusion (PE) and survival in patients with primary lung adenocarcinoma. The concentrations of the 3 cytokines were measured in PE from 79 lung adenocarcinoma patients with malignant pleural effusion (MPE) and 23 patients with tuberculosis. Data were correlated with the efficacy of MPE control and patient survival. The level of MCP-1 in PE was significantly higher in patients with lung adenocarcinoma than those with tuberculosis. By contrast, the levels of TNF-α and IL-6 were significantly lower in patients with lung adenocarcinoma than those with tuberculosis. An MCP-1 level greater than 3,187 pg/mL (which was used as a cutoff point) indicated failure to control MPE (odds ratio [OR]=2.82, 95% confidence interval [CI]=1.02–7.82, p=0.04). In multivariate analysis, MCP-1 was confirmed as an independent prognostic factor for progression-free survival (hazard ratio [HR]=2.02, 95% CI=1.24–3.30, p=0.01). The level of MCP-1 in PE appears to be a reliable surrogate marker for evaluating the therapeutic efficacy in the control of MPE and predicting survival in lung adenocarcinoma patients with MPE.

Παθοφυσιολογία της αντίδρασης του ενδοθηλίου μετά από αγγειοπλαστική νεφρικής αρτηρίας

2014 ◽  
Author(s):  
Κυριακή Ταβερναράκη
Keyword(s):  
Adhesion Molecule ◽  
Intercellular Adhesion Molecule ◽  
Vascular Cell Adhesion ◽  
Intercellular Adhesion Molecule 1 ◽  
Monocyte Chemoattractant Protein 1 ◽  
Monocyte Chemoattractant ◽  
Tnf Α ◽  
Factor Α ◽  
Cell Adhesion Molecule 1 ◽  
Necrosis Factor

Σκοπός:Για τη μελέτη του παθοφυσιολογικού μηχανισμού αντίδρασης του τοιχώματος της νεφρικής αρτηρίας που εκλύεται κατά την αγγειοπλαστική με τοποθέτηση stent πραγματοποιήθηκε ποσοτικός προσδιορισμός έξι διαφορετικών παραγόντων φλεγμονής -μεσολαβητών (κυτοκίνες) στον ορό αίματος ασθενών που υποβλήθηκαν σε αυτήν την μέθοδο. Απώτερος σκοπός της μελέτης, μέσω της αξιολόγησης των διαφορών στις συγκεντρώσεις των μεσολαβητών σε ασθενείς που εμφάνισαν ή όχι επαναστένωση του αγγείου, είναι η αναγνώριση καποιού παράγοντα φλεγμονής που θα αποτελέσει δείκτη πρόβλεψης της επαναστένωσης με στόχο την πρόληψη αυτής.Υλικό - Μέθοδος:Μελετήθηκαν είκοσι δύο ασθενείς (17 άνδρες, μέσος όρος ηλικίας 66 έτη), με στένωση στην έκφυση της νεφρικής αρτηρίας και μή καλώς ρυθμιζόμενη υπέρταση, οι οποίοι υποβλήθησαν σε αγγειοπλαστική νεφρικής αρτηρίας με τοποθέτηση stent. Στους ασθενείς αυτούς πραγματοποιήθηκαν αιμοληψίες σε τρεις διαφορετικούς χρόνους: αμέσως πριν την αγγειοπλαστική (baseline), 24 ώρες και 6 μήνες μετά την αγγειοπλαστική και μετρήθηκαν στον ορό τους οι εξής μεσολαβητές: (1) Παράγοντας Νέκρωσης Όγκου-α (Tumor necrosis factor-α, TNF-α), (2) Ιντερλευκίνη 6 (Interleukin-6, IL-6), (3) Πρωτεΐνη χημειοτακτική για τα μονοκύτταρα τύπου-1 (Monocyte Chemoattractant protein-1, MCP-1), (4) Διακυτταρικό μόριο προσκόλλησης-1 (Intercellular adhesion molecule-1, ICAM-1), (5) Μόριο προσκόλλησης αγγειακών κυττάρων-1 (Vascular cell Adhesion Molecule-1, VCAM-1) και (6) Παράγοντας RANTES (Regulated upon Activation Normal T-cell Expressed presumed Secreted). Στους έξι μήνες μετά την αγγειοπλαστική πραγματοποιήθηκε έχρωμο Doppler υπερηχογράφημα και καταγράφηκε η ανάπτυξη ή όχι επαναστένωσης εντός του stent. Επιπλέον, αξιολογήθηκαν οι διαφορές της συγκέντρωσης αυτών σε ασθενείς που εμφάνισαν επαναστένωση της νεφρικής αρτηρίας στους 6 μήνες μετά την αγειοπλαστική συγκριτικά με αυτούς που δεν εμφάνισαν επαναστένωση.Αποτελέσματα:Η συγκέντρωση της ΙL-6 αυξήθηκε σημαντικά 24 ώρες μετά την αγγειοπλαστική (8.3 pg/mL ± 1.24 vs 2.76 pg/mL ± 1.27 τιμές baseline), ενώ στους 6 μήνες μετά επέστρεψε στις προ την επέμβαση τιμές (2.6 pg/mL ± 1.77) (Ρ<.0001). Δεν σημειώθηκαν στατιστικά σημαντικές διαφορές στις συγκεντρώσεις των υπολοίπων μεσολαβητών σε κανέναν από τους τρεις χρόνους. Επίσης, βρέθηκε πως η συγκέντρωση της ΙL-6 τόσο πρίν την αγγειοπλαστική όσο και 6 μήνες μετά την αγγειοπλαστική ήταν σημαντικά υψηλότερη στους ασθενείς που ανάπτυξαν επαναστένωση (8.13 pg/mL ± 4 vs 0.75 pg/mL ± 0.47 [P,.005] και 9.55 pg/ml ± 6.5 vs 0.42 pg/ml ± 0.35 [p<.02] αντίστοιχα).Συμπέρασμα:Με βάση τα αποτελέσματα προτείνουμε πως η αγγειοπλαστική της νεφρικής αρτηρίας με τοποθέτηση stent προκαλεί μια φλεγμονώδη αντίδραση στο τοίχωμα της αρτηρίας, όπως αυτή εκφράζεται με την υψηλή συγκέντρωση ΙL-6 στο αίμα 24 ώρες μετά την επέμβαση. Όσον αφορά στην ανάπτυξη ή όχι επαναστένωσης του αγγείου προτείνουμε πως η ΙL-6 μπορεί να να αναγνωρίσει τους ασθενείς υψηλού κινδύνου και κατ’ επέκταση να αποτελέσει έναν δείκτη πρόβλεψης της επαναστένωσης.

Abstract 224: Chronic Infusion Of Angiotensin-(1-7) Alleviates Cerebral Hemorrhagic Injury Compromised By Angiotensin II

Hypertension ◽  
2014 ◽  
Vol 64 (suppl_1) ◽  
Author(s):  
Ji C Bihl ◽  
Xiang Xiao ◽  
Cheng Zhang ◽  
Shuzhen Chen ◽  
Jinju Wang ◽  
...  
Keyword(s):  
Hemorrhagic Stroke ◽  
Ang Ii ◽  
Monocyte Chemoattractant Protein 1 ◽  
Treatment Groups ◽  
Arterial Blood ◽  
Tnf Α ◽  
Chronic Infusion ◽  
Factor Α ◽  
Necrosis Factor

Angiotensin-(1-7) [Ang-(1-7)] is a potential vascular protective peptide which counteracts the effects of Ang II. In this study, we investigated the role of Ang-(1-7) in hemorrhagic stroke. Adult male C57BL/6 mice implanted with telemetric probe for recording arterial blood pressure (BP) were divided into four minipump treatment groups: saline, Ang II, Ang II + Ang-(1-7), Ang II + Ang-(1-7) + A-779. After 2 weeks of treatment, mice were subjected to induction of hemorrhagic stroke by microinjection of collagenase (type VII; 0.075 U in 0.5 μL) in striatum. Mice were sacrificed at twenty-four hours after ICH induction. Brains were dissected and cut into coronal slices for histological analysis of middle cerebral artery (MCA)remodeling and hemorrhagic size. The plasma levels of tumor necrosis factor-α (TNF-α), monocyte chemoattractant protein 1 (MCP-1) and interleukin (IL-8) were determined by ELISA and the levels of NFκB and inhibitor of kappa B (IκB) in cerebral microvasculature were determined by western blot. We found (Figure): 1) Ang II increased BP, MCA remodeling and hemorrhagic size. 2) Ang-(1-7) significantly decreased the effects of Ang II on MCA and hemorrhage without affecting the BP, which were abolished by A-779. 3) Ang-(1-7) induced a 26-32% reduction in plasma level of TNF-α, MCP-1 and IL-8 increased by Ang II. 4) Ang-(1-7) also counter-regulated Ang II-induced NFƙB up-regulation and IƙB down-regulation. In conclusion, Ang-(1-7) counteracts Ang II on vascular remodeling and hemorrhagic injury by alleviating NFκB-related inflammation.

scholarly journals Angiotensin II enhances the increase in monocyte chemoattractant protein-1 production induced by tumor necrosis factor-α from 3T3-L1 preadipocytes

2009 ◽  
Vol 202 (2) ◽  
pp. 199-205 ◽  
Author(s):  
Sachie Asamizu ◽  
Masaharu Urakaze ◽  
Chikaaki Kobashi ◽  
Manabu Ishiki ◽  
Amal Khalifa Norel Din ◽  
...  
Keyword(s):  
Mrna Expression ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Ang Ii ◽  
Monocyte Chemoattractant Protein 1 ◽  
Monocyte Chemoattractant ◽  
Monocyte Chemoattractant Protein ◽  
Tnf Α ◽  
Factor Α ◽  
Necrosis Factor

Monocyte chemoattractant protein-1 (MCP-1) and angiotensin II (Ang II) in adipose tissue are thought to induce systemic insulin resistance in rodents; but the precise mechanism is not fully clarified. We examined the mechanism of Ang II-induced and/or tumor necrosis factor-α (TNF-α)-induced MCP-1 production from 3T3-L1 preadipocytes. The MCP-1 protein and MCP-1 mRNA expression in 3T3-L1 preadipocytes were increased significantly by stimulation with TNF-α. We found no significant increase in MCP-1 concentrations by Ang II alone; but it enhanced the TNF-α-induced MCP-1 mRNA expression in a dose-dependent manner. Then, we examined the effect of Ang II and/or TNF-α on phosphorylation of extracellular signal-regulated kinase (ERK), p38MAPK, and IκB-α. Ang II and TNF-α clearly enhanced ERK and p38MAPK phosphorylation. IκB-α phosphorylation was enhanced by TNF-α, but not by Ang II. The MCP-1 mRNA expression induced by TNF-α and co-stimulation with Ang II was inhibited by either ERK inhibitor, p38MAPK inhibitor or NF-κB inhibitor. Moreover, Ang II enhanced the activation of AP-1 (c-fos) induced by TNF-α. Our results suggest that Ang II may serve as an additional stimulus on the TNF-α-induced MCP-1 production through the ERK-and p38MAPK-dependent pathways probably due to AP-1 activation.

The Role of Tumor Necrosis Factor-α (TNF-α) Polymorphisms in Gastric Cancer: a Meta-Analysis

2021 ◽  
Author(s):  
Maryam Gholamalizadeh ◽  
Samaneh Mirzaei Dahka ◽  
Hadi Sedigh Ebrahim-Saraie ◽  
Mohammad Esmail Akbari ◽  
Azam Pourtaheri ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Meta Analysis ◽  
Tnf Α ◽  
Factor Α ◽  
Necrosis Factor

Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding

1999 ◽  
Vol 112 (21) ◽  
pp. 3603-3617 ◽  
Author(s):  
J. Schlondorff ◽  
C.P. Blobel
Keyword(s):  
Tumor Necrosis ◽  
Ectodomain Shedding ◽  
Membrane Glycoproteins ◽  
Tnf Α ◽  
Disintegrin Domain ◽  
Protein Ectodomain Shedding ◽  
Integrin Ligands ◽  
Factor Α ◽  
Necrosis Factor

Metalloprotease-disintegrins (ADAMs) have captured our attention as key players in fertilization and in the processing of the ectodomains of proteins such as tumor necrosis factor (α) (TNF(α)), and because of their roles in Notch-mediated signaling, neurogenesis and muscle fusion. ADAMs are integral membrane glycoproteins that contain a disintegrin domain, which is related to snake-venom integrin ligands, and a metalloprotease domain (which can contain or lack a catalytic site). Here, we review and critically discuss current topics in the ADAMs field, including the central role of fertilin in fertilization, the role of the TNF(α) convertase in protein ectodomain processing, the role of Kuzbanian in Notch signaling, and links between ADAMs and processing of the amyloid-precursor protein.

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