scholarly journals Factors affecting the concentration of soluble tumour necrosis factor-α receptor type I in the blood serum of patients with localized scleroderma

2020 ◽  
Vol 37 (4) ◽  
pp. 524-530
Author(s):  
Martyna Zbiciak-Nylec ◽  
Dominika Wcisło-Dziadecka ◽  
Ligia Brzeźińska-Wcisło
Keyword(s):  
Blood Serum ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Receptor Type ◽  
Localized Scleroderma ◽  
Type I ◽  
Tumour Necrosis Factor Α ◽  
Factors Affecting ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals Effects of antihypertensive treatment on systemic inflammation, oxidative stress and proinflammatory cytokine levels

2020 ◽  
Vol 11 (4) ◽  
pp. 536-541
Author(s):  
T. V. Ashcheulova ◽  
N. N. Gerasimchuk ◽  
O. N. Kovalyova ◽  
K. N. Kompaniiets ◽  
O. V. Honchar
Keyword(s):  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Type I ◽  
Soluble Receptor ◽  
Tumour Necrosis Factor Α ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Tnf Α ◽  
Factor Α ◽  
Necrosis Factor

Hypertension in its origin is a heterogeneous and multisystemic disease. Evaluation of oxidative stress activity based on the level of 8-iso-PgF2α, proinflammatory activity based on tumour necrosis factor-α, its type I soluble receptor, and C-reactive protein levels is relevant for further understanding of pathogenesis of hypertension and improvement of the early diagnostics of heart failure. 186 hypertensive patients were observed during a 2-months course of treatment, aged 30 to 65 years. Serum levels of 8-iso-PgF2α (n = 34), tumour necrosis factor-α and its type I soluble receptor were determined by ELISA before and after course of treatment. C-reactive protein level was determined by biochemical method. The control group included 16 clinically healthy individuals, aged 27 to 55 years. Hypertensive patients enrolled into the study were randomized into three groups that received different protocols of combined anti-hypertensive therapy: I clinical group – а combination of bisoprolol and indapamid, II – а combination of lacidipine and candesartan, III – а combination of fosinopril sodium and hydrochlorothiazide. On the background of combined antihypertensive therapy, we observed favourable dynamics of 8-iso-PgF2α, tumour necrosis factor-α and its type I soluble receptor, and C-reactive protein levels. Taking into account the insignificance of the correlations revealed, a one-factor dispersion analysis was applied which allowed us to determine the influence of the grade and duration of hypertension on the dynamics of the studied parameters. It has been found that the grade of hypertension is related to an increase in TNF-α and 8-iso-PgF2α serum levels, but not in TNF-α type I soluble receptor, and the duration of hypertension is related to an increase in C-reactive protein, TNF-α and its type I soluble receptor levels, with no relation to the level of 8-iso-PgF2α. Thus, oxidative stress possibly promotes the activation of potentially damaging immune mechanisms mediated by proinflammatory cytokines, nonspecific inflammation and drives the further progression of lesions in the target organs.

scholarly journals Tumour necrosis factor α-converting enzyme mediates ectodomain shedding of Vps10p-domain receptor family members

2006 ◽  
Vol 395 (2) ◽  
pp. 285-293 ◽  
Author(s):  
Guido Hermey ◽  
Susanne S. Sjøgaard ◽  
Claus Munck Petersen ◽  
Anders Nykjær ◽  
Jørgen Gliemann
Keyword(s):  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Chinese Hamster Ovary Cells ◽  
Amyloid Β ◽  
Type I ◽  
Converting Enzyme ◽  
Tumour Necrosis Factor Α ◽  
Vacuolar Protein ◽  
Factor Α ◽  
Necrosis Factor

Several transmembrane molecules are cleaved at juxtamembrane extracellular sites leading to shedding of ectodomains. We analysed shedding of members of the Vps10p-D (Vps10p domain; where Vps is vacuolar protein sorting) family of neuronal type-I receptors with partially overlapping functions, and additional proteolytic events initiated by the shedding. When transfected into CHO (Chinese-hamster ovary) cells (CHO-K1), sorCS1a–sorCS1c isoforms were shed at high rates (∼0.61%·min−1) that were increased approx. 3-fold upon stimulation with phorbol ester. sorCS1c identified in the cultured neuroblastoma cell line SH-SY5Y was shed similarly. In CHO-K1 transfectants, constitutive and stimulated shedding of sorCS3 also occurred at high rates (0.29% and 1.03%·min−1). By comparison, constitutive and stimulated shedding of sorLA occurred at somewhat lower rates (0.07% and 0.48%·min−1), whereas sorCS2 and sortilin were shed at very low rates even when stimulated (∼0.01%·min−1). Except for sorCS2, shedding of the receptors was dramatically reduced in mutant CHO cells (CHO-M2) devoid of active TACE (tumour necrosis factor α-converting enzyme), demonstrating that this enzyme accounts for most sheddase activity. The release of sorCS1 and sorLA ectodomains initiated rapid cleavage of the membrane-tethered C-terminal stubs that accumulated only in the presence of γ-secretase inhibitors. Purified shed sorLA bound several ligands similarly to the entire luminal domain of the receptor, including PDGF-BB (platelet-derived growth factor-BB) and amyloid-β precursor protein. In addition, PDGF-BB also bound to the luminal domains of sorCS1 and sorCS3. The results suggest that ectodomains shed from a subset of Vps10p-D receptors can function as carrier proteins.

Substrate specificity and inducibility of TACE (tumour necrosis factor α-converting enzyme) revisited: the Ala-Val preference, and induced intrinsic activity

2003 ◽  
Vol 70 ◽  
pp. 39-52 ◽  
Author(s):  
Roy A. Black ◽  
John R. Doedens ◽  
Rajeev Mahimkar ◽  
Richard Johnson ◽  
Lin Guo ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Recent Work ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Transforming Growth Factor ◽  
Intrinsic Activity ◽  
Converting Enzyme ◽  
Tumour Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor

Tumour necrosis factor α (TNFα)-converting enzyme (TACE/ADAM-17, where ADAM stands for a disintegrin and metalloproteinase) releases from the cell surface the extracellular domains of TNF and several other proteins. Previous studies have found that, while purified TACE preferentially cleaves peptides representing the processing sites in TNF and transforming growth factor α, the cellular enzyme nonetheless also sheds proteins with divergent cleavage sites very efficiently. More recent work, identifying the cleavage site in the p75 TNF receptor, quantifying the susceptibility of additional peptides to cleavage by TACE and identifying additional protein substrates, underlines the complexity of TACE-substrate interactions. In addition to substrate specificity, the mechanism underlying the increased rate of shedding caused by agents that activate cells remains poorly understood. Recent work in this area, utilizing a peptide substrate as a probe for cellular TACE activity, indicates that the intrinsic activity of the enzyme is somehow increased.

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