Role of allergic reactions of peripheral blood leukocytes in the pathogenesis of experimental allergic (pertussis) encephalomyelitis

1977 ◽  
Vol 83 (3) ◽  
pp. 366-369 ◽  
Author(s):  
A. Kh. Kanchurin ◽  
A. A. Babakhin ◽  
A. V. Safronova
Keyword(s):  
Peripheral Blood ◽  
Allergic Reactions ◽  
Peripheral Blood Leukocytes ◽  
Blood Leukocytes ◽  
Experimental Allergic

scholarly journals Critical Role of Nitric Oxide During the Apoptosis of Peripheral Blood Leukocytes from Patients with AIDS

1999 ◽  
Vol 5 (12) ◽  
pp. 812-819 ◽  
Author(s):  
M. Djavad Mossalayi ◽  
Pierre-André Becherel ◽  
Patrice Debré
Keyword(s):  
Nitric Oxide ◽  
Peripheral Blood ◽  
Critical Role ◽  
Peripheral Blood Leukocytes ◽  
Blood Leukocytes

scholarly journals Leucine-rich α2-glycoprotein-1 upregulation in plasma and kidney of patients with lupus nephritis

2020 ◽  
Author(s):  
Yi Yang ◽  
Ran Luo ◽  
Yichun Cheng ◽  
Tingting Liu ◽  
Wei Dai ◽  
...  
Keyword(s):  
Renal Function ◽  
Lupus Nephritis ◽  
Disease Activity ◽  
Peripheral Blood ◽  
Enzyme Linked Immunosorbent Assay ◽  
Epithelial Cell Line ◽  
Peripheral Blood Leukocytes ◽  
Blood Leukocytes ◽  
Expression Levels

Abstract Background Increased leucine-rich α2-glycoprotein-1 (LRG1) has been observed in various inflammatory and autoimmune diseases. We aimed to explore the expression and role of LRG1 in lupus nephritis (LN). Methods Plasma LRG1 (pLRG1) was measured by enzyme-linked immunosorbent assay in 101 patients with renal biopsy-proven LN and 21 healthy controls (HC). Relationships between pLRG1 and clinical and pathological characteristics were analyzed. The expression of LRG1 in peripheral blood leukocytes and kidney was detected by flow cytometry, immunohistochemistry and immunofluorescence, respectively. Further cell experiments were focused on the role of LRG1. Results We found that LRG1 was expressed in plasma, some peripheral blood leukocytes, proximal tubule and several inflammatory cells. The levels of LRG1 in plasma, peripheral blood leukocytes and kidney were elevated in LN patients as compared to HC. Plasma expression levels of LRG1 correlated positively with renal function and renal disease activity, and reflect specific pathologic lesions in the kidneys of patients with LN. Interleukin-1β and interleukin-6, not tumor necrosis factor-α and interferon γ induced the LRG1 expression in human renal tubular epithelial cell line. Moreover, stimulation of recombinant human LRG1 could inhibit late apoptosis, promote proliferation and regulate expression of inflammatory factors and cytokines. Conclusions Plasma expression levels of LRG1 were associated with renal function, disease activity, and pathology in LN. It might also be involved in renal inflammation, proliferation and apoptosis of endothelial cells. LRG1 might be a potential prognosis novel predictor in LN patients.

scholarly journals EHV-1 gene63 is not essential for in vivo replication in horses and mice, nor does it affect reactivation in the horse: Short Communication

2001 ◽  
Vol 49 (4) ◽  
pp. 473-478
Author(s):  
J. Iqbal ◽  
A. S. Purewal ◽  
N. Edington
Keyword(s):  
Peripheral Blood ◽  
Acute Infection ◽  
Early Gene ◽  
Peripheral Blood Leukocytes ◽  
Blood Leukocytes ◽  
Equine Herpesvirus 1 ◽  
Nasal Swabs

The aim of this study was to investigate the role of immediate early gene (gene63) in the pathogenesis of equine herpesvirus 1 (EHV-1) acute and latent infections in equine and murine models. EHV-1 gene63 mutant virus (g63mut) along with EHV-1 (Ab4) was used for intracerebral and intranasal infection of 3 and 17-day-old mice. Both viruses were recovered at the same frequency from tissues after infection. Two Welsh ponies were infected via the intranasal route with each of the viruses. Acute infection was monitored by virus isolation from nasal swabs and peripheral blood leukocytes. Six weeks post infection, peripheral blood leukocytes were taken from ponies and in vitro reactivation was positive for both viruses. At autopsy, both viruses were isolated by co-cultivation from bronchial and submandibular lymph nodes. These findings indicate that the mutation of EHV-1 gene63 does not play a role in the establishment and reactivation from latency.

scholarly journals Leucine-rich α2-glycoprotein-1 upregulation in plasma and kidney of patients with lupus nephritis

2020 ◽  
Author(s):  
Yi Yang ◽  
Ran Luo ◽  
Yichun Cheng ◽  
Tingting Liu ◽  
Wei Dai ◽  
...  
Keyword(s):  
Renal Function ◽  
Lupus Nephritis ◽  
Disease Activity ◽  
Peripheral Blood ◽  
Enzyme Linked Immunosorbent Assay ◽  
Epithelial Cell Line ◽  
Peripheral Blood Leukocytes ◽  
Blood Leukocytes ◽  
Expression Levels

Abstract Background Increased leucine-rich α2-glycoprotein-1 (LRG1) has been observed in various inflammatory and autoimmune diseases. We aimed to explore the expression and role of LRG1 in lupus nephritis (LN). Methods Plasma LRG1 (pLRG1) was measured by enzyme-linked immunosorbent assay in 101 patients with renal biopsy-proven LN and 21 healthy controls (HC). Relationships between pLRG1 and clinical and pathological characteristics were analyzed. The expression of LRG1 in peripheral blood leukocytes and kidney was detected by flow cytometry, immunohistochemistry and immunofluorescence, respectively. Further cell experiments were focused on the role of LRG1. Results We found that LRG1 was expressed in plasma, some peripheral blood leukocytes, proximal tubule and several inflammatory cells. The levels of LRG1 in plasma, peripheral blood leukocytes and kidney were elevated in LN patients as compared to HC. Plasma expression levels of LRG1 correlated positively with renal function and renal disease activity, and reflect specific pathologic lesions in the kidneys of patients with LN. Interleukin-1β and interleukin-6, not tumor necrosis factor-α and interferon γ induced the LRG1 expression in human renal tubular epithelial cell line. Moreover, stimulation of recombinant human LRG1 could inhibit late apoptosis, promote proliferation and regulate expression of inflammatory factors and cytokines. Conclusions Plasma expression levels of LRG1 were associated with renal function, disease activity, and pathology in LN. It might also be involved in renal inflammation, proliferation and apoptosis of endothelial cells. LRG1 might be a potential prognosis novel predictor in LN patients.

scholarly journals Leucine-rich α2-glycoprotein-1 upregulation in plasma and kidney of patients with lupus nephritis

2019 ◽  
Author(s):  
Yi Yang ◽  
Ran Luo ◽  
Yichun Cheng ◽  
Tingting Liu ◽  
Wei Dai ◽  
...  
Keyword(s):  
Renal Function ◽  
Lupus Nephritis ◽  
Disease Activity ◽  
Peripheral Blood ◽  
Enzyme Linked Immunosorbent Assay ◽  
Epithelial Cell Line ◽  
Peripheral Blood Leukocytes ◽  
Blood Leukocytes ◽  
Expression Levels

Abstract Background Increased leucine-rich α2-glycoprotein-1 (LRG1) has been observed in various inflammatory and autoimmune diseases. We aimed to explore the expression and role of LRG1 in lupus nephritis (LN).Methods Plasma LRG1 (pLRG1) was measured by enzyme-linked immunosorbent assay in 101 patients with renal biopsy-proven LN and 21 healthy controls (HC). Relationships between pLRG1 and clinical and pathological characteristics were analyzed. The expression of LRG1 in peripheral blood leukocytes and kidney was detected by flow cytometry, immunohistochemistry and immunofluorescence, respectively. Further cell experiments were focused on the role of LRG1.Results We found that LRG1 was expressed in plasma, some peripheral blood leukocytes, proximal tubule and several inflammatory cells. The levels of LRG1 in plasma, peripheral blood leukocytes and kidney were elevated in LN patients as compared to HC. Plasma expression levels of LRG1 correlated positively with renal function and renal disease activity, and reflect specific pathologic lesions in the kidneys of patients with LN. Interleukin-1β and interleukin-6, not tumor necrosis factor-α and interferon γ induced the LRG1 expression in human renal tubular epithelial cell line. Moreover, stimulation of recombinant human LRG1 could inhibit late apoptosis, promote proliferation and regulate expression of inflammatory factors and cytokines.Conclusions Plasma expression levels of LRG1 were associated with renal function, disease activity, and pathology in LN. It might also be involved in renal inflammation, proliferation and apoptosis of endothelial cells. LRG1 might be a potential prognosis novel predictor in LN patients.

ENDOTHELIAL-DEPENDENT MECHANISMS OF LEUKOCYTE ADHESION: ROLE OF MONOKINES

1987 ◽  
Author(s):  
M A Gimbrone ◽  
M P Bevilacqua ◽  
M E Wheeler
Keyword(s):  
Endothelial Cells ◽  
Monoclonal Antibodies ◽  
Endothelial Cell ◽  
Surface Structure ◽  
Peripheral Blood ◽  
Leukocyte Adhesion ◽  
Active Role ◽  
Peripheral Blood Leukocytes ◽  
Blood Leukocytes

Localized adhesion of peripheral blood leukocytes to the vessel wall is an essential component of inflammatory reactions. There is increasing experimental evidence that vascular endothelial cells play an active role in this process. Our laboratory has been especially interested in defining endothelial-dependent mechanisms of leukocyte adhesion, and the role of leukocyte products in their modulation. We have reported1 that purified natural human monocyte-derived interleukin 1 (IL-1) can act directly on cultured human endothelial cells (HEC) to dramatically increase the adhesiveness of their surfaces for human polymorphonuclear leukocytes (PMN), monocytes and the related cell lines HL-60 and U937. This effect was concentration-, time- (onset≅30 min; peak≅4h) , and protein/RNA-synthesis-requiring, and, in selective pretreatment/fixation experiments, was shown to be mediated primarily through the endothelial cell. To better define this inducible endothelial pro-adhesive mechanism, we have developed a series of murine monoclonal antibodies directed against monokine-stimulated HEC surfaces. One of these antibodies (H4/18) recognizes an endothelial cell surface structure which is induced by IL-1 (and certain other cytokines)2 in a similar fashion (kinetics, concentration - dependence, sensitivity to metabolic inhibitors) as the pro-adhesive surface change for leukocytes. H4/18 partially blocks HD-60 cell adhesion to monokine-treated HEC, and, in vivo, labels human vascular endothelium at sites of experimental delayed hypersensitivity reactions4. A second monoclonal antibody (H18/7)5 significantly blocks the adhesion of both HL-60 cells and PMN to monokine-treated HEC. Monoclonal antibodies H4/18 and H18/7 appear to recognize the same inducible surface structure as assessed by immunoprecipitation of extracts of metabolically labeled, monokine-stimulated HEC. We have designated this monokine-inducible, endothelial-leukocyte adhesion molecule "E-IAM 1". IL-1 treated HEC cultures (in contrast to sham-treated control cultures) generate a soluble leukocyte adhesion inhibitor (LAI)6,7. LAI acts on PMN to inhibit their adhesion to hyperadhesive endothelial monolayers as well as to serum-coated plastic surfaces, but does not inhibit PMN activation by chemotactic stimuli (LTB4, f-met-leu-phe). IAI appears to differentially inhibit adhesion of peripheral blood leukocytes, isolated from the same donor, to hyperadhesive HEC (PMN > monocytes; lymphocytes, no effect), and does not inhibit HL-60 cell-HEC adhesion. Endothelial production of IAI is time-dependent (peak 5-6 h.), and blocked by cycloheximide but not by aspirin. Preliminary characterization indicates that LAI is nonsedimentable (250,000 xg, 45 min), nondialyzable (>10 kD), stable to heat (80°C, 30 min) and acid (pH 2) and is precipitable by ammonium sulphate (60-80% saturation). Thus, this endothelial-derived inhibitory activity, which appears to be distinct from PGI2 or other cyclooxygenase products, blocks leukocyte adhesion without globally suppressing leukocyte function. Further characterization of the cellular and molecular mechanisms regulating the endothelial expression of E-LAM 1 and LAI should contribute to our understanding of the active role of the vascular wall in the inflammatory process.1. Bevilacqua et al. (1985); J. Clin. Invest.76:2003.2. Cotran et al. (1986); J. Exp. Med. 164:661.3. Bevilacqua et al. (1987); Fed. Proc. (in press).4. Wheeler et al. (1986); Fed. Proc. 45:1725.5. Wheeler et al. (1987); Fed. Proc. (in press).

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