Neuraminidase alters red blood cells in sepsis

Piagnerelli, Michaël; Boudjeltia, Karim Zouaoui; Rapotec, Alessandro; Richard, Thibault; Brohée, Dany; Babar, Sajida; Bouckaert, Vanessa; Simon, A.; Toko, Jean-Pierre; Walravens, Therese; Vincent, Jean‐Louis; Vanhaeverbeek, Michel

doi:10.1097/ccm.0b013e31819cebbe

Cited by 32 publications

(42 citation statements)

References 48 publications

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“…Increased neuraminidase activity was previously suggested as the most probable mechanism (20). It was recently shown that neuraminidase activity increases in sepsis which leads to erythrocyte desialylation (35) and that neuraminidase 1, one of the four human neuraminidases, has an important role in the immune response and inflammation (36)(37)(38)(39). However, the present re- sults show that, in contrast to transferrin, total plasma proteins do not show a decrease in their sialylation levels.…”

Section: Discussioncontrasting

confidence: 55%

Change of Transferrin Sialylation Differs between Mild Sepsis and Severe Sepsis and Septic Shock

Gornik

Kolednjak

et al. 2011

Intern. Med.

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Objective and Design To investigate the association between the severity of sepsis and changes in sialylation of serum proteins we have conducted a single center pilot study. Subjects and Methods Sialylation of transferrin (with enzyme-linked lectin assay-ELLA) and total serum proteins (with colorimetric assay) as well as serum iron and transferrin levels were measured in 27 patients with sepsis through the first eight days of the disease. Results Total serum sialylation increased in the first two days, transferrin sialylation decreased, while serum iron and transferrin fell. Patients who developed severe sepsis had either a small or marked change in transferrin sialylation while in patients with mild sepsis sialylation decreased moderately. Conclusion We hypothesize that the change in transferrin sialylation could be a reflection of the intensity of inflammatory response which is insufficient if under-expressed and detrimental if over-expressed. This new feature is a potential marker of sepsis severity early in the disease.

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Section: Discussioncontrasting

confidence: 55%

Change of Transferrin Sialylation Differs between Mild Sepsis and Severe Sepsis and Septic Shock

Gornik

Kolednjak

et al. 2011

Intern. Med.

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“…Desialylation of glycans are known to contribute to increased clearance of platelets and von Willebrand factor in bacteria-mediated sepsis models. 38 Consistently, increased sialidase activity in serum is reported in sepsis patients 39 and in rodent CLP sepsis models. 26 Our data showed the increased sialidase in the lymph from CLP mice, which caused desialylation and promoted degradation of PDPN on LECs primarily by MMPs in the lymph.…”

Section: Discussionsupporting

confidence: 52%

Podoplanin requires sialylated O-glycans for stable expression on lymphatic endothelial cells and for interaction with platelets

Pan

Yago

et al. 2014

Blood

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Key Points• Sialylated O-glycans protects PDPN from proteolytic degradation.• Sialylated core 1 O-glycans of PDPN on lymphatic endothelial cells (LECs) are required for interacting with platelets.O-glycosylation of podoplanin (PDPN) on lymphatic endothelial cells is critical for the separation of blood and lymphatic systems by interacting with platelet C-type lectin-like receptor 2 during development. However, how O-glycosylation controls endothelial PDPN function and expression remains unclear. In this study, we report that core 1 O-glycan-deficient or desialylated PDPN was highly susceptible to proteolytic degradation by various proteases, including metalloproteinases (MMP)-2/9. We found that the lymph contained activated MMP-2/9 and incubation of the lymph reduced surface levels of PDPN on core 1 O-glycan-deficient endothelial cells, but not on wild-type ECs. The lymph from mice with sepsis induced by cecal ligation and puncture, which contained bacteriaderived sialidase, reduced PDPN levels on wild-type ECs. The MMP inhibitor, GM6001, rescued these reductions. Additionally, GM6001 treatment rescued the reduction of PDPN level on lymphatic endothelial cells in mice lacking endothelial core 1 O-glycan or cecal ligation and puncture-treated mice. Furthermore, core 1 O-glycan-deficient or desialylated PDPN impaired platelet interaction under physiological flow. These data indicate that sialylated O-glycans of PDPN are essential for platelet adhesion and prevent PDPN from proteolytic degradation primarily mediated by MMPs in the lymph. (Blood. 2014;124(24):3656-3665)

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“…In our study, the neutrophil YM in rats does not change, which attests to the absence of the infection impact in experimental group. In sepsis, the erythrocytes acquire a spherical shape [7,9]. In our study, rat erythrocytes had common (biconcave) shape in all groups.…”

Section: Resultsmentioning

confidence: 86%

Studies of the Structure and Functions of Blood Cells in Senile Patients with Pneumonia on the Biological Model of Hypoxia by Scanning Probe Microscopy

et al. 2014

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Biological model of hypoxia can be used for the diagnosis o f functional changes in human erythrocytes under the effect of the hypoxic factor. The use of this model together with mod ern methods of scanning probe microscopy for evaluation o f the severity of pulmonological disease in senile patients will help to predict treatment efficiency and outcome. Key W ords: scanning probe microscopy (SPM); Young' s modulus; pneumoniaPhysiological changes in human tissues during aging manifest in impaired adaptation capacity to metabolic stress and general deterioration of the health status. The older the individual, the higher is the risk o f disease development, o f which pulmonological diseases, in cluding acute community-acquired pneumonia (called pneumonia in the text below) are most hazardous [1]. Respiratory diseases often cause a potent unfavorable effect, oxygen deficit in tissues, and therefore, studies of tissue hypoxia is the main problem o f pulmonol ogy and physiology [2]. Studies o f the mechanisms of cell response in hypoxia, evaluation of regularities of disease development, and the search for prognostic and diagnostic criteria are expected to improve evalu ation of the severity and progress o f various diseases, including pneumonia [8]. Scanning probe microscopy (SPM) is an informative method for studies o f the physiological status in health and disease, specifically, for studies o f blood cell parameters. Extrapolation o f experimental data on animal blood obtained on a biological model to the data ob tained in studies of hypoxia in patients is expected to show the trend of changes in blood cell structure and functions, indicating the effect of the hypoxic stress factor on the organism.The strong impact of infection is essential in pneu monia, which can modulate the cell parameters, specif ically the erythrocyte values [1]. Use o f the biological model will help differentiate the hypoxic effects on changes in human blood erythrocyte characteristics from the bacteriological factor. If the trend of changes in the rat red blood cells is similar to changes in pa tients with pneumonia, presumably, it is the hypoxic, but not the bacterial factor, that is mainly responsible for changes in human erythrocytes.We used the biological model for SPM studies of the blood cell structure and functions in senile patients with pneumonia.

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Neuraminidase alters red blood cells in sepsis

Abstract: In sepsis, desialylation under the influence of increased neuraminidase activity may contribute to the alterations in RBC rheology. Inhibition of neuraminidase may represent a new therapeutic option to ameliorate RBC rheology and perhaps oxygen delivery to the cells.

Cited by 32 publications

References 48 publications

Change of Transferrin Sialylation Differs between Mild Sepsis and Severe Sepsis and Septic Shock

Change of Transferrin Sialylation Differs between Mild Sepsis and Severe Sepsis and Septic Shock

Podoplanin requires sialylated O-glycans for stable expression on lymphatic endothelial cells and for interaction with platelets

Studies of the Structure and Functions of Blood Cells in Senile Patients with Pneumonia on the Biological Model of Hypoxia by Scanning Probe Microscopy

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