scholarly journals Changes in IgG and total plasma protein glycomes in acute systemic inflammation

2014 ◽  
Vol 4 (1) ◽  
Author(s):  
Mislav Novokmet ◽  
Edita Lukić ◽  
Frano Vučković ◽  
Željko –Durić ◽  
Toma Keser ◽  
...  



1984 ◽  
Vol 56 (3) ◽  
pp. 666-670 ◽  
Author(s):  
H. M. O'Brodovich ◽  
M. Andrew ◽  
G. W. Gray ◽  
G. Coates

Acute decompression is associated with a shortening of the activated partial thromboplastin time (aPTT). This study was performed to examine whether this change in aPTT results from hypoxia or hypobaria. We exposed healthy adults on three separate occasions to 2 h of 1) hypoxic hypobaria (410 Torr, n = 5), 2) hypoxic normobaria (fractional inspired O2 tension = 0.11, n = 4), or 3) normoxic hypobaria (410 Torr breathing supplemental O2, n = 5). The aPTT shortened during hypoxic hypobaria and hypoxic normobaria (P less than 0.05) but was unchanged during normoxic hypobaria. The prothrombin and thrombin times, hematocrit, and concentrations of fibrinogen, total plasma protein, and fibrinogen-fibrin fragment E were unchanged. During hypoxic hypobaria biologic levels of prekallikrein, high-molecular-weight kininogen, and factors XII, XI, X, VII, V, and II were unchanged, but procoagulant VIII (VIII:C) increased 50% without an increase in VIII-related antigen levels (VIIIR:Ag). Fibrin monomer was not detected in any group. In one subject who became ill after 1.5 h of hypoxic normobaria aPTT shortened by 10 s; the platelet count decreased by 93,000/mm3; VIII:C increased fivefold, but VIIIR:Ag only increased three-fold. We conclude that it is the hypoxia which shortens aPTT during acute decompression to 410 Torr and speculate that it results from an increase in plasma VIII:C-like activity.



2006 ◽  
Vol 70 (2) ◽  
pp. 472-478 ◽  
Author(s):  
MICHAEL A. GREGG ◽  
MIKE R. DUNBAR ◽  
JOHN A. CRAWFORD ◽  
MICHAEL D. POPE


2007 ◽  
Vol 70 (5) ◽  
pp. 709-711 ◽  
Author(s):  
Burcu Okutucu ◽  
Ayşşe Dınçer ◽  
Ömer Habib ◽  
Figen Zıhnıoglu




2001 ◽  
Vol 27 (2) ◽  
pp. 133-139 ◽  
Author(s):  
Seema Rosqvist ◽  
Gunvor Johannesson ◽  
Christian H Lindh ◽  
Bo AG Jönsson


2021 ◽  
Vol 99 (Supplement_3) ◽  
pp. 267-267
Author(s):  
Djaafar M Rehrah ◽  
Mulumebet Worku ◽  
Hamid Ismail

Abstract Galectins are part of a conserved family of β-galactoside-binding proteins that contribute to critical biological events during mammalian gestation and increasingly recognized for a possible role in the immune response of the cow. The objective of this study was to evaluate the effect of Galectins on signal transduction and cell activation in cow blood. Whole blood was collected aseptically from the jugular vein of healthy Holstein Friesian dairy cows (N=3). Blood samples (2.5ml) in duplicate were treated with 150µl of the four different type of recombinant galectins (1, 3, 4, and 9) respectively and untreated samples were served as control. The concentration of total plasma protein was determined using the Pierce BCA kit. Protein expression profiling was performed using1,358 antibodies on the Full Moon BioSystems’ Signaling Explorer antibody array covering 20 cell signaling pathways, as recommended by the manufacturer using an Agilent microarray scanner. Data normalization was performed using GeneSpring GX software to generate fold changes in gene expression and then filtered to obtain a list of significantly upregulated and downregulated genes. Features were extracted from protein array images of samples treated with Galectin 1, 3, 4, 9, and untreated sample as a control group. Treatment with all four Galectins increased the concentration of total plasma protein. Average increases due to treatment with Gal1, Gal3, Gal4, and Gal9 were 27%, 10%, 20%, and 14% respectively. ANOVA test showed significance difference among the groups (p < 0.05). Dunnett option was used to compare each of the treated samples to the control group as a baseline. The results also showed that there was significant difference between the control group and any of the treated group (p < 0.05). Distinct signaling pathways are activated in response to Galectin exposure. Further studies are needed to define their regulation and functional impact on cow health.



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