A comparison of equine and bovine sera as sources of lipopolysaccharide-binding protein activity in equine monocytes incubated with lipopolysaccharide

Figueiredo, Monica D.; Salter, Caroline E.; Hurley, David J.; Moore, James N.

doi:10.1016/j.vetimm.2007.10.002

Cited by 9 publications

(14 citation statements)

References 7 publications

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“…40 We found that inclusion of heterologous serum or autologous plasma (with or without heat inactivation) did not yield additional TF procoagulant activity in cytokine-stimulated canine PBMC. Fetal bovine serum alone stimulates TF procoagulant activity in canine and equine PBMC, primate kidney cells, and human fibroblasts 8,39,41,42 ; however, we found that canine PBMC had a variable response to HI-FBS, with serum stimulating activity in PBMC in some dogs but not in others. In contrast, there was a consistent increase in surface TF procoagulant activity in canine PBMC incubated with untreated, but not heat-inactivated, ACP.…”

Section: Cytokinecontrasting

confidence: 65%

“…The factor in canine plasma that is responsible for induction of procoagulant activity in canine PBMC is unknown and may be species specific. Untreated or heat‐inactivated autologous plasma did not stimulate TF procoagulant activity in equine PBMC, whereas untreated autologous plasma stimulated TF activity in porcine endothelial cells …”

Section: Discussionmentioning

confidence: 91%

“…Heterologous serum or autologous plasma enhances LPS‐induced TF procoagulant activity in canine and equine PBMC, presumably through provision of LPS‐binding protein . We reasoned that similar serum components may be required for induction of TF procoagulant activity in response to rc‐IL‐6 or rc‐IL‐8 in canine PBMC.…”

Section: Discussionmentioning

confidence: 99%

“…Heterologous serum or autologous plasma enhances LPS-induced TF procoagulant activity in canine and equine PBMC, presumably through provision of LPS-binding protein. 8,39 We reasoned that similar serum components may be required for induction of TF procoagulant activity in response to rc-IL-6 or rc-IL-8 in canine PBMC. For instance, IL-6 complexes with a soluble IL-6 receptor and the complex can then activate cells lacking the IL-6 receptor, a process called trans-signaling.…”

Section: Cytokinementioning

confidence: 99%

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Effect of recombinant canine interleukin‐6 and interleukin‐8 on tissue factor procoagulant activity in canine peripheral blood mononuclear cells and purified canine monocytes

Ogasawara

Trimpert

Stokol

2012

Veterinary Clinical Pathol

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Background Inflammation is a major cause of disseminated intravascular coagulation (DIC) in dogs, but underlying mechanisms for its initiation are unknown. We hypothesized that pro‐inflammatory cytokines, interleukin (IL)‐6 and IL‐8, induce tissue factor (TF) expression on canine monocyte surfaces, which may contribute to DIC initiation. Objectives The objectives of this study were to determine if (1) IL‐6 and IL‐8 would induce TF activity on canine monocytes, (2) fetal bovine serum or autologous plasma was required for IL‐6– or IL‐8–induced TF responses in canine monocytes, and (3) these pro‐inflammatory cytokines would enhance TF activity on canine monocytes in response to low concentrations of lipopolysaccharide (LPS). Methods Canine monocytes were isolated from EDTA‐anticoagulated blood as peripheral blood mononuclear cells (PBMC) by double‐density gradient centrifugation and adhesion to plastic. Adherent cells were stimulated for 4 hours with recombinant canine (rc)‐IL‐6 or rc‐IL‐8 (10–5000 pg/mL) with or without 10% heat‐inactivated (HI) fetal bovine serum, untreated autologous canine plasma (ACP), or HI‐ACP. Lipopolysaccharide (100 ng/mL) served as a positive control. Cells were also costimulated with either cytokine (100 pg/mL) or low concentrations of LPS (0.1 and 1 ng/mL). Monocytes immunopurified from PBMC with anti‐CD14 antibodies were also stimulated with both cytokines (100 and 5000 pg/mL). TF activity on cell surfaces was measured by a 2‐stage amidolytic assay, based on activated factor X generation. Results Neither rc‐IL‐6 nor rc‐IL‐8 consistently stimulated TF procoagulant activity in canine PBMC or purified monocytes after 4 hours. Serum, plasma, or low concentrations of LPS did not enhance the TF response to these cytokines. Conclusions IL‐6 or IL‐8 at evaluated concentrations may not play major roles in coagulation activation by induction of TF expression on monocytes in dogs with inflammation.

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Section: Cytokinecontrasting

confidence: 65%

Section: Discussionmentioning

confidence: 91%

Section: Discussionmentioning

confidence: 99%

Section: Cytokinementioning

confidence: 99%

See 2 more Smart Citations

Effect of recombinant canine interleukin‐6 and interleukin‐8 on tissue factor procoagulant activity in canine peripheral blood mononuclear cells and purified canine monocytes

Ogasawara

Trimpert

Stokol

2012

Veterinary Clinical Pathol

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“…The phenotype can be modified in vitro by exposure to various cytokines or exogenous stimuli such as lipopolysaccharide (LPS) during the maturation process [9-11]. Both fetal bovine serum (FBS) and autologous human serum (AHS) are in use as additions in in vitro culture conditions in biomaterials research [12-16].…”

Section: Introductionmentioning

confidence: 99%

Fetal bovine serum xenoproteins modulate human monocyte adhesion and protein release on biomaterials in vitro

2011

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Monocyte-derived macrophages are critical in the host foreign body response to biomaterials and have been studied extensively in various culture conditions in vitro such as medium supplemented with fetal bovine serum (FBS) or autologous human serum (AHS). Since monocyte maturation into macrophages is highly plastic and may vary considerably depending on the surface, isolation procedures, and in vitro culture conditions, we hypothesize that variations in protein adsorption and serum type will greatly impact monocyte behavior in a surface-dependent manner. The impact of xenoproteins on monocyte-surface interaction is not well studied methodically and the use of AHS rather than FBS for macrophage-biomaterials studies in vitro is far from universal. The commonly used reference materials: tissue culture polystyrene (TCPS), polyethylene glycol (PEG), and poly-dimethylsiloxane (PDMS) were employed in this study and we found a 3-fold higher adherent monocyte density on TCPS when AHS was used versus FBS-supplemented medium. On PEG hydrogels, an 8-10 fold higher adhesion density was observed when AHS was employed versus FBS, while on PDMS no difference in adhesion density was observed between the two sera conditions. Additionally, the presence of lipopolysaccharide abrogated the serum-dependent effect on cell adhesion on TCPS. Significant differential variations in protein release were observed between the serum conditions on these surfaces, in particular there was a 100-fold higher concentration of growth-related oncogene for the AHS condition on PDMS even though the adhesion levels were comparable between the two serum conditions. These results emphasize the combined impact of the surface type and FBS xenoproteins in mediating the observed monocyte response to biomaterials in vitro.

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Interleukin-1β, tumour necrosis factor-α and lipopolysaccharide induce C-type natriuretic peptide from canine aortic endothelial cells

Osterbur

DeClue

2013

Research in Veterinary Science

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A comparison of equine and bovine sera as sources of lipopolysaccharide-binding protein activity in equine monocytes incubated with lipopolysaccharide

Cited by 9 publications

References 7 publications

Effect of recombinant canine interleukin‐6 and interleukin‐8 on tissue factor procoagulant activity in canine peripheral blood mononuclear cells and purified canine monocytes

Effect of recombinant canine interleukin‐6 and interleukin‐8 on tissue factor procoagulant activity in canine peripheral blood mononuclear cells and purified canine monocytes

Fetal bovine serum xenoproteins modulate human monocyte adhesion and protein release on biomaterials in vitro

Interleukin-1β, tumour necrosis factor-α and lipopolysaccharide induce C-type natriuretic peptide from canine aortic endothelial cells

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