Immunological Studies in Inflammatory Bowel Disease

Pepys, Mark B.; Druguet, M.; Klass, H J; Dash, Ajit; Mirjah, D. D.; Petrie, Aviva

doi:10.1002/9780470720288.ch14

Cited by 30 publications

(16 citation statements)

References 33 publications

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“…A possible association of anti-␣-enolase antibodies with increased concentrations of CRP was examined in a cohort of 90 UC and GI patients. In this cohort, we did not find such an association, possibly due to a modest CRP response in UC (40 ).…”

Section: Discussioncontrasting

confidence: 82%

Anti–α-enolase Antibodies in Patients with Inflammatory Bowel Disease

et al. 2008

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Background: Patients with inflammatory bowel disease (IBD) carry autoantibodies such as perinuclear antineutrophil cytoplasmic antibodies (pANCA). α-Enolase has been proposed as a target antigen in IBD. We evaluated the prevalence and diagnostic value of anti–α-enolase antibodies in IBD and related disorders. Methods: We used a classic proteomic approach with extracts from granulocytes and pANCA-positive ulcerative colitis (UC) sera to confirm α-enolase as a target antigen. By means of Western blot analysis, we screened a cohort of 525 subjects for the presence of anti–α-enolase antibodies. We performed GeneArray experiments on RNA extracted from colonic mucosal biopsies from 35 IBD and 6 control patients. Results: We detected anti–α-enolase antibodies 49.0% of patients with UC, 50.0% of patients with Crohn’s disease, 30.5% of patients with primary sclerosing cholangitis, 37.8% of patients with autoimmune hepatitis, 34.0% of patients with ANCA-positive vasculitis, 31.0% of non-IBD gastrointestinal controls, and 8.5% of healthy controls. Gene array experiments showed a significant upregulation of α-enolase mRNA in colonic mucosal biopsies from patients with IBD, but not from controls. There was no association between the presence of pANCA and anti–α-enolase antibodies. Preabsorption with α-enolase did not eliminate the pANCA pattern on indirect immunofluorescence. Conclusions: Anti–α-enolase antibodies are present in a substantial proportion of patients with IBD, patients with various inflammatory/autoimmune disorders, and non-IBD gastrointestinal controls. Therefore, anti–α-enolase antibodies are of limited diagnostic value for the diagnosis of IBD.

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Section: Discussioncontrasting

confidence: 82%

Anti–α-enolase Antibodies in Patients with Inflammatory Bowel Disease

et al. 2008

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“…In IBD, activated leukocytes (mostly polymorphonuclear cells) infiltrate the mucosa and appear in faeces due to shedding in the intestinal lumen [3,4]. Faeces is in direct contact with this inflammed intestinal mucosa, thus making stool is an obvious place for biomarker discovery in IBD [5].…”

Section: Introductionmentioning

confidence: 99%

Faecal leukocyte esterase activity is an alternative biomarker in inflammatory bowel disease

Dumoulin

Biervliet

Vos

et al. 2015

Clinical Chemistry and Laboratory Medicine (CCLM)

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Background: Leukocyte cytosolic proteins (e.g., calprotectin) are emerging biomarkers for inflammatory bowel disease. Leukocyte aryl esterase activity has been commonly used for sensitive detection of leukocytes in human body fluids such as urine. Urine test strip results are generally reported in categories. As automated strip readers allow quantitative data to be reported, sensitive quantitative detection of leukocytes in body fluids has become possible. Here, we explored the use of leukocyte esterase as a potential alternative faecal biomarker for inflammatory bowel disease. Methods: We evaluated leukocyte esterase activity in faecal extracts and compared Cobas u 411 (Roche) quantitative reflectance data with calprotectin concentration for 107 routine samples. Stability of leukocyte esterase for trypsin digestion was carried out by adding trypsin to the extract. Incubation occurred at 37 °C for 24 h or 48 h. Results: Reproducibility of the reflectance signal was good (within-run imprecision: 6.1%; between-run imprecision: 6.2%). Results were linear in the range 10

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“…7,39,40 The transmural inflammation and the accumulation of intraabdominal fat in CD, which is a source of interleukin-6, may be probably responsible for the higher CRP response in CD. 41,42 Individual genetic factors may also contribute to differences in the CRP response.…”

Section: Discussionmentioning

confidence: 99%