Multifunctional α-enolase: its role in diseases

Pancholi, Vijay

doi:10.1007/pl00000910

Cited by 790 publications

(783 citation statements)

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“…This protein is also found on the surface of streptococci, which can cause acute rheumatic fever 3 Cumulative rate of steroid use for the IgM anti-a-enolase antibody positive and negative groups were 38 and 31% at 1 year, 40 and 35% at 2 years, 46 and 43% at 3 years, 51 and 48% at 4 years, and 60 and 48% at 5 years, respectively (P = 0.022) [21], and has been identified as a type of heat-shock protein [22]. The evidence suggests that a-enolase plays an important role in autoimmune and inflammatory diseases, such as rheumatoid arthritis, systemic lupus erythematosus, discoid lupus erythematosus, cancer-associated retinopathy, ANCA-positive vasculitis, systemic sclerosis, endometriosis, primary membranous nephropathy, autoimmune liver disease, and mixed connective tissue disease [20,23,24]. In our study, IgM AAEA was positive in 54 of 80 (67.5%) intestinal BD patients, which was higher than the prevalence among BD patients (45.0%) reported by Lee et al [13].…”

Section: Discussionmentioning

confidence: 97%

“…This protein apparently serves as a plasminogen receptor on the surface of a variety of hematopoietic, epithelial, and endothelial cells and plays a crucial role in intravascular and pericellular fibrinolytic systems [19,20]. This protein is also found on the surface of streptococci, which can cause acute rheumatic fever 3 Cumulative rate of steroid use for the IgM anti-a-enolase antibody positive and negative groups were 38 and 31% at 1 year, 40 and 35% at 2 years, 46 and 43% at 3 years, 51 and 48% at 4 years, and 60 and 48% at 5 years, respectively (P = 0.022) [21], and has been identified as a type of heat-shock protein [22].…”

Section: Discussionmentioning

confidence: 99%

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Anti-Alpha-Enolase Antibody as a Serologic Marker and Its Correlation with Disease Severity in Intestinal Behçet’s Disease

Shin

Kim

et al. 2010

Dig Dis Sci

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Background Intestinal Behçet's disease (BD) is a chronic inflammatory bowel disease, as are Crohn's disease (CD) and ulcerative colitis (UC). But unlike CD and UC, serologic markers for intestinal BD are not well known. Recently, antia-enolase antibody (AAEA) has been detected in sera from BD patients. Aims The aim of this study was to evaluate the prevalence of AAEA in intestinal BD and its clinical correlations. Methods The study sample included 80 patients with intestinal BD and 23 healthy controls. IgM AAEA was detected by ELISA. The positivity of IgM AAEA was defined as an optical density greater than three standard deviations above the mean of the control sera. Other parameters, such as demographic information, subtype of BD, colonoscopic findings, disease severity and treatment modality, were analyzed retrospectively. Results The prevalence of IgM AAEA was 67.5% in intestinal BD and 0% in the control group. The positivity rate of IgM AAEA was higher in complete or incomplete BD than in suspected BD (77.5% vs. 51.6%, P = 0.016). The mean HBI score was higher in antibody positive patients than in antibody negative patients (5.60 vs. 4.61, P = 0.003). The cumulative probability of steroid use for aggravation of intestinal and extra-intestinal symptoms was higher in antibody positive patients than in antibody negative patients (P = 0.012). The number of patients with systemic involvement was higher in the AAEA positive group than in the negative group. Conclusions Monitoring IgM AAEA may be helpful for diagnosis of intestinal BD and could be used to predict clinical course and disease severity.

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Anti-Alpha-Enolase Antibody as a Serologic Marker and Its Correlation with Disease Severity in Intestinal Behçet’s Disease

Shin

Kim

et al. 2010

Dig Dis Sci

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“…The consequent binding of plasminogen to ␣-enolase plays a crucial role in fibrinolysis. The role of this enzyme in systemic or invasive autoimmune disease was recently reported (30). Certain properties of ␣-enolase, especially those related to surface expression and plasminogen binding, indicate that enolase may play an important role in the initiation of the disease process by modulating the pericellular and intravascular fibrinolytic system.…”

Section: Aeca Against ␣-Enolase In Behç Et's Disease 2031mentioning

confidence: 98%

“…Antibodies against ␣-enolase have been found in various inflammatory and immune disorders, such as cancer-associated retinopathy, ANCA-positive vasculitis, inflammatory bowel disease, discoid lupus erythematosus, SLE, systemic sclerosis, endometriosis, primary membranous nephropathy, mixed connective tissue disease, and in autoimmune liver diseases (27,30,31). In SLE with nephritis, mixed cryoglobulinemia, and diffuse systemic sclerosis, antienolase antibodies react readily with renal and endothelial cell antigens, which express abundant ␣-enolase and, thus, induce injury to those cells (27).…”

Section: Aeca Against ␣-Enolase In Behç Et's Disease 2031mentioning

confidence: 99%

Human α‐enolase from endothelial cells as a target antigen of anti–endothelial cell antibody in Behçet's disease

Lee¹,

Chung²,

Kim³

et al. 2003

Arthritis & Rheumatism

176

108

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Objective. To identify and recombine a protein of the human dermal microvascular endothelial cell (HD-MEC) that specifically reacts with anti-endothelial cell antibody (AECA) in the serum of patients with Behçet's disease (BD), and to evaluate the usefulness of this protein in BD.Methods. The proteomics technique, with 2-dimensional gel electrophoresis and matrix-assisted laser desorption ionization؊time-of-flight (MALDI-TOF) mass spectrometry, was used to identify and recombine HDMEC antigen. Western blotting and enzyme-linked immunosorbent assay (ELISA) of recombinant protein isolated by gene cloning were performed on serum from healthy controls, patients with BD, and patients with other rheumatic diseases (rheumatoid arthritis, systemic lupus erythematosus, and Wegener's granulomatosis).Results. Eighteen of 40 BD patients had serum IgM antibody to HDMEC antigen. The purified protein that reacted with AECA in BD patient sera was found to be ␣-enolase by 2-dimensional gel electrophoresis followed by immunoblotting and MALDI-TOF mass spectrometry. Recombinant ␣-enolase protein was isolated and refined by gene cloning. On Western blots, AECApositive IgM from the sera of patients with active BD reacted strongly with recombinant human ␣-enolase. BD patient sera positive for anti-␣-enolase did not react with human ␥-enolase. On dot-blotting, reactivity to human ␣-enolase was detected only in the IgM-positive group. Fifteen of the 18 AECA-positive sera that were positive for the HDMEC antigen showed reactivity to recombinant ␣-enolase IgM antibody by ELISA.Conclusion. The ␣-enolase protein is the target protein of serum AECA in BD patients. This is the first report of the presence of IgM antibodies to ␣-enolase in endothelial cells from the serum of BD patients. Although further studies relating this protein to the pathogenesis of BD will be necessary, ␣-enolase and its antibody may prove useful in the development of new diagnostic and treatment modalities in BD.

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“…Periodontitis patients have elevated levels of serum antibodies to human heat shock protein 60 and antibodies to P. gingivalis GroEL that are cross-reactive to each other [20]. ENO1 is a highly conserved protein from prokaryotes to eukaryotes, with 40–90% identity between enolases from different species [21]. A similarity search of the bacterial protein database for ENO1 revealed that the enolase of T. denticola (TdEno) has the highest score among those of human-associated bacteria [22].…”

Section: Introductionmentioning

confidence: 99%

Treponema denticola enolase contributes to the production of antibodies against ENO1 but not to the progression of periodontitis

et al. 2018

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Autoantibodies against alpha-enolase (ENO1) are often detected in various infectious and autoimmune diseases. Anti-ENO1 antibody titers were reported to be associated with the severity of periodontitis in patients with rheumatoid arthritis. Because the enolase of the periodontal pathogen Treponema denticola (TdEno) has the highest homology with ENO1 among the enolases of human-associated bacteria, we hypothesized that anti-ENO1 autoantibodies produced during the immune response to TdEno may contribute to the progression of periodontitis and tested it in human and mouse systems. In human subjects with healthy periodontium or chronic periodontitis, a strong positive correlation between the levels of anti-TdEno and anti-ENO1 antibodies was observed. In addition, the purified anti-TdEno antibodies recognized ENO1 as well as TdEno in a dot blot, confirming the cross-reactivity between TdEno and ENO1. However, anti-ENO1 antibody titers were not associated with the severity of periodontitis. To further investigate the role of TdEno in the production of anti-ENO1 antibodies and the progression of periodontitis, mice received an oral gavage of P. gingivalis alone, subcutaneous immunization with TdEno alone, or both P. gingivalis oral gavage and TdEno immunization. Immunization with TdEno induced not only anti-TdEno but also anti-mouse Eno1 (mEno1) antibodies and increased the expression of TNFα in the gingival tissues. However, alveolar bone loss was not increased by TdEno immunization. In conclusion, autoreactive anti-ENO1/mEno1 antibodies that are produced as byproducts during the antibody response to TdEno play a minimal role in the progression of periodontitis in the absence of rheumatoid arthritis.

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Multifunctional α-enolase: its role in diseases

Cited by 790 publications

References 109 publications

Anti-Alpha-Enolase Antibody as a Serologic Marker and Its Correlation with Disease Severity in Intestinal Behçet’s Disease

Anti-Alpha-Enolase Antibody as a Serologic Marker and Its Correlation with Disease Severity in Intestinal Behçet’s Disease

Human α‐enolase from endothelial cells as a target antigen of anti–endothelial cell antibody in Behçet's disease

Treponema denticola enolase contributes to the production of antibodies against ENO1 but not to the progression of periodontitis

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