Serum Adenosine Deaminase Levels in Pancreatic Diseases

doi:10.1159/000108970

Pancreatology

Volume 7, Issues 5–6, October 2007, Pages 526-530

https://doi.org/10.1159/000108970 Get rights and content

Abstract

Background: Adenosine deaminase (ADA) is found in most tissues including the pancreas. Its role in inflammation and malignancy has been studied experimentally. To date, serum ADA levels in pancreatic diseases have not been studied before. Aim: To assess the levels of ADA in patients with pancreatitis and cancer of the pancreas. Methodology: Serum levels of ADA were investigated in 14 cases with acute pancreatitis (mean age 46 years; male/female 5/9), 38 with chronic pancreatitis (mean age 46 years; male/female 25/13), 21 with cancer of the pancreas (mean age 67 years; male/female 11/10), and 21 healthy controls (mean age 40 years; male/female 11/10). The ADA levels were also compared among patients with pancreatic cancer with regard to tumor size and localization and the presence of métastases. Correlation analysis between ADA and CA 19.9 was also performed. Results: Serum ADA levels were 12.66 (9.54–20.72), 12.51 (8.88–26.64), 15.36 (10.20–21.05) and 9.39 (6.58–11.84) U/l in patients with acute pancreatitis, chronic pancreatitis, pancreatic cancer, and healthy controls, respectively. Serum ADA levels were significantly higher in acute and chronic pancreatitis, and pancreatic cancer patients compared to the control group (p < 0.05). Pancreatic cancer patients had significantly higher serum ADA levels when compared with acute and chronic pancreatitis cases (p < 0.05). The serum ADA levels were comparable according to tumor size and location and the presence of metastases. There was a linear correlation between serum ADA and CA 19-9 levels (p = 0.027, r = 0.552). Conclusions: Our data suggest that the ADA enzyme may play a role in inflammatory diseases of the pancreas. Serum ADA levels increase in pancreatic disorders especially in pancreatic cancer. It may be a serum marker for the diagnosis of pancreatic cancer.

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Citation Excerpt :
An increase in ADA activity results in inflammation and tissue injury [83]. High ADA activity occurs in various diseases and disorders including different cancers (Table 1), in addition, its association with disease staging [46,84–94] and, cancer staging both, in serum [95–100] and in cancerous tissues [98,101–104] has been reported. This suggests ADA activity as an effective biomarker to diagnose disease and monitor the therapeutic success.
Adenosine deaminase is a critical enzyme in purine metabolism that regulates intra and extracellular adenosine concentrations by converting it to inosine. Adenosine is an important purine that regulates numerous physiological functions by interacting with its receptors. Adenosine and consequently adenosine deaminase can have pro or anti-inflammatory effects on tissues depending on how much time has passed from the start of the injury. In addition, an increase in adenosine deaminase activity has been reported for various diseases and the significant effect of deaminase inhibition on the clinical course of different diseases has been reported. However, the use of inhibitors is limited to only a few medical indications. Data on the increase of adenosine deaminase activity in different diseases and the impact of its inhibition in various cases have been collected and are discussed in this review. Overall, the evidence shows that many studies have been done to introduce inhibitors, however, in vivo studies have been much less than in vitro, and often have not been expanded for clinical use.
Split aptamer based sensing platform for adenosine deaminase detection by fluorescence resonance energy transfer
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In this paper, a split aptamer based fluorescence resonance energy transfer (FRET) platform was constructed for the determination of adenosine deaminase (ADA) activity by using gold nanoclusters (AuNCs) and gold nanoparticles (AuNPs). A single adenosine triphosphate (ATP) aptamer was split into two fragments (referred to as P1 and P2). P1 was covalently attached to the AuNCs at the 5′ end (P1-AuNCs), and P2 was labeled with AuNPs at the 3′ end (P2-AuNPs). In the presence of ATP, ATP bound with the two fragments with high affinity to link P1-AuNCs and P2-AuNPs together, thus the fluorescence of P1-AuNCs was quenched via FRET from P1-AuNCs to P2-AuNPs. With the addition of ADA, ATP was transformed into inosine triphosphate (ITP), and then P1 and P2 were released to cause the fluorescence recovery of the system. So a split aptamer based FRET platform for ADA detection can be established via the fluorescence intensity change of the system. This platform showed a good linear relationship between the fluorescence intensity and ADA concentration in the range of 2–120 U L⁻¹, and the limit of detection (LOD) was 0.72 U L⁻¹. Moreover, the detection of ATP in human serum sample demonstrated the accuracy and applicability of the method for ADA detection in real sample.
Stimulation of splenic and lymphocytic acetylcholinesterase and adenosine deaminase activities in Rhamdia quelen experimentally infected with Pseudomonas aeruginosa: Impairment of immune system
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The adenosinergic signaling system plays an important role in bacterial infections, modulating inflammation and the immune response due to the regulation of adenosine (Ado) levels; this molecule has anti-inflammatory properties and protects the host against cellular and tissue damage (Baldissera et al., 2016). Adenosine deaminase (ADA) catalyzes the irreversible deamination of deoxyadenosine and adenosine into deoxyinosine and inosine, respectively (Ibis et al., 2007). This enzyme is present in all cell types, and exerts a fundamental role in the proliferation and differentiation of lymphocytes (Frode and Medeiros, 2011).
Appropriate control of immune responses is a critical determinant of fish health. The cholinergic and adenosinergic systems have important roles in the immune response, since acetylcholine (ACh) and adenosine (Ado) possess important anti-inflammatory properties and modulate the immune response during infectious diseases. Thus, the aim of this study was to evaluate whether splenic and lymphocytic adenosinergic and cholinergic systems are able to modulate the immune response during Pseudomonas aeruginosa infection. Acetylcholinesterase (AChE) and adenosine deaminase (ADA) activities in spleen tissue and splenic lymphocytes increased in infected animals compared to uninfected animals. Moreover, plasmatic and splenic metabolites of nitric oxide (NOx) increased in infected animals compared to uninfected animals. Therefore, our results support the hypothesis that the cholinergic and adenosinergic systems are not able to modulate the immune response against P. aeruginosa. In summary, increased AChE and ADA activities exert a pro-inflammatory profile, impairing the immune system and contributing to inflammatory damage.
Cattle naturally infected by Eurytrema coelomaticum: Relation between adenosine deaminase activity and zinc levels
2017, Research in Veterinary Science
Citation Excerpt :
Adenosine deaminase (E-ADA; EC 3.5.4.4) is an enzyme that actively participates in the metabolism of the adenine nucleotides. It catalyzes the irreversible hydrolytic deamination of deoxyadenosine and adenosine with the production of deoxyinosine and inosine, respectively (Iwaki-Egawa et al., 2004; Ibiş et al., 2007; Pospisilova and Frebort, 2007). This enzyme is present in all cell types, and can increase or decrease their activity during parasitic diseases (Bottari et al., 2014).
The enzyme adenosine deaminase (ADA) is critical for modulating the immune system, and in the presence of zinc, its activity is catalyzed. The aim of this study was to evaluate the ADA activity in pancreas of cattle naturally infected by Eurytrema coelomaticum in relation to the results of zinc levels, pathological findings and parasite load. For this study 51 slaughtered cattle were used. The animals were divided into two groups: Group A consisting of animals naturally infected by E. coelomaticum (n = 33) and Group B of uninfected animals (n = 18). Blood and pancreas were collected of each animal for analysis of zinc and ADA, respectively. Infected cattle showed a reduction on seric levels of zinc, and decreased ADA activity in the pancreas (P > 0.05). A positive correlation between zinc levels and ADA activity was observed. Thus, high parasite load and severity of histopathologic lesions affect the ADA activity in pancreas, as well as the zinc levels in serum of infected animals (negative correlation between these variables). Therefore, we can conclude that cattle infected by E. coelomaticum have low ADA activity in pancreas, which can be directly related to zinc reduction, responsible for ADA activation and catalyzes.
Screening for pancreatic cancer
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Similarly, because diabetes is commonly associated with pancreatic adenocarcinoma, either because of age-related incidence or as a consequence of pancreatic injury [111], the ability of a biomarker to discriminate pancreatic adenocarcinoma from other causes of diabetes is also desirable, although rarely evaluated in published biomarker studies. Several biomarkers have been evaluated in serum or plasma from pancreatic adenocarcinoma cases [112–120]. None have yielded sufficiently high sensitivity or specificity to be considered useful for screening as individual biomarkers.
Serum adenosine deaminase activity as a predictor of disease severity in ulcerative colitis
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Giblett et al.37 was the first that demonstrated the vital and putative role of ADA on the immune system's function in patients with severe combined immunodeficiency. Moreover as a sign of cell-mediated immune response, serum concentrations of ADA have been proposed to be elevated in several inflammatory and autoimmune conditions including infectious diseases, SLE, celiac disease, acute appendicitis, Graves’ disease, RA and tuberculosis.14–19,38,39 In a recent study by Maor et al.40 it has been demonstrated that serum total ADA levels were also elevated in active CD.
Ulcerative colitis (UC) is a chronic inflammatory disease characterized by recurrent inflammation and ulcerations of colonic mucosa and an inappropriate and delayed healing. Adenosine deaminase (ADA) is a cytoplasmic enzyme involved in the catabolism of purine bases, capable of catalyzing the deamination of adenosine, forming inosine in the result process. Although ADA has been shown to increase in several inflammatory conditions, there are no literature data indicating an alteration in UC.
This study evaluated the activity of total ADA in serum of 43 patients with UC and 18 healthy controls. Patients’ age, disease duration, drug intake, and other medical history were all noted for each subject. Complete blood count, erythrocyte sedimentation rate (ESR), and C-reactive protein (CRP) were determined for both patients and controls. Correlation analysis was also performed between ADA and other inflammation markers of UC.
Serum mean ADA levels were 11.12 ± 2.03 and 7.99 ± 2.04 U/l for patients with UC in active state and in remission and 8.55 ± 2.26 U/l in the healthy control group. Mean serum ADA levels were significantly elevated in active UC patients compared with patients with UC in remission and control groups. Overall accuracy of ADA in determination of active UC was 83.7 with sensitivity 83.3%, specificity 84.2%.
Serum ADA levels were found to be elevated in UC patients in active state suggesting a partial role of activated T-cell response in the disease pathophysiology. Further randomized controlled studies are warranted to demonstrate the role of ADA in UC patients, with a special interest in specifically targeted therapies against ADA for achieving disease remission.

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¹: Seyfettin Köklü, MD Karargahtepe mahallesi Kumrulu sokak, 18/1 Keçiören, Ankara (Turkey) Tel. +90 312 361 2568, Fax +90 312 312 4120

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Serum Adenosine Deaminase Levels in Pancreatic Diseases

Abstract

Clin Biochem

Free Radic Biol Med

Pancreatology

Gastroenterology

Lancet

Free Radic Biol Med

Pancreatology

Clin Biochem

Two forms of adenosine deaminase in pig epidermis

J Dermatol

Adenosine deaminase complexing proteins are localized in exocrine glands of the rabbit

J Histochem Cytochem

Distribution of adenosine deaminase complexing protein in human tissues

J Histochem Cytochem

Adenosine deaminase activity in lymphocytes

Br J Haematol

Serum adenosine deaminase activity and its isoenzyme pattern in patients with systemic lupus erythematosus

Clin Exp Rheumatol

Adenosine deaminase activity and its isoenzyme pattern in patients with juvenile rheumatoid arthritis and systemic lupus erythematosus

Clin Rheumatol

Deaminase in progressive systemic sclerosis

Acta Dermatol Venereol

Serum adenosine deaminase and total superoxide dismutase activities before and after surgical removal of cancerous laryngeal tissue

J Laryngol Otol

Serum enzymes in head and neck cancer III

J Laryngol Otol

Serum adenosine deaminase, 5t'-nucleotidase and alkaline phosphates in breast cancer patients

Indian J Med Res

Multienzyme patterns of serum adenosine deaminase by agar gel electrophoresis: an evaluation of the diagnostic value in lung cancer

Clin Chim Acta