CD26/Dipeptidyl Peptidase IV Does Not Work as an Adenosine Deaminase-Binding Protein in Rat Cells

1997 ◽  
Vol 178 (2) ◽  
pp. 180-186 ◽  
Author(s):  
Sachiko Iwaki-Egawa ◽  
Yasuhiro Watanabe ◽  
Yukio Fujimoto
Keyword(s):  
Adenosine Deaminase ◽  
Binding Protein ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv

scholarly journals Influence of dipeptidyl peptidase IV on enzymatic properties of adenosine deaminase.

2006 ◽  
Vol 53 (3) ◽  
pp. 539-546 ◽  
Author(s):  
Svetlana Sharoyan ◽  
Alvard Antonyan ◽  
Sona Mardanyan ◽  
Giulio Lupidi ◽  
Gloria Cristalli
Keyword(s):  
Adenosine Deaminase ◽  
Immune Cell ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Soluble Form ◽  
Kidney Cortex ◽  
Peptidase Activity ◽  
Extracellular Medium ◽  
Ph Profile ◽  
Enzyme Preparations

The importance of ADA (adenosine deaminase) in the immune system and the role of its interaction with an ADA-binding cell membrane protein dipeptidyl peptidase IV (DPPIV), identical to the activated immune cell antigen, CD26, has attracted the interest of researchers for many years. To investigate the specific properties in the structure-function relationship of the ADA/DPPIV-CD26 complex, its soluble form, identical to large ADA (LADA), was isolated from human blood serum, human pleural fluid and bovine kidney cortex. The kinetic constants (Km and Vmax) of LADA and of small ADA (SADA), purified from bovine lung and spleen, were compared using adenosine (Ado) and 2'-deoxyadenosine (2'-dAdo) as substrates. The Michaelis constant, Km, evidences a higher affinity of both substrates (in particular of more toxic 2'-dAdo) for LADA and proves the modulation of toxic nucleoside neutralization in the extracellular medium due to complex formation between ADA and DPPIV-CD26. The values of Vmax are significantly higher for SADA, but the efficiency, Vmax/Km, in LADA-catalyzed 2'-dAdo deamination is higher than that in Ado deamination. The interaction of all enzyme preparations with derivatives of adenosine and erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA) was studied. 1-DeazaEHNA and 3-deazaEHNA demonstrate stronger inhibiting activity towards LADA, the DPPIV-CD26-bound form of ADA. The observed differences between the properties of the two ADA isoforms may be considered as a consequence of SADA binding with DPPIV-CD26. Both SADA and LADA indicated a similar pH-profile of adenosine deamination reaction with the optimum at pHs 6.5-7.5, while the pH-profile of dipeptidyl peptidase activity of the ADA/DPPIV-CD26 complex appeared in a more alkaline region.

Adenosine deaminase, dipeptidyl peptidase-IV activities and lipid peroxidation are increased in the saliva of obese young adult

2015 ◽  
Vol 53 (7) ◽  
Author(s):  
Eduardo Ottobelli Chielle ◽  
Gabriela Bonfanti ◽  
Karine Santos De Bona ◽  
Rafael Noal Moresco ◽  
Maria Beatriz Moretto
Keyword(s):  
Lipid Peroxidation ◽  
Adenosine Deaminase ◽  
Inflammatory Diseases ◽  
Dipeptidyl Peptidase ◽  
Normal Weight ◽  
Dipeptidyl Peptidase Iv ◽  
Salivary Biomarkers ◽  
The Metabolic Syndrome ◽  
Dpp Iv ◽  
Young Subjects

AbstractObesity is the hallmark of the metabolic syndrome representing a major global health problem. It is considered a state of chronic inflammation with minimal exploration of salivary biomarkers. Thus, the intent of the present study was to assess the activities of salivary dipeptidyl peptidase IV (DPP-IV), adenosine deaminase (ADA) and lipid peroxidation in obese young and overweight young subjects.ADA, DPP-IV activities and lipid peroxidation were investigated in saliva, as well as insulin, glucose, HbASalivary ADA and DPP-IV activities as well as lipid peroxidation were higher in patients with obesity compared to the normal weight group. Correlations between ADA/DPP-IV activities, lipid peroxidation/ADA activity, ADA activity/hip circumference and BMI/weight were observed.Our results indicate that the increase in the salivary ADA and DPP-IV activities as well as in the lipid peroxidation could be related of the regulation to various aspects of adipose tissue function and inflammatory obesity. It is suggested that these salivary biomarkers may be used as biochemical test in clinical abnormalities present in obesity, in the absence of oral inflammatory diseases.

scholarly journals Clustered Charged Amino Acids of Human Adenosine Deaminase Comprise a Functional Epitope for Binding the Adenosine Deaminase Complexing Protein CD26/Dipeptidyl Peptidase IV

2002 ◽  
Vol 277 (22) ◽  
pp. 19720-19726 ◽  
Author(s):  
Eva Richard ◽  
S. Munir Alam ◽  
Francisco X. Arredondo-Vega ◽  
Dhavalkumar D. Patel ◽  
Michael S. Hershfield
Keyword(s):  
Amino Acids ◽  
Adenosine Deaminase ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Charged Amino Acids

scholarly journals The Binding Site of Human Adenosine Deaminase for Cd26/Dipeptidyl Peptidase IV

2000 ◽  
Vol 192 (9) ◽  
pp. 1223-1236 ◽  
Author(s):  
Eva Richard ◽  
Francisco X. Arredondo-Vega ◽  
Ines Santisteban ◽  
Susan J. Kelly ◽  
Dhavalkumar D. Patel ◽  
...  
Keyword(s):  
Adenosine Deaminase ◽  
Severe Combined Immunodeficiency ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Site Mutation ◽  
Extracellular Adenosine ◽  
Human T Cell ◽  
Helical Segment ◽  
Cell Membrane Protein ◽  
Human T Cell Line

Human, but not murine, adenosine deaminase (ADA) forms a complex with the cell membrane protein CD26/dipeptidyl peptidase IV. CD26-bound ADA has been postulated to regulate extracellular adenosine levels and to modulate the costimulatory function of CD26 on T lymphocytes. Absence of ADA–CD26 binding has been implicated in causing severe combined immunodeficiency due to ADA deficiency. Using human–mouse ADA hybrids and ADA point mutants, we have localized the amino acids critical for CD26 binding to the helical segment 126–143. Arg142 in human ADA and Gln142 in mouse ADA largely determine the capacity to bind CD26. Recombinant human ADA bearing the R142Q mutation had normal catalytic activity per molecule, but markedly impaired binding to a CD26+ ADA-deficient human T cell line. Reduced CD26 binding was also found with ADA from red cells and T cells of a healthy individual whose only expressed ADA has the R142Q mutation. Conversely, ADA with the E217K active site mutation, the only ADA expressed by a severely immunodeficient patient, showed normal CD26 binding. These findings argue that ADA binding to CD26 is not essential for immune function in humans.

scholarly journals Crystal Structure of CD26/Dipeptidyl-peptidase IV in Complex with Adenosine Deaminase Reveals a Highly Amphiphilic Interface

2004 ◽  
Vol 279 (41) ◽  
pp. 43330-43335 ◽  
Author(s):  
Wilhelm A. Weihofen ◽  
Jiango Liu ◽  
Werner Reutter ◽  
Wolfram Saenger ◽  
Hua Fan
Keyword(s):  
Crystal Structure ◽  
Adenosine Deaminase ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv
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