Cell surface adenosine deaminase: Much more than an ectoenzyme

@article{Franco1997CellSA,
  title={Cell surface adenosine deaminase: Much more than an ectoenzyme},
  author={Rafael Franco and Vicent Casad{\'o} and Francisco Ciruela and Carles Saura and Josefa Mallol and Enric I. Canela and Carmen Lluis},
  journal={Progress in Neurobiology},
  year={1997},
  volume={52},
  pages={283-294}
}
Ecto‐adenosine deaminase: An ecto‐enzyme and a costimulatory protein acting on a variety of cell surface receptors
TLDR
Apart from degrading extracellular Ado or dAdo, which are toxic for lymphocytes and other cells, ecto‐ADA has got an extraenzymatic function by means of its interaction with cell surface proteins.
Adenosine A2B receptors behave as an alternative anchoring protein for cell surface adenosine deaminase in lymphocytes and cultured cells.
TLDR
It is demonstrated that cell surface ADA in ADA+/CD26- T lymphocytes anchors to adenosine receptors of the A2B subtype (A2BR), and binding of ADA to A2BR increases the affinity of the agonist 5'-N-ethylcarboxamidoadenosine and cAMP production.
Adenosine A 2 B Receptors Behave as an Alternative Anchoring Protein for Cell Surface Adenosine Deaminase in Lymphocytes and Cultured Cells
TLDR
It is demonstrated that cell surface ADA in ADA/CD26 T lymphocytes anchors to adenosine receptors of the A2B subtype (A2BR) and binding of ADA to A2BR increases the affinity of the agonist 59-Nethylcarboxamidoadenosine and cAMP production.
Enzymatic and extraenzymatic role of ecto‐adenosine deaminase in lymphocytes
TLDR
The fact that, besides CD26, ADA can interact with different cell‐surface proteins opens new perspectives in the research for a role of ecto‐ADA in the function of the immune system and in the Interactions that take place between different cells in the development of theimmune system.
Molecular Evidence of Adenosine Deaminase Linking Adenosine A2A Receptor and CD26 Proteins
TLDR
Direct evidence of the specific formation of trimeric complexes CD26-ADA-A2AR involving two cells is shown and it is demonstrated that A2AR-NanoLuc fusion proteins are functional.
Secreted Bacterial Adenosine Deaminase Is an Evolutionary Precursor of Adenosine Deaminase Growth Factor
TLDR
This finding provides the first example of evolution of an extracellular eukaryotic signaling protein from a secreted bacterial analogue with identical activity and suggests a potential role of ADGF/ADA2 in bacterial communication.
CD26 and adenosine deaminase interaction: its role in the fusion between horse membrane vesicles and spermatozoa.
TLDR
The fusion process between horse sperm cells and vesicles was evidenced by confocal microscopy, which showed the localization of CD26 at the postacrosomal region and at the midpiece of the spermatozoa after incubation with vesicle, suggesting that the interaction CD26/ecto-ADA might be responsible for fusion.
Adenosine deaminase: Functional implications and different classes of inhibitors
TLDR
A number of ADA inibitors have been designed and synthesized, classified as ground‐state and transition‐state inhibitors, which may be used to mimic the genetic deficiency of the enzyme, in lymphoproliferative disorders or immunosuppressive therapy, to potentiate the effect of antileukemic or antiviral nucleosides, and, together with adenosine kinase, to reduce breakdown ofadenosine in inflammation, hypertension, and ischemic injury.
The A2B adenosine receptor colocalizes with adenosine deaminase in resting parietal cells from gastric mucosa
TLDR
The findings demonstrate that A2BR and ADA are expressed in cell membranes isolated from gastric parietal cells and suggest a tight association between A2 BR and ADA that might be specifically linked to glandular secretory function.
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References

SHOWING 1-10 OF 94 REFERENCES
Adenosine Deaminase Interacts with A1 Adenosine Receptors in Pig Brain Cortical Membranes
TLDR
It is shown that adenosine deaminase and A1Adenosine receptors interact in pig brain cortical membranes, the first report in brain demonstrating an interaction between a degradative ectoenzyme and the receptor whose ligand is the enzyme substrate.
Characterization of adenosine deaminase binding to human CD26 on T cells and its biologic role in immune response.
TLDR
The data suggest that ADA on the cell surface is involved in an important immunoregulatory mechanism by which released ADA binds to cell surface CD26, and this complex is capable of reducing the local concentration of adenosine.
Presence of adenosine deaminase on the surface of mononuclear blood cells: immunochemical localization using light and electron microscopy.
TLDR
It is demonstrated that adenosine deaminase can be found associated with the plasma membrane of lymphocytes and monocytes, and new hypotheses about the mechanisms involving purine metabolism in immune dysfunctions or immunodeficiency syndromes may be considered.
Adenosine deaminase of cultured brain cells.
TLDR
The evidence that points to adenosine and its derivatives as neurohumoral modulators of central-nervous-system function is discussed, including the case of mouse neuroblastoma and neonatal hamster astrocytes.
Direct association of adenosine deaminase with a T cell activation antigen, CD26.
TLDR
CD26, the T cell activation molecule dipeptidyl peptidase IV (DPPIV), associates with a 43-kilodalton protein, which may provide a clue to the pathophysiology of SCID caused by ADA deficiency.
Surface expression of adenosine deaminase in mitogen‐stimulated lymphocytes
TLDR
Results suggest a role for ecto‐adenosine deaminase in lymphocyte proliferation and/or triggering in mitogen‐stimulated lymphocytes and suggest a correlation between ADA and CD71 expression.
Human adenosine deaminase. Distribution and properties.
Control of nucleoside transport in neural cells. Effect of protein kinase C activation.
TLDR
There is recent evidence of the interaction between adenosine receptors and transporters in this cellular model, where the A2 agonist, NECA, activates theAdenosine transport6.
Expression of ecto-adenosine deaminase and CD26 in human T cells triggered by the TCR-CD3 complex. Possible role of adenosine deaminase as costimulatory molecule.
TLDR
The set of results strongly indicates that ADA binding to CD26 produces a costimulatory response in T cell activation events.
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