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Human Placental Adenosine A2-Like Binding Sites Properties and Homology with Mammalian and Avian Stress Proteins

  • K. A. Hutchison
  • B. Nevins
  • F. Perini
  • I. H. Fox
Conference paper

Abstract

Adenosine is a biologically active compound at two cell surface receptors, the adenosine A1 and the adenosine A2 receptors. The adenosine A1 receptor has been labeled and characterized with selective adenosine analogs. The adenosine A2 receptor has been labeled using N-ethylcarboxamidoadenosine (NECA). However, in most tissues the majority of definable specific NECA binding is to the ubiquitous adenosine A2-like binding sites which has properties that distinguish it from the adenosine A2 receptor (Lohse et al., 1988). One of the major differences in binding relates to the high affinity binding of N6 substituted adenosine analogs and C8 substituted xanthines to the adenosine A2 receptor and the lack of binding of these compounds to the adenosine A2-like binding site.

Keywords

Partial Specific Volume Adenosine Analog Placental Membrane Stokes Radius Tumor Rejection Antigen 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Hutchison, K.A. et al., 1989, Soluble human adenosine A2-like binding site: Properties and homology with human membrane adenosine A2-like binding site, hamster GRP 94, murine ERP99 and GP96, and chicken HSP 108. J. Biol Chem. (Submitted for publication).Google Scholar
  2. Hutchison, K.A. and I.H. Fox, 1989, Purification and characterization of the adenosine A2-like binding site from human placental membranes. J. Biol. Chem. (In press).Google Scholar
  3. Lohse, M.J. et al., 1988, Separation of solubilized A2 adenosine receptors of human platelets from non-receptor [3H]NECA binding sites by gel filtration. Naunyn Schmiedeberg’s Arch. Pharmacol. 337:64–68.Google Scholar

Copyright information

© Springer-Verlag New York Inc. 1990

Authors and Affiliations

  • K. A. Hutchison
  • B. Nevins
  • F. Perini
  • I. H. Fox

There are no affiliations available

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