The role of G protein B subunits in the release of ATP from human erythrocytes

• Autorzy: Sprague R.S. , Bowles E.A. , Olearczyk J.J. , Stephenson A.H. , Lonigro A.J.
• Języki publikacji: EN

Abstrakty

EN

Previously, we demonstrated that adenosine triphosphate (ATP) is released from human erythrocytes in response to mechanical deformation and that this release requires activation of a signal-transduction pathway involving adenylyl cyclase and the heterotrimeric G protein, Gs. Here we investigate the role of heterotrimeric G proteins of the Gi subtype in the release of ATP from human erythrocytes. In addition, we determined the profile of heterotrimeric G protein ß submits present in these erythrocyte membranes. The activity of Gi was stimulated by incubation of erythrocytes (20% hematocrit) with mastoparin (10 µM). ATP release was measured using the luciferin/luciferase assay. Heterotrimeric G protein ß subunits present in erythrocyte membranes were resolved using gel electrophoresis and subunit specific antibodies. Incubation of human erythrocytes with mastoparan (an activator ofGi/o) resulted in a 4.1 ±0.6-fold increase in ATP present in the medium (P<0.01). Human erythrocyte membranes stain positively for ß subunit types 1, 2, 3 and 4, all of which been reported to activate of some isoforms of adenylyl cyclase. Activation of the heterotrimeric G protein, Gi, results in ATP release from erythrocytes. This effect is may be related to the activity of ß submits associated with this G protein in the human erythrocyte.

Słowa kluczowe

EN

adenosine triphosphate; G protein; man; erythrocyte; B subunit; adenylyl cyclase

• Wydawca: -
• Czasopismo: Journal of Physiology and Pharmacology
• Rocznik: 2002
• Tom: 53
• Numer: 4,1
• Opis fizyczny: p.667-674,fig.

Twórcy

autor

Sprague R.S.

• Saint Louis University School of Medicine, 1402 South Grand Bldv. St.Louis, MO 63104 USA

autor

Bowles E.A.

autor

Olearczyk J.J.

autor

Stephenson A.H.

autor

Lonigro A.J.