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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Hoffman, Joseph F. Galan, Jacob A. Low, Philip S. Tao, W. Andy Chu, Haiyan Puchulu-campanella, Estela |
| Description | Author Affiliation: Chu H ( Department of Chemistry and Biochemistry, Purdue University, West Lafayette, IN 47907, USA.); |
| Abstract | The type of metabolic compartmentalization that occurs in red blood cells differs from the types that exist in most eukaryotic cells, such as intracellular organelles. In red blood cells (ghosts), ATP is sequestered within the cytoskeletal–membrane complex. These pools of ATP are known to directly fuel both the $Na^{+}/K^{+}$ and $Ca^{2+}$ pumps. ATP can be entrapped within these pools either by incubation with bulk ATP or by operation of the phosphoglycerate kinase and pyruvate kinase reactions to enzymatically generate ATP. When the pool is filled with nascent ATP, metabolic labeling of the $Na^{+}/K^{+}$ or $Ca^{2+}$ pump phosphoproteins $(E_{Na}-P$ and $E_{Ca}-P,$ respectively) from bulk $[γ-^{32}P]-ATP$ is prevented until the pool is emptied by various means. Importantly, the pool also can be filled with the fluorescent ATP analog trinitrophenol ATP, as well as with a photoactivatable ATP analog, 8-azido-ATP $(N_{3}-ATP).$ Using the fluorescent ATP, we show that ATP accumulates and then disappears from the membrane as the ATP pools are filled and subsequently emptied, respectively. By loading $N_{3}-ATP$ into the membrane pool, we demonstrate that membrane proteins that contribute to the pool’s architecture can be photolabeled. With the aid of an antibody to $N_{3}-ATP,$ we identify these labeled proteins by immunoblotting and characterize their derived peptides by mass spectrometry. These analyses show that the specific peptides that corral the entrapped ATP derive from sequences within β-spectrin, ankyrin, band 3, and GAPDH. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 31 |
| Volume Number | 109 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2012-08-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Adenosine Triphosphate Analogs & Derivatives Azides Metabolism Calcium Channels Cytoskeleton Erythrocyte Membrane Sodium-Potassium-Exchanging ATPase Pharmacology Anion Exchange Protein 1, Erythrocyte Ankyrins Antibodies Chemistry Glyceraldehyde-3-Phosphate Dehydrogenases Spectrin Research Support, N.I.H., Extramural Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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