Literature DB >> 7370243

Is inosine the physiological energy source of pig erythrocytes?

S M Jarvis, J D Young, M Ansay, A L Archibald, R A Harkness, R J Simmonds.   

Abstract

Pig erythrocytes are unable to metabolize glucose and their physiological energy source is unknown. These cells have a high-capacity nucleoside transport system with similar properties to that responsible for nucleoside transport in other species. Nucleoside transport is sufficiently rapid to allow the possibility that inosine and/or adenosine may represent major energy substrates for pig erythrocytes in vivo. Normal and adenosine deaminase-deficient pig erythrocytes have similar ATP levels, suggesting that adenosine is not important in this respect. However, it was calculated that an extracellular inosine concentration of only 40 nM could support the cells' entire energy requirement, a value 40-fold lower than plasma levels of this nucleoside.

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Year:  1980        PMID: 7370243     DOI: 10.1016/0005-2736(80)90162-5

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  15 in total

1.  5'-S-(2-aminoethyl)-N6-(4-nitrobenzyl)-5'-thioadenosine (SAENTA), a novel ligand with high affinity for polypeptides associated with nucleoside transport. Partial purification of the nitrobenzylthioinosine-binding protein of pig erythrocytes by affinity chromatography.

Authors:  F R Agbanyo; D Vijayalakshmi; J D Craik; W P Gati; D P McAdam; J Asakura; M J Robins; A R Paterson; C E Cass
Journal:  Biochem J       Date:  1990-09-15       Impact factor: 3.857

2.  Volume-activated Na/H exchange activity in fetal and adult pig red cells: inhibition by cyclic AMP.

Authors:  S Sergeant; D H Sohn; H D Kim
Journal:  J Membr Biol       Date:  1989-08       Impact factor: 1.843

3.  Characterization of monoclonal antibodies that recognize band 4.5 polypeptides associated with nucleoside transport in pig erythrocytes.

Authors:  A H Good; J D Craik; S M Jarvis; F Y Kwong; J D Young; A R Paterson; C E Cass
Journal:  Biochem J       Date:  1987-06-15       Impact factor: 3.857

4.  Demonstration of adenosine deaminase activity in human fibroblast lysosomes.

Authors:  E R Lindley; R L Pisoni
Journal:  Biochem J       Date:  1993-03-01       Impact factor: 3.857

5.  Nucleoside transport in human and sheep erythrocytes. Evidence that nitrobenzylthioinosine binds specifically to functional nucleoside-transport sites.

Authors:  S M Jarvis; J D Young
Journal:  Biochem J       Date:  1980-08-15       Impact factor: 3.857

6.  Proteolytic cleavage of [3H]nitrobenzylthioinosine-labelled nucleoside transporter in human erythrocytes.

Authors:  N S Janmohamed; J D Young; S M Jarvis
Journal:  Biochem J       Date:  1985-09-15       Impact factor: 3.857

7.  Selective protection of tubercidin toxicity by nitrobenzyl thioinosine in normal tissues but not in human neuroblastoma cells.

Authors:  C Kaplinsky; H Yeger; Z Estrov; J Barankiewicz; G Pawlin; M H Freedman; A Cohen
Journal:  Cancer Chemother Pharmacol       Date:  1986       Impact factor: 3.333

8.  Erythrocyte nucleoside transport: asymmetrical binding of nitrobenzylthioinosine to nucleoside permeation sites.

Authors:  S M Jarvis; D McBride; J D Young
Journal:  J Physiol       Date:  1982-03       Impact factor: 5.182

9.  Species differences in nucleoside transport. A study of uridine transport and nitrobenzylthioinosine binding by mammalian erythrocytes.

Authors:  S M Jarvis; J R Hammond; A R Paterson; A S Clanachan
Journal:  Biochem J       Date:  1982-10-15       Impact factor: 3.857

10.  Nucleoside translocation in sheep reticulocytes and fetal erythrocytes: a proposed model for the nucleoside transporter.

Authors:  S M Jarvis; J D Young
Journal:  J Physiol       Date:  1982-03       Impact factor: 5.182

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