Ca2+ transport activities of inside-out vesicles prepared from density-separated erythrocytes from rat and human.

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  • Author(s): Seidler NW;Seidler NW; Swislocki NI
  • Source:
    Molecular and cellular biochemistry [Mol Cell Biochem] 1991 Jul 10; Vol. 105 (2), pp. 159-69.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Springer Country of Publication: Netherlands NLM ID: 0364456 Publication Model: Print Cited Medium: Print ISSN: 0300-8177 (Print) Linking ISSN: 03008177 NLM ISO Abbreviation: Mol Cell Biochem Subsets: MEDLINE
    • Publication Information:
      Publication: New York : Springer
      Original Publication: The Hague, Dr. W. Junk B. V. Publishers.
    • Subject Terms:
      Erythrocyte Aging*; Calcium/*blood ; Calcium-Transporting ATPases/*blood ; Erythrocyte Membrane/*metabolism; Acetylcholinesterase/blood ; Adenosine Triphosphate/blood ; Animals ; Cell Fractionation ; Erythrocytes/metabolism ; Humans ; Rats
    • Abstract:
      The plasma membrane Ca2+ ATPase in erythrocytes is vital for the maintenance of intracellular Ca2+ levels. Since the cytoplasmic Ca2+ concentration is elevated in older erythrocytes, the properties of the Ca2+ transport ATPase were examined during cell aging using inside-out vesicles (IOVs) prepared from density-separated, young (less dense, Ey) and old (more dense, Eo) rat and human erythrocytes. The transport of Ca2+ and the coupled hydrolysis of ATP were measured using radiolabeled substrates. The calmodulin-independent Ca2+ transport activity (Ey, 38.8 vs. Eo, 23.3 nmols/min/mg IOV protein) and the Ca2+ dependent ATP phosphohydrolase activity (Ey, 53.5 vs. Eo, 48.8 nmols/min/mg protein) were greater in IOVs prepared from younger (less dense) rat erythrocytes. The calmodulin-independent Ca2+ transport activity in IOVs from human erythrocytes was 12.9 nmols/min/mg IOV protein for Ey and 10.7 nmols/min/mg IOV protein for Eo. Inside-out vesicles from older (more dense) cells exhibited a lower pumping efficiency as determined by the calculated stoichiometry, molecule of Ca2+ transported per molecule of ATP hydrolyzed (rat: Ey, 0.74 vs. Eo, 0.49; human: Ey, 1.22 vs. Eo, 0.77). The enzymatic activity of rat and human Ey IOVs was labile. The Ca2+ transport activity in Ey but not Eo IOVs rapidly declined during cold storage (4 degrees C). The decrease in Ca2+ transport activity during aging may accentuate the age-related decline in several erythrocytic properties.
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    • Accession Number:
      8L70Q75FXE (Adenosine Triphosphate)
      EC 3.1.1.7 (Acetylcholinesterase)
      EC 7.2.2.10 (Calcium-Transporting ATPases)
      SY7Q814VUP (Calcium)
    • Publication Date:
      Date Created: 19910710 Date Completed: 19911031 Latest Revision: 20191210
    • Publication Date:
      20250114
    • Accession Number:
      10.1007/BF00227755
    • Accession Number:
      1833624