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Polyamines and membrane proteins in sickle cell disease

C L Natta, L T Kremzner

    Blood Cells
    |January 1, 1982
    PubMed
    Summary

    Polyamines like putrescine, spermidine, and spermine are elevated in sickle cell disease red blood cells (RBCs). These polyamines bind to spectrin, potentially altering RBC membrane properties.

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    Area of Science:

    • Biochemistry
    • Hematology
    • Cell Biology

    Background:

    • Polyamines (putrescine, spermidine, spermine) play roles in cell growth and membrane stability.
    • Previous research suggests polyamine involvement in various cellular processes.

    Purpose of the Study:

    • To investigate polyamine levels in red blood cells (RBCs) of individuals with sickle cell disease (SS and SC) compared to controls (AA).
    • To determine the association of polyamines with specific RBC membrane components, particularly spectrin.
    • To explore the potential impact of altered polyamine levels on sickle RBC membrane properties.

    Main Methods:

    • Quantification of polyamine levels in RBC stroma and lysates from SS, SC, and AA individuals.
    • Isolation and analysis of the crude spectrin fraction from RBC stroma.
    • Preliminary experiments involving 14C-putrescine incorporation into washed RBCs from SS and AA subjects.

    Main Results:

    • Significantly elevated polyamine levels (putrescine, spermidine, spermine) were observed in RBC stroma and lysates of SS and SC patients compared to AA controls.
    • A substantial fraction of stroma polyamines was found associated with the crude spectrin fraction.
    • Spermine levels were notably high in SS lysates, intermediate in SC, and undetectable in AA.
    • Evidence of extensive 14C-putrescine incorporation into red cell protein, forming labeled N-(gamma-glutamyl) putrescine, indicating covalent binding.

    Conclusions:

    • Sickle cell disease is associated with significantly increased polyamine levels in red blood cells.
    • Polyamines preferentially bind to spectrin in the RBC stroma.
    • Elevated polyamines, particularly when bound to spectrin, may alter the physical-chemical properties of sickle RBC membranes, potentially contributing to disease pathophysiology.
    • Polyamines can be covalently bound to red cell proteins.

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