Letter | Published:

Polymerisation of red cell membrane protein contributes to spheroechinocyte shape irreversibility

Nature volume 274, pages 505507 (03 August 1978) | Download Citation

Subjects

Abstract

THE discocyte–spheroechinocyte transformation of red cells undergoing ATP depletion and calcium accumulation is reversible after restoration of normal ATP and calcium levels or exposure of cells to stomacytogenic agents such as cationic anaesthetics1–3. This transformation becomes irreversible after a prolonged incubation without glucose or an introduction of high calcium concentrations into the cells.4 In our studies of membrane protein composition of metabolically depleted red cells, we have noted that aerobically ATP-depleted erythrocytes contained a >1 × 106-dalton reducible membrane protein polymer which was selectively enriched in spectrin, the major protein at the cytosol membrane interface5. We suggested that the formation of this complex was due to changes in the assembly of spectrin in ATP-depleted red cell membranes to form closer contacts, allowing a spontaneous crosslinking of the nearest spectrin neighbours through disulphide couplings5. Another polymer differing from that in ATP-depleted red cells by an absence of cleavage with reducing agents was recently noted in fresh red cells, into which Ca2+ (>0.5 mM) was introduced by ionophore A23187 (ref. 6); it has been attributed to a crosslinking of γ-glutamyl ε-lysine residues of spectrin and other membrane proteins, catalysed by a Ca2+-activated cytoplasmic transglutaminase6,7. As both the above membrane protein polymers were found in cells which transformed into spheroechinocytic shape, we have studied and report here results which show that such spontaneous membrane protein crosslinking contributes to a permanent fixing of the red cells to their abnormal shape.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

References

  1. 1.

    , & J. clin. Invest. 48, 795–809 (1969).

  2. 2.

    , , & Biochemistry 45, 487 (1961).

  3. 3.

    et al. Blood 50, 155–163 (1977).

  4. 4.

    Am. J. Path. 77, 507–514 (1974).

  5. 5.

    , & Blood 51, 385–395 (1978).

  6. 6.

    & Proc. natn. Acad. Sci. U.S.A. 73, 4479–4481 (1976).

  7. 7.

    , & J. biol. Chem. 252, 6617–6623 (1977).

  8. 8.

    Nouv. Revue fr. Hémat. 12, 1–25 (1972).

  9. 9.

    Red Cell Metabolism: A Manual of Biochemical Methods 2nd edn (Grune and Stratton, New York, 1975).

  10. 10.

    , & Biochemistry 16, 4066–4074 (1977).

  11. 11.

    , , & J. Lab. clin. Med. 89, 41–50 (1977).

  12. 12.

    , & Membranes and Diseases (eds Bolis, L., Hoffman, J. F. & Leaf, A.) 41–60 (Raven, New York, 1976).

Download references

Author information

Affiliations

  1. Hematology Research Laboratory, St. Vincent Hospital, University of Massachusetts Medical School, Worcester, Massachusetts 01610

    • JIRI PALEK
    • , P. A. LIU
    •  & S. C. LIU

Authors

  1. Search for JIRI PALEK in:

  2. Search for P. A. LIU in:

  3. Search for S. C. LIU in:

About this article

Publication history

Received

Accepted

Published

DOI

https://doi.org/10.1038/274505a0

Further reading

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.