Residue gamma153Cys is essential for the formation of the complexes Aalphagamma and Bbetagamma, assembly intermediates for the AalphaBbetagamma complex and intact fibrinogen

Clin Chim Acta. 2005 Mar;353(1-2):157-64. doi: 10.1016/j.cccn.2004.10.017.

Abstract

Background: Fibrinogen Matsumoto IV was found in a hypofibrinogenemia caused by a heterozygous missense mutation, i.e., the substitution of the fibrinogen gamma-chain residue Cys153 by Arg.

Methods: To examine the precise basis for the fibrinogen deficiency, mixtures of any two vectors, the fibrinogen Aalpha-, Bbeta-, gamma- (153Cys) or gammam-(153Ala) chain were transfected into Chinese hamster ovary cells (CHO-Aalpha/gamma, -Aalpha/gammam, -Bbeta/gamma, -Bbeta/gammam). Expression and constitution of each of two chains and their complexes in the individual CHO cell lines were identified by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) and immunoblot analysis using polypeptide specific antibodies and two-dimensional electrophoresis (2-DE).

Results: In the CHO-Aalpha/gamma and -Bbeta/gamma, the Aalpha/gamma- or Bbeta/gamma-complex was formed, whereas in the CHO-Aalpha/gammam and -Bbeta/gammam, no Aalpha/gammam- or Bbeta/gammam-complex was observed. These results demonstrate that gamma153Ala cannot assemble with the Aalpha- and Bbeta-chains, leading to impaired fibrinogen assembly and secretion.

Conclusion: gamma153Cys is an essential residue for the fibrinogen assembly which is dependent on Aalpha/gamma- and Bbeta/gamma-complex formation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Western
  • CHO Cells
  • Cricetinae
  • Cysteine / chemistry*
  • Electrophoresis, Gel, Two-Dimensional
  • Fibrinogen / chemistry
  • Fibrinogen / metabolism*

Substances

  • Fibrinogen
  • Cysteine