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Human fibrinogen.

J A Shafer1, D L Higgins

  • 1Department of Biological Chemistry, University of Michigan, Ann Arbor.

Critical Reviews in Clinical Laboratory Sciences
|January 1, 1988
PubMed
Summary
This summary is machine-generated.

This review details human fibrinogen and fibrin structure, function, and metabolism. It explores protein interactions crucial for hemostasis and thrombosis, and discusses genetic regulation of fibrinogen synthesis.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Hematology

Background:

  • Fibrinogen and fibrin are key proteins in hemostasis and thrombosis.
  • Understanding their structure-function relationships is critical for clinical applications.

Purpose of the Study:

  • To review the structure and physical properties of human fibrinogen and fibrin.
  • To examine protein interactions relevant to thrombosis and hemostasis.
  • To discuss genetic regulation of fibrinogen synthesis and catabolism.

Main Methods:

  • Literature review of structural and functional studies.
  • Analysis of kinetic and thermodynamic parameters of protein interactions.
  • Discussion of genetic and regulatory mechanisms.

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Main Results:

  • Detailed characterization of fibrinogen to fibrin conversion pathway.
  • Delineation of structural determinants for protein interactions.
  • Correlation of fibrinogen mutations with altered hemostatic properties.

Conclusions:

  • Fibrinogen structure and interactions are central to hemostasis and thrombosis.
  • Genetic factors significantly influence fibrinogen function.
  • Further research can elucidate mechanisms for therapeutic interventions.