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BIOCHEMICAL EFFECT OF FIBRINOGEN

CHAPTER ONE

INTRODUCTION

1.1         FIBRINOGEN

Fibrinogen is a 340-kDa glycoprotein synthesized in the liver, with a multitude of functions including fibrin clot formation, non-substrate thrombin binding, platelet aggregation and fibrinolysis. The first clinical report of congenital afibrinogenemia dates back to 1920 when a 9-year-old boy suffering from recurrent bleeding episodes since birth and lacking fibrinogen in blood was described and shown subsequently to be autosomal recessive in inheritance with variable penetrance (Lang et al., 2009). The estimated prevalence of afibrinogenemia which is the most severe form of the disorder is around 1 in 1 000 000 and recent registries from Italy, Iran and North America have greatly improved understanding of the clinical  spectrum of presentation (Kollman et al., 2009). However, knowledge on the incidence of these disorders has been confounded by publication bias. In populations where consanguinity is high, as noted in the Iranian Registry, the prevalence may be similar to other autosomal recessive disorders. In fact, a sevenfold higher incidence of fibrinogen disorders was observed in the Iranian Registry for Rare Bleeding Disorders in

TABLE OF CONTENT

CHAPTER ONE

1.0     Introduction

1.1     Fibrinogen

1.1.1  Fibrinogen Synthesis

1.1.2  Functions of Fibrinogen

CHAPTER TWO

2.0     Types of fibrinogen disorders

2.1     Clinical manifestations

2.1.1  Hypofibrinogenemia

2.1.2  Dysfibrinogenemia

2.2     Laboratory diagnosis

2.2.1  Molecular diagnosis

2.2.2  Dysfibrinogenemia mutations

2.2.3  Prenatal diagnosis

CHAPTER THREE

3.0     Fibrinogen Replacement

3.1     Fresh Frozen Plasma

3.2     Cryoprecipitate

3.3     Fibrinogen Concentrate

3.4     Current understanding of fibrinogen replacement

3.4.1  Preclinical Data

3.4.2  Clinical Data

3.4.2.1 Trauma

3.4.2.2 Perioperative Bleeding

CHAPTER FOUR

4.0     Conclusion and Recommendation

4.1     Conclusion

4.2     Recommendation

References.

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