Effect of L-asparaginase on Some Hemostatic Proteins during Induction Chemotherapy in Childhood Acute Lymphoblastic Leukemia

Acute lymphoblastic leukemia (ALL) is the most common pediatric cancer, accounting for a quarter of all malignancies diagnosed among children aged < 15 years it is a malignant proliferation of lymphoid precursor cells in the bone marrow, blood and extramedullary sites its peak incidence occurs between age 2 and 5 years affects both children and adultsSteady progress in development of effective treatments has led to a cure rate of more than 80% in children, creating opportunities for innovative approaches that would preserve past gains in leukemia-free survival while reducing the toxic side-effects of current intensive regimens .L-asparaginase is an important chemotherapeutic agent used for the treatment of a variety of lymphoproliferative disorders and lymphomas, acute lymphoblastic leukemia in particular. It has been a mainstay of combination chemotherapy protocols used in treatment of pediatric ALL for almost 30 yearsL-asparaginase, a potent lympholytic agent, is an essential component of ALL therapy. It is a bacterially derived enzyme, which converts the amino acid asparagine to aspartic acid and ammonia. This leads to rapid depletion of extracellular pools of asparagine in the body. Unlike the normal cells, the lymphoblasts lack the enzyme asparagines synthatase and are dependent on exogenous asparagines supplies making them very susceptible to the cytotoxic effects of asparaginaseThe objective of this work was to study the effect of L-asparaginase on some haemostatic proteins (Fibrinogen (Fg), Antithrombin III (AT) and D-dimer) during induction chemotherapy in childhood acute lymphoblastic leukemia..