Plasma matrix metalloproteinase and tissue inhibitor of metalloproteinase in patients with agnogenic myeloid metaplasia or idiopathic primary myelofibrosis

• Published in: British journal of haematology 2002-12, Vol.119 (3), p.709-712
• Main Authors: Wang, Jen C., Novetsky, Akiva, Chen, Chi, Novetsky, Allan D.
• Format: Article
• Language: English
• Subjects: Aged; agnogenic myeloid metaplasia; Biological and medical sciences; Enzyme-Linked Immunosorbent Assay - methods; Hematologic and hematopoietic diseases; Humans; idiopathic primary myelofibrosis; Leukemias. Malignant lymphomas. Malignant reticulosis. Myelofibrosis; matrix metalloproteinase; Matrix Metalloproteinases - metabolism; Medical sciences; Middle Aged; Polycythemia Vera - blood; Primary Myelofibrosis - blood; Thrombocythemia, Essential - blood; Thrombocytosis - blood; tissue inhibitor of metalloproteinase; Tissue Inhibitor of Metalloproteinases - metabolism
• ISSN: 0007-1048; 1365-2141
• DOI: 10.1046/j.1365-2141.2002.03874.x

Agnogenic myeloid metaplasia (AMM) is characterized by bone marrow fibrosis with abnormal accumulation of extracellular matrix components (ECM), which is dependent on the balance between matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). Twenty‐five patients with AMM, 30 with essential thrombocythemia (ET), 12 with polycythemia vera (PV) and 20 normal control subjects were studied. AMM patients had decreased plasma levels of MMP‐3 and marked elevated levels of TIMP‐1, but MMP‐1, MMP‐2 and MMP‐9 levels were not significantly different from control subjects. Elevated levels of plasma TIMP‐1, but not MMPs, were found in ET and PV. Reduced MMP activity together with increased TIMP‐1 activity may be essential in fibrosis formation.