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Localization of GTP cyclohydrolase I in human peripheral blood smears using a specific monoclonal antibody and an
G Schoedon1, H C Curtis, A Niederwieser
1Department of Pediatrics, University of Zurich, Switzerland.
Abstract:
GTP cyclohydrolase I, the enzyme catalyzing the first step in the cofactor biosynthesis for the aromatic amino acid hydroxylases, has been localized in situ. By the use of a monoclonal antibody specific to human GTP cyclohydrolase I, the enzyme has been visualized immuno-enzymatically by alkaline phosphatase monoclonal anti-alkaline phosphatase labeling. In routine blood smears lymphocytes, monocytes/macrophages, and granulocytes show strong intraplasmatic staining. Premature erythrocytes show clear staining of the reticulated cytoplasmatic structure, while mature erythrocytes are completely negative. Neither is there any staining for GTP cyclohydrolase I in the blast cells of a case of T-cell acute lymphoblastic leukemia. These results closely confirm the prior finding that mature erythrocytes as well as most malignant mononuclear cells lack GTP cyclohydrolase I activity, and they indicate that in these cells the enzyme protein may be absent.
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