Localization of GTP cyclohydrolase I in human peripheral blood smears using a specific monoclonal antibody and an immune-alkaline phosphatase labeling technique.
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.
Schoedon
G
G
Department of Pediatrics, University of Zurich, Switzerland.
Curtis
H C
HC
Niederwieser
A
A
D000469:Alkaline Phosphatase; D000619:Aminohydrolases / Q000097:blood*; D000911:Antibodies, Monoclonal; D001708:Biopterins / Q000031:analogs & derivatives* / Q000096:biosynthesis; D001773:Blood Cells / Q000201:enzymology*; D006136:GTP Cyclohydrolase / Q000097:blood*; D006801:Humans; D007124:Immunoenzyme Techniques
D000911:Antibodies, Monoclonal; D001708:Biopterins; D000469:Alkaline Phosphatase; D000619:Aminohydrolases; D006136:GTP Cyclohydrolase; C003402:sapropterin