Cytochemical localization of alkaline and acid phosphatase in human vanishing bone disease.
This report is the first cytochemical investigation of vanishing bone disease "Gorham's Disease" (Gorham and Stout 1955). The ultrastructural localization of non-specific alkaline phosphatase and of specific and non-specific acid phosphatase activity was studied in slices of tissue removed from a patient with this rare disorder. Sodium beta-glycerophosphate and phosphorylcholine chloride were used as substrates. Alkaline phosphatase was present around the plasma membranes of osteoblasts and associated with extracellular matrix vesicles in new woven bone. This is consistent with the proposed role for this enzyme (Robison 1923) and for matrix vesicles (Bonucci 1967) in the mineralization of bone (Bernard and Marvaso 1981). Concentrations of specific secretory acid phosphatase reaction product in the cytoplasm of degenerating osteoblasts may contribute to the imbalance between bone formation and resorption. Osteoclasts, while few in number, showed non-specific and specific acid phosphatase activity. The Golgi apparatus and heterophagic lysosomes of mononuclear phagocytes were rich in non-specific acid phosphatase. This was also present in the Golgi lamellae and lysosomes of endothelial cells. Acid phosphatase cytochemistry suggests that mononuclear phagocytes, multinuclear osteoclasts and the vascular endothelium are involved in bone resorption in this disease.
Dickson
G R
GR
Department of Anatomy, Queen's University of Belfast, Northern Ireland.
Mollan
R A
RA
Carr
K E
KE
D000135:Acid Phosphatase / Q000032:analysis*; D000469:Alkaline Phosphatase / Q000032:analysis*; D001842:Bone and Bones / Q000201:enzymology / Q000648:ultrastructure; D002462:Cell Membrane / Q000201:enzymology; D006651:Histocytochemistry; D006801:Humans; D010014:Osteolysis / Q000201:enzymology*; D010015:Osteolysis, Essential / Q000201:enzymology* / Q000473:pathology
D000469:Alkaline Phosphatase; D000135:Acid Phosphatase