acid-phosphatase and Femoral-Neoplasms

Spectrometry has been employed to assess the levels of collagenase, catepsin D, trypsin-like proteinases and their inhibitors as well as bone acid and alkaline phosphatase both in the center and along the periphery of giant cell tumor of bone (GCTB) and chondrosarcoma. The levels of collagenase, trypsin-like proteinases and their inhibitors in the center of chondrosarcoma were much higher while those of alkaline phosphatase--lower than along tumor periphery. The catepsin D and acid phosphatase concentrations of the center and periphery of chondrosarcoma were similar. It was suggested that an extremely low concentration of trypsin-like inhibitors may contribute to degradation of the matrix in tissues adjacent to chondrosarcoma and, consequently, to tumor invasion development.

Topics: Acid Phosphatase; Alkaline Phosphatase; Bone Neoplasms; Cathepsin D; Chondrosarcoma; Collagenases; Femoral Neoplasms; Femur; Giant Cell Tumor of Bone; Humans; Ilium; Statistics, Nonparametric; Tibia; Trypsin; Trypsin Inhibitors

We have studied the effect of 3-amino-1-hydroxypropylidene-1,1-bisphosphonate (APD) on the morphology of rat bone and the metastatic behavior of Walker 256 (W256) cancer cells in the rat skeleton. Male Fischer rats (150-175 g) received s.c. injections for 7 days with APD (0.5 mg/kg body weight/day) (+ APD; n = 20) or with vehicle (-APD; n = 20). Subsequently, 10 + PD and 10 -APD rats received i.m. injections with W256 cells (+ W256), and the remaining rats received injections of vehicle (-W256). All rats were killed 14 days later. Trabecular bone volume was increased by 46 +/- 3% by APD treatment alone and was decreased by 56 +/- 7% (SEM) by W256 tumor burden alone. After 14 days of tumor burden, + APD/+ W256 rats had 3-fold more trabecular bone than did -APD/+W256 rats. Despite this bone-sparing effect, APD treatment of +W256 rats was associated with a 2.6-fold increase in skeletal tumor burden, while metastatic tumor burden in the liver, lungs, and kidneys was unaffected. The increased skeletal tumor burden in + APD/+ W256 rats was accompanied by an increase in the growth rate of W256 cells located in bone. Independent of APD treatment, W256 cells located adjacent to trabecular bone surfaces had greater growth rates than did W256 cells in the marrow, located > 50 microns from trabecular bone. In summary, the APD-induced increase in trabecular bone volume in rats is associated with a selective increase in skeletal tumor burden and an increased growth rate of W256 cells in the skeleton.

Topics: Acid Phosphatase; Animals; Bone and Bones; Bone Neoplasms; Carcinoma 256, Walker; Cell Division; Diphosphonates; Femoral Neoplasms; Male; Pamidronate; Pilot Projects; Rats; Rats, Inbred F344; Thymidine

In a proliferating giant cell tumor of bone the activities of tartrate-resistant acid phosphatase (acPase) and of NADH-tetrazolium reductase were demonstrated by enzyme histochemical methods. Quantitative microphotometry made it possible to determine the relative enzyme activities per given volume unit in the cytoplasm of giant cells of several sizes. The activity of tartrate-resistant acid phosphatase increases with increasing cell size, whereas the activity of tetrazolium reductase will decrease in proportion. This coincidence of high acPase activity and low tetrazolium reductase activity in larger giant cells is interpreted as an expression of degenerative change.

Topics: Acid Phosphatase; Adult; Bone Neoplasms; Cytoplasm; Female; Femoral Neoplasms; Giant Cell Tumors; Humans; NADH Tetrazolium Reductase; NADH, NADPH Oxidoreductases; Photometry

Topics: Acid Phosphatase; Adenocarcinoma; Adult; Bone Neoplasms; Diagnosis, Differential; Femoral Neoplasms; Gaucher Disease; Humans; Kidney Neoplasms; Male; Neoplasm Metastasis; Ribs

Three cases of giant cell tumor of bone were studied with the light and electron microscopes to determine the histochemical and cytochemical distribution of acid phosphatase isoenzymes. Using beta-glycerophosphate as a nonspecific substrate, acid phosphatase was found in the giant cells as well as the stromal cells. Ultrastructurally, using this substrate, the enzyme was found to be associated with lysosomes in the stromal cells and giant cells and also with the profuse system of tubules and vesicles in the cytoplasm of the giant cells. Using phosphorylcholine and D-ephedrinephosphate, which are substrates for a specific secretory isoenzyme of acid phosphatase, activity was found only in the vesicles of the giant cell cytoplasm. Lysosomes did not show activity with these substrates. Multinucleated cells of giant cell tumor contain a specific secretory type of acid phosphatase which is not present in the stromal cells. This suggests that the giant cells are attempting to form a secretory system similar to osteoclasts and that the vesicles in the cytoplasm which contain this acid phosphates are the morphologic expression of an abortive secretory system.

Topics: Acid Phosphatase; Adolescent; Aged; Bone Neoplasms; Cytoplasm; Dysgerminoma; Female; Femoral Neoplasms; Histocytochemistry; Humans; Humerus; Lysosomes; Metacarpus; Middle Aged; Osteoclasts

The fine structural localization of acid phosphatase in the different cells in a benign giant cell tumor of bone has been studied. Stromal cells type 1 and 2 (fibroblast-like and macrophage-like, respectively) showed the presence of lead phosphate precipitate following incubation in a Gomori-type lead salt medium only in conventional lysosomes. In the multinucleated giant cells, the final product was deposited over lysosome-like organelles, and also over Golgi cisternae, vesicles, and vacuoles. Furthermore, evidence for presence of acid phosphatase was obtained in smooth-surfaced tubular, sausage-, horse-shoe-, and ring-shaped structures and over digestive vacuoles of autophagic or heterophagic origin. Finally, in these cells, many of the tubular and vacuolar elements located subjacent to areas of the plasma membrane with microvillous specializations (abortive brush borders?) were shown to carry acid phosphatase.

Topics: Acid Phosphatase; Adult; Femoral Neoplasms; Giant Cell Tumors; Histocytochemistry; Humans; Male; Microscopy, Electron; Organoids

Topics: Acid Phosphatase; Adolescent; Adult; Alkaline Phosphatase; Bone Neoplasms; Child; Child, Preschool; Esterases; Female; Femoral Neoplasms; Fibroma; Fibrosarcoma; Fibrous Dysplasia of Bone; Glucuronidase; Humans; Humerus; Hydrolases; Infant, Newborn; Leucyl Aminopeptidase; Male; Mandibular Neoplasms; Middle Aged; Osteosarcoma; Tibia