acid-phosphatase and Pheochromocytoma

Topics: 17-Hydroxycorticosteroids; 17-Ketosteroids; Acid Phosphatase; Adrenal Gland Neoplasms; Alkaline Phosphatase; Amino Acids; Amylases; Bone Neoplasms; Breast Neoplasms; Carcinoid Tumor; Catecholamines; Chorionic Gonadotropin; Clinical Enzyme Tests; Clinical Laboratory Techniques; Female; Glucose-6-Phosphate Isomerase; Humans; Hydroxyindoleacetic Acid; L-Lactate Dehydrogenase; Liver Neoplasms; Male; Neoplasms; Neoplasms, Nerve Tissue; Neuroblastoma; Nucleotidases; Pancreatic Neoplasms; Pheochromocytoma; Pregnancy; Prostatic Neoplasms; Trophoblastic Neoplasms; Vanilmandelic Acid

Treatment with neuronal growth factor (NGF) results in the growth of neuronal processes by PC12 cells and a concomitant 70% increase in the area of the Golgi apparatus. To define the observed morphologic changes in biochemical terms, we investigated the effect of NGF treatment on some Golgi and lysosomal enzyme activities of PC12 cells. Enzyme activities characteristic of the Golgi apparatus, lysosomes, plasma membranes, mitochondria, and endoplasmic reticulum were measured in cell homogenates, in post-mitochrondrial supernatants, and in Golgi-enriched fractions from control and from NGF-stimulated PC12 cells. Treatment of PC12 cells with NGF did not change the level of the Golgi activity of UDPGal:GlcNAc galactosyltransferase while that of CMP-sialic acid:lactosylceramide sialyltransferase was increased three- to fivefold in all fractions studied. For lysosomal enzymes, NGF treatment resulted in a two- to threefold higher level of arylsulfatase activity compared to either acid phosphatase or acid alpha-mannosidase activities. These results indicate that there is a selective increase of at least one Golgi and one lysosomal activity as a result of NGF stimulation of PC12 cells. Both of these enzymes are involved in glycolipid metabolism. It is possible that the dramatic morphologic changes observed during NGF-induced differentiation of PC12 cells are associated not only with increased synthesis in the Golgi apparatus of plasma membrane components such as gangliosides, but also with increased degradation in lysosomes of other plasma membrane components such as sulfatide.

Topics: Acid Phosphatase; Adrenal Gland Neoplasms; alpha-Mannosidase; Animals; Arylsulfatases; Golgi Apparatus; Histocytochemistry; Lysosomes; Mannosidases; Microscopy, Electron; N-Acetyllactosamine Synthase; Nerve Growth Factors; Pheochromocytoma; Rats; Sialyltransferases; Tumor Cells, Cultured

Although prostate-specific acid phosphatase (PASP) has been recognized as a specific marker of tissue of prostatic origin, several investigators have pointed out that some of the carcinoid tumours and islet cell tumours of the pancreas reacted immunohistochemically to PSAP. We investigated 50 cases immunohistochemically comprising 44 carcinoids of the G-I tract, 3 of the bronchus, 1 each of the ovary, kidney and middle ear. PSAP positive cases were, 30 in G-I tract, one each in ovary and kidney. Eighty percent of tumours of hindgut origin were positive. Apart from the immunohistochemical study, the content of PSAP in preoperative serum and tumour tissue was estimated in a case with a rectal carcinoid. Extremely elevated PSAP was confirmed in both the serum and tumour tissue. Neuroendocrine tumours such as pheochromocytoma, medullary thyroid carcinoma, and islet cell carcinoma were investigated as controls. No cells immunoreactive to PSAP were observed in these control cases. Prostate specific antigen was definitely negative in carcinoids. We would emphasize that PSAP may be an excellent marker of carcinoids especially when derived from hindgut.

Topics: Acid Phosphatase; Adenoma, Islet Cell; Carcinoid Tumor; Female; Gastrointestinal Neoplasms; Humans; Immunoenzyme Techniques; Male; Pheochromocytoma; Prostate; Radioimmunoassay; Rectal Neoplasms; Thyroid Neoplasms

Cells of the PC-12 rat pheochromocytoma cell line respond to nerve growth factor (NGF) by sprouting neurites and biochemically differentiating into sympathetic ganglion-like cells. NGF-stimulated ('differentiated') and unstimulated ('undifferentiated') cells were studied by cytochemical techniques for the localization of the enzymes acid phosphatase (ACPase) and thiamine pyrophosphatase (TPPase), and by a morphometric analysis of the distribution of endocytosed wheat-germ agglutinin labelled with horseradish peroxidase (WGA-HRP). Both cytochemical stains showed the enzymes to be distributed in lysosomes and certain cisternae of the Golgi apparatus in both NGF stimulated and unstimulated cells. ACPase was not confined to GERL (Golgi-endoplasmic reticulum-lysosome) as in certain other cells. The morphometric studies demonstrated that the reaction product of the internalized WGA-HRP occupied 4.7% of the cytoplasmic area in unstimulated cells and 4.5% in NGF-stimulated ones. Despite this similarity, the distribution of the WGA-HRP among the studied intracellular compartments in these two cell groups varied. In the NGF-stimulated cells 3.3% of the WGA-HRP reaction product was found in the innermost Golgi cisterna(e) while in unstimulated cells only 0.3% was seen in this compartment. Similarly, 4.3% of the WGA-HRP stain was found in small vesicles at the 'trans' aspect of the Golgi apparatus in stimulated cells, when only 0.3% of the stain occupied this compartment in 'undifferentiated' cells. The morphometric analysis also revealed that when the PC-12 cells were stimulated with NGF, the Golgi apparatus increased in area by approximately 70%. These findings are consistent with the hypothesis that NGF induced differentiation of PC-12 cells is coupled with enhanced endocytosis of WGA and probably of its 'receptor' to the innermost Golgi cisterna(e) and the closely associated vesicles.

Topics: Acid Phosphatase; Animals; Cell Line; Endocytosis; Golgi Apparatus; Histocytochemistry; Horseradish Peroxidase; Lectins; Nerve Growth Factors; Pheochromocytoma; Rats; Thiamine Pyrophosphatase; Wheat Germ Agglutinins

The endocytosis of [125I]nerve growth factor (NGF) by cultured rat pheochromocytoma cells, the PC12 line, was studied by ultrastructural quantitative autoradiography. Cells previously grown in the absence of NGF were incubated at 37 degrees C with [125I]NGF for periods of up to 26 h. Under these conditions, PC12 cells have not yet shown outgrowth of neurites. Heavy labeling of the plasma membrane was observed at 2 h. At 6 and 26 h, lower but significant levels of labeling of the plasma membrane were still noted. After 2, 6 and 26 h, endocytosis of [125I]NGF was detected. Low breakdown of [125I]NGF was observed only after 26 h. At 26 h, grain density distributions of [125I]NGF showed significant labeling of lysosomes, while nuclei and rough endoplasmic reticulum showed the lowest levels of labeling. Significant apparent labeling of vesicles of smooth endoplasmic reticulum and of various cytoplasmic components, including cytoskeletal elements, was also observed. These findings indicate that [125I]NGF undergoes endocytosis quite slowly. During the initial phase of the interaction between NGF and PC12 cells, plasma membrane moieties are constantly labeled while lysosomes show progressively increasing uptake of NGF. The pathway of endocytosis of [125I]NGF included vesicles of the smooth endoplasmic reticulum but the Golgi apparatus was not unequivocally labeled. The findings do not support the hypothesis that NGF is transported to the nucleus for the initiation of transcriptional events. Our morphologic observations are consistent with the hypothesis that NGF constantly occupies sites on or adjacent to the plasma membrane, and that it slowly undergoes endocytosis into lysosomes.

Topics: Acid Phosphatase; Adrenal Gland Neoplasms; Animals; Cell Line; Endocytosis; Kinetics; Mice; Microscopy, Electron; Neoplasms, Experimental; Nerve Growth Factors; Pheochromocytoma; Rats

Topics: Acid Phosphatase; Autopsy; Carcinoma; Chromaffin System; Diagnosis, Differential; Humans; Liver Neoplasms; Lung Neoplasms; Male; Middle Aged; Neoplasm Metastasis; Pheochromocytoma; Prostatic Neoplasms; Spinal Neoplasms; Urinary Bladder Neoplasms

Topics: Acid Phosphatase; Adenosine Triphosphate; Adrenal Gland Neoplasms; Adult; Carbonic Anhydrases; Catecholamines; Cytoplasmic Granules; Epinephrine; Humans; Lysophosphatidylcholines; Male; Norepinephrine; Pheochromocytoma