acid-phosphatase and Waldenstrom-Macroglobulinemia

In two cases of vacuolated plasma cells, one of which was associated with primary macroglobulinemia and the other was with kappa-chain Bence Jones multiple myeloma, we examined the immunopathological features of the vacuoles in order to know whether the Ig-secreting system or the lysosomal system is of importance in the process of vacuole formation. Immunofluorescent studies detected no Ig in the vacuoles. Detection of intracellular Ig by immunoelectron microscopic technique revealed that Ig was localized only in a small portion of the vacuoles but not in most vacuoles. Even when Ig was included in the vacuoles, only the contents of the vacuoles were positive for Ig but their demarcating membrane was negative for Ig. In contrast, electron microscopic studies of acid phosphatase activity revealed the presence of its activity in all vacuoles. These findings suggest that the lysosomal system but not the Ig-secreting system may play a major role in vacuolation of these myeloma cells.

Topics: Acid Phosphatase; Bence Jones Protein; Female; Fluorescent Antibody Technique; Histocytochemistry; Humans; Immunoglobulin kappa-Chains; Immunoglobulins; Male; Microscopy, Electron; Middle Aged; Multiple Myeloma; Plasma Cells; Vacuoles; Waldenstrom Macroglobulinemia

The differential diagnostic significance of acid phosphatase and beta-glucuronidase were studied in 77 cases of low-grade B cell non-Hodgkin's lymphomas. In most cases the results of cytochemical enzyme studies performed on malignant cells of the bone marrow were evaluated. B cell chronic lymphocytic leukaemia, centrocytic and centroblastic/centrocytic lymphomas were characterized by a weak or a negative acid phosphatase and beta-glucuronidase activity. Stronger positivity was observed in immunocytoma and in Waldenström's macroglobulinaemia, while the highest activity was found in multiple myeloma. Hairy cell leukaemia of B cell origin showed intensive tartrate-resistant acid phosphatase activity. The cytochemical examination of these lysosomal enzymes may be useful in the diagnosis of low-grade malignant lymphomas of B cell origin by completing other methods.

Topics: Acid Phosphatase; Adult; B-Lymphocytes; Bone Marrow; Glucuronidase; Humans; Leukemia, Hairy Cell; Leukemia, Lymphoid; Lymphoma; Lymphoma, Follicular; Lysosomes; Multiple Myeloma; Waldenstrom Macroglobulinemia

Topics: Acid Phosphatase; Bone Marrow; Diagnosis, Differential; Humans; Hypergammaglobulinemia; Multiple Myeloma; Naphthol AS D Esterase; Plasma Cells; Waldenstrom Macroglobulinemia

Acid phosphatase (AcP) in neoplastic cells from various lymphoid leukemias was examined. In the cytochemical studies, tartrate-resistant AcP (T-rAcP) activity was observed in the neoplastic cells from well-differentiated lymphoid leukemias such as adult T-cell leukemia (ATL), B-cell chronic lymphocytic leukemia (B-CLL), T-cell chronic lymphocytic leukemia (T-CLL), and hairy-cell leukemia (HCL). T-rAcP activity was also detected in a small number of leukemic cells obtained from T-cell acute lymphoblastic leukemia (T-ALL), while it was not detected in the neoplastic cells from null-ALL, macroglobulinemia, and multiple myeloma (MM). In the electrophoretical studies, fraction 1 (F-1), F-3, F-3b, and F-4 were completely tartrate-sensitive, while F-2 was partially resistant and F-5 was completely resistant. T-rAcP activity (F-5) was observed in ATL cells, B-CLL cells, and HCL cells, while it was not detected in ALL cells, macroglobulinemia cells, and MM cells. The present study indicates that T-rAcP activity is observed not only in HCL cells but also in the well-differentiated lymphoid cells such as ATL cells, B-CLL and T-CLL cells except the most highly differentiated forms of B-cells of MM and macroglobulinemia.

Topics: Acid Phosphatase; Cell Transformation, Neoplastic; Electrophoresis, Polyacrylamide Gel; Humans; Isoenzymes; Leukemia, Hairy Cell; Leukemia, Lymphoid; Multiple Myeloma; T-Lymphocytes; Tartrates; Waldenstrom Macroglobulinemia

Malignant lymphocytes from 30 B-cell chronic lymphocytic leukemia (B-CLL) patients were studied for the cytochemical localization of two acid hydrolases, alpha-naphthyl acetate esterase (ANAE) and acid phosphatase (AT). The large majority of the cells stained for both ANAE and AP in 7 cases, for AP only in 18 cases, and were negative for both the enzymes in 5 cases. Ultrastructural analysis revealed that the cells that displayed more mature morphological features, such as well developed smooth and rough membrane compartments, were those positive for acid hydrolases. That ANAE and AP are expressed by B cells at late stage of maturation was confirmed by the finding that some lymphocytes and all of the plasmacytoid lymphocytes and plasma cells from Walderström's macroglobulinemia, from mixed cryoglobulinemia, and from multiple myeloma patients stained strongly for both ANAE and AP. Using the expression of acid hydrolases and certain ultrastructural features as markers of cell differentiation, it was possible to demonstrate a process of maturation within the single B-CLL clones with accumulation of the cells at stages that differed in the various cases.

Topics: Acid Phosphatase; B-Lymphocytes; Cell Transformation, Neoplastic; Cryoglobulinemia; Cytoplasm; Humans; Hydrolases; Immunoglobulin G; Leukemia, Lymphoid; Naphthol AS D Esterase; Waldenstrom Macroglobulinemia

Topics: Acid Phosphatase; Adenosine Triphosphatases; Blood Protein Disorders; Esterases; Humans; Multiple Myeloma; Plasma Cells; Plasmacytoma; Waldenstrom Macroglobulinemia

Cytochemistry is disappointing in lymphoproliferative syndromes for it does not permit one to classify the various diseases with certainty. In the early stages, if the three indices are lowered, the prognosis seems poorer. A study of glucuronidase permits, in hyperlymphocytosis, one to differentiate benign from malignant lymphocytes, but does not permit one to differentiate from one another, the other chronic lymphoproliferative syndromes. The acid phosphatase is interesting in the study of hairy cell leukemia. Finally, it was not possible to distinguish chronic lymphoid leukemia from leukemia with lymphosarcomatous cells, nor from the cytochemical point of view nor using tests for delayed hypersensitivity.

Topics: Acid Phosphatase; Glucuronidase; Glycosaminoglycans; Humans; Leukemia; Leukemia, Lymphoid; Leukemia, Myeloid; Skin Tests; Waldenstrom Macroglobulinemia

Topics: Acid Phosphatase; Animals; Complement System Proteins; Flocculation Tests; Glucuronidase; Immunodiffusion; Immunoelectrophoresis; Immunoglobulin M; Lysosomes; Neutrophils; Phagocytosis; Rabbits; Rheumatoid Factor; Waldenstrom Macroglobulinemia

Topics: Acid Phosphatase; Animals; Animals, Newborn; Cat-Scratch Disease; Glucuronidase; Hexosaminidases; Humans; Infectious Mononucleosis; Leukemia, Lymphoid; Lymphocyte Activation; Lymphocytes; Muramidase; Rats; Waldenstrom Macroglobulinemia

Topics: Acid Phosphatase; Adenosine Triphosphatases; Bone Marrow; Esterases; Histocytochemistry; Humans; Multiple Myeloma; Plasma Cells; Waldenstrom Macroglobulinemia

Topics: Acid Phosphatase; Adenosine Triphosphatases; Aged; Alkaline Phosphatase; Autopsy; Blood Proteins; Bone Marrow Cells; Bone Marrow Examination; Diagnosis, Differential; Esterases; Histocytochemistry; Humans; Immunoelectrophoresis; Lymphocytes; Male; Microscopy, Electron; Mitochondria; Multiple Myeloma; Naphthaleneacetic Acids; Peroxidases; Plasma Cells; Ultracentrifugation; Waldenstrom Macroglobulinemia

Topics: Acid Phosphatase; Adolescent; Adult; Aged; Blood Proteins; Culture Techniques; Female; Glucuronidase; Hodgkin Disease; Humans; Infectious Mononucleosis; Lectins; Leukemia, Lymphoid; Lymphocyte Activation; Lymphocytes; Lymphoma, Follicular; Lysosomes; Malate Dehydrogenase; Male; Middle Aged; Plasmacytoma; Sarcoidosis; Waldenstrom Macroglobulinemia

Topics: Acid Phosphatase; Alkaline Phosphatase; Blood Proteins; Bone Marrow; Bone Marrow Cells; Female; Glucosephosphate Dehydrogenase; Glycoproteins; Histocytochemistry; Humans; L-Lactate Dehydrogenase; Male; Multiple Myeloma; Periodic Acid; Plasma Cells; Succinate Dehydrogenase; Waldenstrom Macroglobulinemia