Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Sera, purified myeloma proteins, and urinary proteins obtained from eight patients with igA multiple myeloma were studied by physical-chemical and immunochemical methods. In six patients whose serum viscosity was increased, the sedimentation constants of the principal component of myeloma proteins ranged from 9.1 to 10.2 S. In two patients with nearly normal serum viscosity, the sedimentation constants of these proteins were 6.2 and 7.2 S. IGA-albumin complexes were detected in most of the sera, but invarying amounts; no complexes of ig with amylase, secretory component, or alpha(1)-antitrypsin were observed. Studies on isolated myeloma proteins revealed that all igA proteisn from sera with increased viscosity represented true polymers, linked by disulfide bonds, rather than noncovalently associated aggregates; J chain was detecable by both alkaline-urea disc electrophoresis and immunoelectrophoresis with a monospecific anti-J chain serum. Increased serum viscosity was not related to the igA subclass, L chain type, or the carbohydrate compositions of individual igA myeloma proteins. The urine of five patients contained free light chains corresponding in type to the light chain of the particular igA myeloma protein. However, free J chain was not detected. The immunoelectrophoretic analysis for the presence of J chain in sera of myeloma patients may be used for early and simple detection of polymeric forms of myeloma proteins.
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PMID:Properties of IgA myeloma proteins isolated rom sera of patients with the hyperviscosity syndrome. 40 74

We describe the case of a 63-year-old woman with an IgD-type multiple myeloma and hyperamylasaemia. The evolution of the amylase concentration, the immunohistochemical data and the intracellular amylase contents of the plasma cell were consistent with secretion of amylase by the malignant clone. Moreover, cytogenetic analysis of the bone marrow revealed two structural rearrangements involving chromosome 1 near the amylase locus. Multiple myeloma should be added to the amylase-secreting tumours. This rare entity is not confined to Japan, where it was first recognized.
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PMID:Amylase-producing IgD-type multiple myeloma. 128 Jun 72

The patient was a 64-year-old woman who was admitted to our hospital because of lumbago. A diagnosis of multiple myeloma (non-producing type) was made, based on (1) the presence of multiple osteolytic lesions, (2) hypercellular marrow with 64.2% plasmacytoid malignant cells, (3) no monoclonal gamma-globulin was detected in the serum and urine, and (4) abnormal monoclonal gamma-globulin was also not detected in the cytoplasm and membranes of these malignant cells. After several courses of chemotherapy, a pleural effusion infiltrated by myeloma cells developed and the patient's serum contained a markedly increased amylase activity of salivary-type. Amylase activity was also detected in vitro in the supernatant of cultured myeloma cells established from the patient's pleural effusion. The presence of alpha-amylase in the myeloma cells, which were derived from pleural effusion, was demonstrated immuno-histochemically. These observations indicates that amylase was ectopically produced by these myeloma cells. Interestingly, 14 out of 20 metaphases in the cells derived from pleural effusion showed translocation of 1p22 near the region of 1p21, where the amylase gene was assigned.
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PMID:[Ectopic production of amylase by a non-producing type of multiple myeloma]. 169 5

Two amylase-producing cell lines have been established, KMK-2 from a patient with gastric cancer, and KHM-1B from a patient with IgA lambda-type multiple myeloma. Both patients exhibited extremely high levels of serum amylase. The production of S-type amylase m-RNA by KMK-2 and KHM-1B was demonstrated by Northern blot analysis. Chromosome analysis showed many qualitative and quantitative abnormalities in both cell lines. In KHM-1B, a translocation was found between 1p13 or 21, near the amylase genes locus, and 9q34, the abl oncogene locus. These findings suggest the amylase gene in KHM-1B to be activated by translocation. A rearranged amylase gene was demonstrated by Southern blot analysis with only one enzyme, Accl.
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PMID:Genetic analysis of amylase-producing cell lines: ectopic activation of the amylase gene by translocation. 170 4

We report a case of ectopic salivary amylase-producing IgA- lambda-type multiple myeloma. A 70-year-old man was admitted because of anemia and renal failure. After chemotherapy for eight months, the serum amylase markedly increased. Amylase activity in the supernatant of cultured myeloma cells, which were obtained from the bone marrow, also increased. The myeloma cells expressed MDR-1/P-glycoprotein). The case implies the association of drug resistance and the ectopic amylase production in a case of multiple myeloma.
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PMID:[Ectopic salivary amylase-producing IgA- lambda-type multiple myeloma with expression of MDR-1/P-glycoprotein]. 171 26

We managed a case of amylase-producing multiple myeloma with extensive extramedullary spread. We reviewed five cases of amylase-producing multiple myeloma, including this case. This type of multiple myeloma has shown unique clinicopathologic features. (1) A distinct elevation of the serum amylase activity was demonstrated in all five patients. The amylase isozyme was of the S type without exception. (2) Extensive extramedullary spread with extramedullary tumors and/or myelomatous pleural effusions or ascites was seen in all five patients during the course of illness. (3) In three of four cases in which it was mentioned, extensive destruction of multiple bones was demonstrated roentgenographically. (4) In four patients, excepting one with a solitary bone lesion, the survival from the initial therapy was shorter than 1 year. (5) Myeloma cell lines were established in three cases. A common feature of these three cell lines was a translocation of chromosome 1, which supplied the amylase gene. This finding may be pathogenetically related to this entity.
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PMID:Amylase-producing multiple myeloma. 171 41

Isoamylases, with an abnormal anodic migration, were detected by an electrophoretic technique in the sera from two patients with immunoglobulin A-type myeloma. The abnormal isoamylase bands migrate towards the anode faster than the salivary isoamylase (S2) band and were stained more strongly than the S2 sub-band. The abnormal isoamylase could be separated from patients' sera by using size-exclusion high-performance liquid chromatography. The serum abnormal isoamylases were showed to be sialic acid residues containing amylase, after the study of treatment with neuraminidase (EC 3.2.1.18), and to be salivary-type amylase, after the study of reaction with human salivary monoclonal antibody. The abnormal bands were not detected in the saliva from one patient. The two patients had no detectable malignancies except myeloma. These findings strongly suggest that the sialic acid-containing salivary-type amylases were produced ectopically from myeloma cells. In this regard the ectopic amylase production by myeloma cells is discussed.
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PMID:Separation and characterization of sialic acid-containing salivary-type amylase from patients' sera with immunoglobulin A-type myeloma. 172 78

A patient with IgA-lambda-type multiple myeloma who appeared to be secreting salivary-type amylase ectopically is reported. Both the patient's serum and urine contained high levels of amylase. Amylase activity in the supernatant of cultured myeloma cells, obtained from the patient's pleural effusion while he had malignant pleuritis, increased almost linearly from the time of cell seeding. The presence of IgA and S-type amylase in the myeloma cells was demonstrated cytochemically and by immunoelectron microscopy. These observations showed that amylase was produced by these human myeloma cells.
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PMID:Ectopic production of salivary-type amylase by a IgA-lambda-type multiple myeloma. 245 22

The first autopsy case of amylase-producing IgA-lambda-type multiple myeloma is described. Immunohistochemically, amylase and alpha and lambda chains of immunoglobulin were demonstrated in the cytoplasm of the myeloma cells. Secretion of amylase by cultured myeloma cells obtained from the patient's pleural effusion was clearly demonstrated by the starch film method. Immunoelectron microscopically, positive reaction products for amylase and the alpha chain of immunoglobulin were observed in the well developed endoplasmic reticulum. Since no secretory granules were observed, we postulated that the secretory process of amylase was not via the zymogen granules but via a mechanism similar to that for immunoglobulin.
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PMID:Amylase-producing multiple myeloma. Cytochemical, immunohistochemical and immunoelectron microscopic studies. 247 86

Two human myeloma cell lines, KMS-12-PE and KMS-12-BM, were established from a 64-year-old woman with a non-producing type of multiple myeloma. The KMS-12-PE line originated from the pleural effusion and the KMS-12-BM from the bone marrow. These two lines showed the same chromosome marker, t(11:14)(q13:q32). However, their phenotypes of surface markers differed from each other. KMS-12-BM cells were positive to CD20, CD38 and PCA-1. showing the plasmacytoid (immature plasma cell) stage of B-cell differentiation, while KMS-12-PE cells were positive to CD38 and PCA-1, but not to CD20, indicating the terminal differentiated stage of B-cells. As seen in the pleural effusion of the patient. KMS-12-PE cells ectopically produced a salivary type of amylase, but KMS-12-BM cells did not. Interestingly, the chromosome abnormality of del(1)(p22----pter) near the region of 1p21, where the amylase gene was assigned, was noticed in as many as 76% of KMS-12-PE cells.
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PMID:Two human myeloma cell lines, amylase-producing KMS-12-PE and amylase-non-producing KMS-12-BM, were established from a patient, having the same chromosome marker, t(11;14)(q13;q32). 247 9


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