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

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.
 ...
PMID:[Ectopic production of amylase by a non-producing type of multiple myeloma]. 169 5

Two stable lines of IgA lambda-producing plasma cells (KHM-1A and KHM-1B) that were free of the Epstein-Barr virus were established from a patient with multiple myeloma complicated by hyperamylasemia. Surface marker studies of the two cell lines showed that the cells had no surface immunoglobulins but were positive for cytoplasmic immunoglobulins (IgA lambda) and for HLA-DR and PCA-1. Secretion of IgA monoclonal immunoglobulin by the two lines was detected by a plaque-forming cell assay and by an enzyme-linked immunosorbent assay of culture media. KHM-1B cells also secreted alpha-amylase, but no such activity was detected in the culture-conditioned supernatant fluid of KHM-1A.
 ...
PMID:Establishment and characterization of an amylase-producing human myeloma cell line. 245 53

An alpha-amylase inhibitor (called the 0.53-inhibitor, Maeda, K., Takamori, Y. and Oka, O. (1982) Agric. Biol. Chem. 41, 2873-2875) and the carboxymethylated inhibitor were used to immunize mice (strain BALB/c) according to a procedure described earlier (McMaster, W.R. and Williams, A.F., (1979) Eur. J. Immunol. 9, 426-433). After fusion of spleen cells with NS-1 myeloma cells, three stable clones producing antibodies against the inhibitor were obtained. The binding characteristics of the monoclonal antibodies, AWAI-1, AWAI-2 and AWAI-3, to the inhibitor were analyzed by radioimmunoassay. Two of these monoclonal antibodies to the alpha-amylase inhibitor did not show any binding affinity towards carboxymethylated inhibitor, suggesting that the main antigenic determinant on the native inhibitor is tertiary-structure dependent. The monoclonal antibodies obtained cross-reacted with three other alpha-amylase inhibitors (the 0.19-, the 0.36- and the 0.38-inhibitor) in wheat and these were separated together with the 0.53-inhibitor from the rest of inhibitors by immunoaffinity chromatography. One stable clone producing antibody against the carboxymethylated inhibitor was also established, AWAI-4. The antigenic determinant to this antibody was found to be included in the region of Met(5)-Lys(25) on the carboxymethylated inhibitor.
 ...
PMID:Monoclonal antibodies against an alpha-amylase inhibitor from wheat kernel. 387 82

A mouse hybridoma cell line which produced an anti-human salivary alpha-amylase monoclonal antibody was obtained by fusion between mouse spleen cells immunized with human salivary alpha-amylase and mouse myeloma cells, followed by screening the hybridoma cells by enzyme-linked immunosorbent assay. The hybridoma cell line (27-4-1) secreted IgG. The monoclonal antibody produced by the hybridoma showed no inhibitory effect on the activity of human salivary alpha-amylase. The specificity and reactivity of this monoclonal antibody were examined by determining the activities of human salivary and pancreatic alpha-amylases bound to the monoclonal antibody immobilized on polystyrene balls or by enzyme immunoassay with the monoclonal antibody conjugated with beta-D-galactosidase. The results revealed that the monoclonal antibody produced by the hybridoma cell line was specific for salivary alpha-amylase and absolutely unreactive to pancreatic alpha-amylase.
 ...
PMID:Preparation of human salivary alpha-amylase specific monoclonal antibody. 387 9