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)

Supernatants of human peripheral mononuclear cells containing membrane components shed in consequence of 4--37 degrees temperature shift were used as source for isolation of Fc-receptors (FcR). Aggregated IgG1 myeloma protein and TMV-anti-TMV complexes proved suitable sorbents to adsorb quantitatively and specifically the FcR-s. The isolated FcR interacts only with IgG and not with IgM. No haemagglutination was observed when the isolated FcR was incubated with sensitized human Rh+ red blood cells. Complement dependent lysis of sheep red blood cells was not inhibited by the isolated FcR-s. The interaction between IgG and SpA from Staphylococcus aureus (Cowan I) bacteria was not inhibited when red blood cells sensitized with IgG were preincubated with the isolated FcR-s. The differences between the FcR-like material isolated from supernatants of peripheral human mononuclear cells and those secreted by stimulated T cells or produced by lymphoblastoid cell lines are discussed.
Immunology 1978 Sep
PMID:Isolation and characterization of Fc-receptors shed from human peripheral mononuclear cells. 70 Jul 82

The percentage of fat-cell areas in bone marrow particles from 22 patients with untreated myelomatosis was estimated. In only 1 patient was the mean fat cell area below 25% of the bone marrow area measured. A negative correlation was found between the area of fat cells and plasma cells, indicating a displacement of the fat cell area by the plasma cells. 28% of the patients had empty bone marrow deposits of iron. However, based on a normal iron saturation of S-transferrin and a normal sideroblast count in the bone marrow, the supply of iron to the erythropoiesis was considered sufficient. All patients but one had normoblastic bone marrows. Using a deoxyuridine suppression test in 10 patients, no biochemical defect could be demonstrated. To judge from the correlation coefficient a minor degree (9-14%) of the variation in Hb values could be predicted from the cellularity in the bone marrow while a major degree (70%) could be predicted from the renal glomerular filtration rate. The results do not support a displacement of blood-forming elements, iron deficiency, vitamin B12 or folic acid deficiency to be of general significance in the pathogenesis of anaemia, but agrees with a causal relationship between anaemia and renal failure.
Scand J Haematol 1978 Sep
PMID:Bone marrow studies in myelomatosis. 71 78

The digestion of human IgG1/K myeloma proteins with pepsin in the presence of 8 M-urea produces fragments that differ from those produced by aqueous peptic digestion, and from other characteristic immunoglobulin fragments. Fb'2, the larger urea/pepsin fragment, was previously shown to consist of the constant regions of the light chains, and the CH1 domains and hinge regions of the heavy chains. The smaller fragment, upFc, has now been characterized. After reduction, three peptides were released from fragment upFc. Amino acid sequencing, N- and C-terminal determinations and amino acid compositions have enabled these peptides to be identified as residues Ile-253 to Leu-306, residues Thr-307 to Asp-376 and residues Thr-411 to Gly-446 of the heavy chain. Fragment upFc therefore contains the entire Fc region, beginning at residue Ile-253, except for a 34-residue section from within the CH3-domain disulphide loop. Peptic digestion of IgG1/K proteins in 8M-urea therefore provides a method for isolating from gamma1 heavy chains five homogeneous peptides in good yield, which account for almost the entire constant region. Characterization of fragments Fb'2 and upFc has shown that the action of pepsin in urea is entirely different from that of aqueous pepsin. Two gamma1 heavy chains have been shown to differ in sequence at three positions from the sequence reported for protein Eu.
Biochem J 1976 Sep 01
PMID:Characterization of upFc, a fragment of human immunoglobulin G1 produced by pepsin in urea. 79 Dec 67

In 1966 a new immunoglobulin was found in persons with allergies and in non-typical myeloma proteins. Normally this immunoglobulin E is present only in nanogramms and rests with predilection on the membrane of mast-cells. There is a reaginic-anaphylactic reaction after re-exposure of antigens to the antigen-antibody reaction followed by denudation of mediators of the anaphylactic reaction. With the Radio-Immuno-Sorbent-Test (RIST) the IgE can be quantitatively determined. Elevated IgE-blood levels are typically found in atopic eczema. With the Radio-Allergo-Sorbent-Test (Rast) the allergen specific IgE can be defined. A conformity with appropriate patchtests can be achieved in 60-80% of the cases. In this review advantoses and problem of RIST- and RAST-diagnoses are described. RAST represents a valuable aid in diagnosis of allergies beeing not burdensome and risky, as it is easy to perform and bears no risk to the patients. At the present time, however, patch tests are necessary in the diagnosis of allergies.
Hautarzt 1976 Sep
PMID:[IgE and the significance of the radio-allergo-sorbent-test (RAST)]. 79

A human IgG1 myeloma protein that has a delection in the third constant domain of the heavy chain (Cgamma3) and forms two-chain half-molecules was studied for its in vivo turnover and its ability to fix C1q and hemolytic complement, to bind to human lymphocytes, neutrophils, and monocytes, and to induce a passive cutaneous reaction in guinea pigs. In both man and monkeys, the half-molecule was rapidly catabolized and in part excreted into the urine. The half-life in man was 4.3 days and the fractional turnover 165% per day; 7.6% of the intravascular pool was excreted into the urine per day. Although the 7S four-chain myeloma protein could not be obtained in a pure form, the elimination from the serum of a partially purified preparation suggested that it was also rapidly catabolized. The unaggregated half-molecule neither formed complexes with C1q, cound to human lymphocytes, neutrophils, and monocytes, nor elicited a reverse passive cutaneous reaction in guinea pigs. In contrast, the aggregated half-molecule fixed hemolytic complement and bound to the human white cells similarly to an intact IgG1 myeloma protein. In order to explain the biological activities of this half-moleculr, it is postulated that IgG1 may have several (at least two) submolecular sites for a given biological activity that are localized on both the Cgamma2 and Cgamma3 domains. Proteins having both sites would be capable of binding to C1q and Fc cell receptors in unaggregated in order to obtain half-molecule, must be aggregated in order to obtain this binding.
J Clin Invest 1975 Sep
PMID:Human myeloma IgG half-molecules. Catabolism and biological properties. 80 59

Small amounts of subtilisin (0.1 mg. per ml.) in the absence of cysteine will instantaneously hydrolyze "enzyme-sensitive" IgG globulins. This procedure permits the identification of antibodies in whole serum and myeloma globulins in the ultracentrifuge with simplicity and speed unmatched by other technics.
Am J Clin Pathol 1975 Sep
PMID:The hydrolysis of human IgG with subtilisin. 80 58

The cases of three patients who had clinical courses and hematologic data consistent with plasma-cell leukemia or a terminal leukemic phase of multiple myeloma are presented. A double Bence Jones protein was demonstrated in the urine of two of the patients. Immunoelectrophoresis and immunofluorescence studies demonstrated kappa light chains. In serum and urine of the third patient, no immunoglobulin abnormality was demonstrated. The three patients had rapidly fatal courses unresponsive to treatment.
Am J Clin Pathol 1975 Sep
PMID:Plasma-cell leukemia with unusual immunoglobulin abnormalities. 80 60

32P-labeled light chain messenger RNA was prepared from mouse MOPC 21 myeloma cells. The messenger RNA was hybridized to purified repetitive nuclear DNA and both the hybridized (repetitive 32P-RNA) and nonhybridized (nonrepetitive 32P-RNA) fractions were isolated. Only the nonhybridized RNA gave a T1 ribonuclease fingerprint showing oligonucleotides derived from the variable and constant regions of the light chain messenger RNA. In addition, this fingerprint showed oligonucleotides derived from the untranslated regions of the light chain messenger RNA. The nonrepetitive 32P-RNA was shown to rehybridize only with the unique fraction of total nuclear DNA. The rapidly hybridizing part of the unfractionated 32P-RNA preparation, therefore, is not a component of the light chain messenger RNA itself. Complementary DNA was prepared with reverse transcriptase using unlabeled light chain messenger RNA as template, and the transcripts were fractionated into various size classes. Complementary DNA molecules greater than 900 bases in length hybridized with both the initial messenger RNA and with the nonrepetitive 32P-RNA but failed to hybridize with excess purified repetitive 32P-RNA. The rapidly hybridizing component of the messenger RNA fraction, therefore, does not appear to be transcribed by reverse transcriptase. It is concluded that, under the experimental conditions used, the light chain messenger RNA hybridizes exclusively with unique DNA.
Cell 1975 Sep
PMID:Demonstration that a mouse immunoglobulin light chain messenger RNA hybridizes exclusively with unique DNA. 80 42

Sodium thiosulfate was used to enhance in vivo the polymerization of myeloma IgM, deficient in disulfide cross-links. The therapy sharply decreased the amount of low molecular weight IgM fractions, while increasing the serum content of molecules of higher molecular weight. The degree of disulfide cross-linking in IgM increased under the influence of thiosulfate. The rate of secretion into the serum and urine of some membrane-related glycopeptides and species rich in sialic acid was reduced. Also, the discharge of L chains to the urine was lowered during the thiosulfate trial. All these changes were attributed to enhancement of disulfide-interchanging enzyme activity by thiosulfate.
Clin Chim Acta 1975 Sep 01
PMID:The use of thiosulfate to increase polymerization of IgM subunits. 80 21

The complete covalent structure has been determined for a human myeloma IgA1 immunoglobulin. This protein has unique features in the amino acid sequence and disulfide bridge structure of the variable (V) and constant (C) regions of both the alpha heavy and the lambda light chains, and in the number and loci of oligosaccharides. Whereas C region domains of heavy chains have evolved independently over eons, recent isotypic variations have occured in lambda light chains and possibly in alpha heavy chains.
Science 1976 Sep 10
PMID:Complete covalent structure of a human IgA1 immunoglobulin. 82 Nov 46


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