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)

Bone marrow natural killer (NK) cell activity was studied in patients with multiple myeloma. Bone marrow mononuclear cells from myeloma patients expressed considerable levels of cytotoxicity against K562 in a 4 h 51Cr-release assay, which was comparable to that of blood lymphocytes. In contrast, NK-cell activity was markedly low or absent in bone marrow of normal donors and control patients. Fractionation of bone marrow cells from myeloma patients on linear bovine serum albumin gradients enriched NK effector cells in the upper, lymphocyte-enriched fraction, with no reactivity in the middle fraction containing mainly myeloma cells. Treatment with either Leu-7 or OKMI monoclonal antibody plus complement reduced or abrogated bone marrow NK-cell activity of myeloma patients as well as blood NK-cell activity. However, OKMI plus complement failed to reduce control bone marrow NK-cell activity, although the activity was reduced by Leu-7 plus complement. Overnight exposure to interferon (IFN) of bone marrow cells resulted in an augmentation of NK-cell activity in myeloma patients, but not in controls. Furthermore, adherent bone marrow cells from controls suppressed IFN-induced enhancement of NK-cell activity of blood lymphocytes, whereas bone marrow of myeloma patients did not contain such suppressor cells. No cytotoxicity was induced in control bone marrow cells by cocultivation with bone marrow myeloma cells. Bone marrow NK cells from myeloma patients were able to lyse control bone marrow cells in a 18 h assay and their lytic activity was augmented by IFN treatment. However, neither bone marrow cells nor blood lymphocytes were cytotoxic to autologous and allogeneic fresh myeloma cells even after activation with IFN. These results suggest that NK precursor cells differentiate into HNK-I- and OKMI-positive mature NK cells in bone marrow of myeloma patients, but not in control bone marrow, and that these functional bone marrow NK cells may interact with other bone marrow elements.
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PMID:Strong natural killer (NK) cell activity in bone marrow of myeloma patients: accelerated maturation of bone marrow NK cells and their interaction with other bone marrow cells. 659 56

A protected tridecapeptide, representing a new peptide corresponding to residues 56-68 of the VH domain in the mouse M603 myeloma protein, has been prepared by solid phase peptide synthesis. The protected tridecapeptide was prepared using the photolabile 4-bromomethyl-(3-nitro)-benzamidomethyl-resin and the multidetachable 2-[4-bromomethyl)phenylacetoxy]propionyl-resin as solid supports. The synthetic protocol and protecting groups were the same for both syntheses. The protected tridecapeptide was removed photolytically from both supports and the sequence integrity was determined by preview analysis using the solid phase Edman degradation procedure. The protected tridecapeptide-OMPA was purified to homogeneity by DMF/H2O precipitation and LH-60 chromatography. The purity of the protected peptide was further demonstrated by high pressure liquid chromatography on the free peptide after HF deprotection. The protected tridecapeptide was reattached to 4-bromomethyl-(3-nitro)-benzamidomethyl-resin to give the photolabile Boc-(protected)peptidyl-4-oxymethyl-(3-nitro)benzamidomethyl-resin in 25% yield. The protected tridecapeptide-oxymethylphenylacetic acid derivative was reattached to aminomethyl-resin to give Boc-(protected)peptidyl-2-[4-oxymethyl)phenyl]acetamidomethyl-resin in 45% yield and to 2-bromopropionyl-resin generating the multidetachable Boc-(protected)peptidyl-2-[(4-oxymethyl)phenylacetoxy] propionyl-resin in 80% yield. The reactivity of these reattached peptides was demonstrated by the quantitative coupling of Boc-leucine to the protected peptide-resin. The advantages and disadvantages of the different resins with respect to solid phase fragment synthesis are discussed.
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PMID:Synthesis of the protected tridecapeptide (56-68) of the VH domain of mouse myeloma immunoglobulin M603 and its reattachment to resin supports. 661 64

A panel of monoclonal antibodies that identify various antigens present on T and B cells was used to characterize circulating blood lymphocyte subsets in multiple myeloma [(MM)--13 patients] and benign monoclonal gammopathy [(BMG)--5 patients]. In MM and BMG an increase in B cell proportions (BA 1 positive cells) was observed, whereas T cells (Lyt 3 positive cells) were reduced compared to normal controls. However, with respect to the T cell subset distribution, a marked diversity between MM and BMG was noted. This may help to differentiate BMG from MM. In MM a relative decrease in inducer/helper T cells (OKT 4 positive cells) and increase in suppressor/cytotoxic T cells (OKT 8 positive cells) as well as in NK/K T cells (Leu 7 positive cells) was observed. On the other hand, in BMG the relative T cell subset distribution was comparable to those seen in normal subjects.
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PMID:Lymphocyte subsets in the peripheral blood of patients with multiple myeloma and benign monoclonal gammopathy. 663 24

Serum and ascites fluid from mice bearing 260 different myeloma tumors were screened serologically for myeloma proteins having light chains like that of L315, the lambda 2 chain produced by myeloma MOPC-315. Four proteins, made by myelomas TEPC-952, CBPC-49, ABPC-72, and SAPC-15, were identified. Their light chains were essentially indistinguishable serologically from L315, and each of them also yielded the characteristic C-terminal amino acid (leucine) and C-terminal tryptic peptide of L315. However, amino acid sequences and other findings reported elsewhere have revealed that although the light chain of TEPC-952 is indeed a lambda 2 chain, the light chains of the others (CBPC-49, ABPC-72, and SAPC-15) represent another, slightly different type of light chain, which has been designated lambda 3.
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PMID:Mouse myeloma proteins with lambda 2 and lambda 3 light chains. 679 67

Hybrids between human spleen cells and the non-secretor NSO mouse myeloma, and also between the rat non-secretor line YB2/O and human peripheral blood cells were prepared. After a month in culture very few hybrids retained the ability to secrete the human kappa light chain. From these, clones could be derived which remained stable over several months of continuous culture. On incorporating [3H]-Leu into the culture medium the cells secrete large amounts of radioactive light chain. It is shown that, even without dialysis, the purity of the preparation is sufficient for an automatic N-terminal sequence analysis at the radioactive level. From the pattern of distribution of leucine in the first twenty-two amino acid residues, it is possible to assign the synthesized light chains to one of the four established human subgroups. The method permits a fast and simple classification of human light chains secreted by hybrid myelomas. Although tested with rodent x human hybrids, we see no reason why the method could not equally apply to human x human hybrids.
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PMID:Chemical typing of human kappa light chain subgroups expressed by human hybrid myelomas. 679 91

A protected tridecapeptide of the sequence Boc-Lys(2CIZ)-Arg(Tos)-Leu-Glu (OcHex)-Trp(For)-Ile-Ala-Ala-Ser(Bzl)-Arg(Tos)-Asn-Lys(2CIZ)-Gly-OH, representing residues 43-55 of the variable region of the heavy chain of mouse myeloma protein M603, was synthesized. It was assembled by a stepwise solid phase method designed to give a fully protected peptide in high yield and purity with minimal side reactions. Thus, the peptide chain was attached as an alpha-methyl phenacyl ester to a 2-bromopropionyl-resin. After the synthesis the protected peptide fragment was obtained in 89% yield by photolytic cleavage from the resin. The peptide was purified by multiple precipitation and column chromatography. It was shown to be homogeneous by reverse phase high pressure liquid chromatography, and it had the correct amino acid composition and sequence. In the course of this work it was shown that tert.-butyloxycarbonyl-amino acids caused the formation of significant amounts of pyrrolidone carboxylic acid residues during the coupling reaction when a gamma-benzyl glutamyl residue was NH2-terminal. Other weak-acid additives also caused this chain terminating side reaction. The cyclization was markedly suppressed by protection of the glutamyl side chain as a cyclohexyl ester. With this protecting group, no evidence of pyrrolidone carboxylic acid formation could be detected in the tridecapeptide 43-55.
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PMID:Solid phase synthesis of the protected 43-55 tridecapeptide of the heavy chain of myeloma immunoglobin M603, employing cyclohexyl ester protection for glutamic acid. 681 68

Monoclonal antibodies to leucine enkephalin have been produced after fusion of mouse myeloma cells with spleen cells from hyper-immune mice. Hybrid clones 2D1 and SL1 were characterised using radioimmunoassay and an enzyme-linked immunosorbent assay. The antibody 2D1 was of low affinity and showed a maximum sensitivity of 0.1ng. The antibody binds equally well to the sulphated leucine enkephalin and to methionine enkephalin. It does not cross-react with dynorphin, methionine enkephalin-arg-phe or oxidised methionine enkephalin. The hybrid clone SL1 appears to be specific for leucine enkephalin. Preliminary immunocytochemical studies have shown that both antibodies bind specifically to leucine enkephalin in defined areas of the central nervous system.
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PMID:Monoclonal antibodies to leucine enkephalin. 687 Aug 87

The proteinase from culture supernatants of Candida albicans strain CBS-2730 was purified virtually to homogeneity by ion-exchange chromatography and affinity chromatography. The enzyme consists of a single polypeptide chain with tryptophan at the N- and leucine at the C-terminus. Its molecular weight is approx. 45,000 and the isoelectric point is at pH 4.4. With albumin as a substrate an apparent Km was determined to be 7 . 10(-5) M. The enzyme is inhibited by pepstatin at equimolar ratio and thus is a carboxyl proteinase (EC 3.4.23.6). Other group-specific inhibitors, though, did not efficiently block the enzyme. Above pH 8.4 the enzyme undergoes alkaline denaturation which is accompanied by dimerization. The enzyme is a glycoprotein. It is stable in presence of non-ionic detergents and can be freeze-dried. The enzyme clots milk at pH 5.5 and has trypsinogen kinase activity. Among several purified proteins that have been tested as a substrate, only horse ferritin was resistant to proteolysis, while myeloma proteins of the A1- and A2-type were readily cleaved, as were two proteinase inhibitors of human serum. Antibodies against purified enzyme did not react with several commercial Candida antigen preparations; antibodies against the enzyme, though, have been detected repeatedly in sera from patients with manifest candidiasis.
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PMID:Properties of a purified proteinase from the yeast Candida albicans. 701 86

Different clones of mouse hybridomas, derived from the fusion of unstimulated mouse peritoneal cells with mouse myeloma cells, producing IgM monoclonal antibodies directed against the membrane of bromelain-treated mouse erythrocytes (MRBC(Br)) have been previously established. We have recently shown that one of these hybridomas produce, in ascites, antibodies cross-reacting with phosphorylcholine derivatives (trimethylammonium (TMA) derivatives). In this work the cross-reactivity for TMA derivatives of the monoclonal antibodies produced by 4 anti-MRBC(Br) hybridomas have been studied at the cell level (plaque-forming cells). Phosphorylcholine, choline bromide and p-aminophenyl-trimethylammonium were found to be potent specific inhibitors of plaque formation (anti MRBC(Br)). The hemolytic activities of ascites and tissue culture supernatants were studied and their inhibition by TMA derivatives was determined. Immunoglobulins from ascites purified on TMA immunoadsorbent column were analyzed by two-dimensional gel electrophoresis, their spectrotype was compared to the spectrotype of immunoglobulins from tissue culture supernatants from the same hybridoma radioactively tagged by internal incorporation of [14C]leucine. It could be shown without ambiguity that the PTMA column retained an IgM with the same characteristics as the IgM secreted in vitro.
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PMID:Relationship between choline derivatives and mouse erythrocyte membrane antigens revealed by mouse monoclonal antibodies. I. Anticholine activity of anti-mouse erythrocyte monoclonal antibodies. 715 55

Sesquiterpene lactones, produced in light and capable of inhibiting auxin-induced elongation growth of coleoptile and hypocotyl segments, were isolated from young leaves of Helianthus annuus (Spring and Hager, Planta in press, 1982). These compounds have an antibiotic effect on gram-negative and gram-positive bacteria as well as on some fungi. The minimal inhibiting concentration (MIC) of compound II (15-hydroxy-3-dehydrodesoxyfruticin, Fig. 1), for example, is 15 micrograms/ml for Bacillus brevis, and 95 micrograms/ml for the fungus Eremothecium ashbyi. In addition, cytotoxic effects on mouse myeloma cells (NS-1) were also shown. Compound II causes a 50% inhibition of cell proliferation (ED50) at a concentration of 170 nM, compound I (niveusin C, Fig. 1) at 220 nM. The LD50-values were 0.15 micrograms II/ml and 1.24 micrograms I/ml, respectively. By measuring 14C-labelled thymidine, uridine and leucine incorporation into murine cells of the ascitic form of Ehrlich carcinoma (EAC) it could be shown that compounds I and II inhibit DNA and RNA synthesis, but do not affect the translation processes involved in protein synthesis. Furthermore, it could be shown that the exocyclic methylene group in the molecules of I and II plays an important role in triggering the described inhibitory effects.
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PMID:Biological activities of sesquiterpene lactones from Helianthus annuus: antimicrobial and cytotoxic properties; influence on DNA, RNA, and protein synthesis. 718 30


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