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Results for “BENCE JONES PROTEIN”

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At least 19 recordsLinked to original sources
PubMed1963

The fate of injected Bence Jones protein.

Bence Jones protein injected into rabbits was excreted rapidly into the urine. The excreted protein retained the physicochemical and immunochemical properties of the injected Bence Jones protein. In spite of the rapid excretion, a significant portion of the injected Bence Jones protein was found to be metabolized. After reinjection of radioactive Bence Jones protein into the donor patient, only a little radioactivity was recovered in the urinary protein. The implications of these results are discussed.

Animals↗
PubMed1994

Amidase activity of human Bence Jones proteins.

Bence Jones proteins purified from urine of patients with multiple myeloma were found to be capable of hydrolyzing carbobenzoxy-L-valyl-glycyl-L-arginine p-nitroanilide (Chromozym TRY) and benzoyl-L-arginine p-nitroanilide (BApNA), synthetic chromogenic substrates for trypsin. The amidolytic activity obeyed classic Michaelis-Menten kinetics, exhibiting optimal activity around pH 8.4 and apparent Km of 140-730 microM and 18-27 microM for Chromozym TRY and BApNA, respectively. No activity was detected with intact IgG or Fab fragment, whereas the activity comparable to those of Bence Jones proteins was found with light chain derived from inactive IgG. Several lines of circumstantial evidence indicate that the observed activity was not due to contaminating enzyme.

Amidohydrolases↗
PubMed2001

Urinary beta2-microglobulin masquerading as a Bence Jones protein.

Bence Jones proteinuria, a common clinical manifestation of multiple myeloma, can also be seen in patients with other B-cell-derived neoplasms. Measurement of pretreatment levels is a useful adjunct in the diagnosis and staging of multiple myeloma, whereas serial levels reflect response to therapy. Serum concentrations of beta2-microglobulin, a small-molecular-weight protein associated with the major histocompatibility complex class I antigens, are often elevated in hematopoietic neoplasms and are also commonly measured at baseline, before treatment, and serially throughout therapy in patients with multiple myeloma and other lymphoproliferative disorders as a marker of tumor burden. Urinary concentrations, however, are considered an indicator of renal tubular function. High urinary levels are found in tubular proteinuria, a frequent sequela of long-standing multiple myeloma. A case is described in which a high urinary concentration of beta2-microglobulin interfered with Bence Jones protein quantification by electrophoresis studies.

Basic Helix-Loop-Helix Proteins↗
PubMed1962

Enzymatically produced subunits of proteins formed by plasma cells in mice. II. beta2a-Myeloma protein and Bence Jones protein.

The relationship of Bence Jones protein (mol wt = 45,000) to a beta(2A)-myeloma protein (mol wt = 160,000) formed by the same mouse plasma cell tumor (MPC-2) was investigated. The beta(2A)-myeloma protein was split by treatment with papain and cysteine into fragments (S(20,w) = 3.7S), similar in size to the Bence Jones protein (S(20,w) = 3.6S). Two types of fragments with distinct antigenic groupings designated S and F, were present in the MPC-2 myeloma protein digest. These were partially separated by DEAE-cellulose chromatography. The Bence Jones protein was found to share antigenic determinants with S fragments from the MPC-2 beta(2A)-myeloma protein and with S fragments from gamma-globulins. Physicochemical observations indicated, however, that the Bence Jones protein was not identical to the globulin fragments produced by treatment with papain and cysteine. Comparison of the S and F fragments from beta(2A)- and gamma-globulins revealed that the antigenic features shared by the various globulins derived from plasma cells (gamma- and beta(2A)-myeloma proteins, the range of normal gamma-globulins) are largely properties of the S fragments, whereas the distinctive antigenic differences between the gamma- and beta(2A)-myeloma proteins were properties which appeared in the F fragments of the molecules.

Animals↗
PubMed1976

Bence Jones proteins and light chains of immunoglobulins. XIII. Effect of elastase-like and chymotrypsin-like neutral proteases derived from human granulocytes on Bence Jones proteins.

Bence Jones proteins can be cleaved specifically by several types of endopeptidases into fragments corresponding to the amino-terminal, variant (VL) portion and to the carboxyl-terminal, constant (CL) portion of the light polypeptide chain. Two types of neutral proteases, designated elastase-like (ELP) and chymotrypsin-like (CLP), have been isolated and purified from human polymorphonuclear leukocytes. Because these proteases have defined proteolytic activity under physiologic conditions for several types of human proteins, we investigated their effect on human Bence Jones proteins. Incubation of kappa-type or lambda-type Bence Jones proteins with ELP or CLP under appropriate conditions resulted in cleavage of both types of light chains as evident by immunochemical and electrophoretic analyses. Treatment with ELP or CLP of one kappa Bence Jones protein resulted in the formation of a single component that had antigenic and electrophoretic properties similar to the VL fragment derived from pepsin digestion of the native protein. No component corresponding to the CL could be detected immunochemically or electrophoretically. Studies of isolated pepsin-labile (37 degrees C) and pepsin-stable (55 degrees C) CL fragments demonstrated the marked susceptibility of the carboxyl-terminal half of the light chain to proteolysis by the leukocyte-derived neutral proteases. Incubation with ELP of three other kappa Bence Jones proteins and three reduced-alkylated lambda Bence Jones proteins resulted, in each case, in the formation of a homogeneous component which was electrophoretically and immunochemically distinct from the pepsin-derived VL fragment. An identical component could also be formed by incubating a pepsin-derived VL fragment with ELP. In the ELP-treated samples, no CL-related material was detected electrophoretically or immunochemically with antisera possessing specificity for CL antigenic determinants present on the unfolded light polypeptide chain or on the isolated CL. The component formed by ELP or CLP treatment of certain Bence Jones proteins thus appears to be VL-related, but lacks the idiotypic antigenic determinant present on the native protein. In this respect, these neutral protease-derived light chain components are similar to the amyloid-like VL fragments generated in vitro from certain endopeptidase-treated Bence Jones proteins.

Bence Jones Protein↗
PubMed1966

Low-molecular-weight proteins related to Bence Jones proteins in multiple myeloma.

Urinary proteins distinct from Bence Jones proteins, but sharing antigenic determinants, were found in the urine of a number of patients with multiple myeloma. These components were smaller in size and antigenically deficient compared with Bence Jones proteins. They were best detected with antiserums to the homologous Bence Jones proteins and, in some cases, were related to the variable portion of the Bence Jones protein molecule.

Bence Jones Protein↗
PubMed1988

Differential nephrotoxicity of low molecular weight proteins including Bence Jones proteins in the perfused rat nephron in vivo.

To investigate the pathogenetic mechanisms of tubule nephrotoxicity of low molecular weight proteins (LMWP), proximal tubules (PT) of rats were perfused in vivo with artificial tubule fluid (ATF) containing one of five LMWPs: three human Bence Jones proteins (BJP), beta-lactoglobulin (BLG), and rabbit myoglobin (MYG). Volume (JV), chloride (JCl) and glucose (JG) fluxes in these perfused PTs were compared with those determined using ATF alone. In separate experiments, perfused nephrons were examined with electron and immunoelectron microscopy. After exposure to BJP1 or BLG, JV, JCl, and JG were less (P less than 0.05) than corresponding control fluxes. Cell damage of these perfused PTs, along with cellular debris in the distal tubules, was prominent. The PT lysosomes often appeared atypical and contained crystals. In contrast, perfusion with BJP2, BJP3, or MYG did not alter JV, JCl, or JG. These findings were corroborated by the normal ultrastructure of these PTs despite immunohistochemical evidence of endocytosis of the BJPs. Isoelectric point, molecular form, and isotype were not factors associated with PT damage. In addition, proteins with pI less than 7.4 precipitated in the distal nephron, forming acellular casts. Thus, certain nephrotoxic LMWPs damaged the PT, while others precipitated in the distal tubule, obstructing the nephron. These two pathogenetic mechanisms may independently be responsible for tubulointerstitial nephropathy of LMWPs in humans.

Animals↗
PubMed1980

An immunochemical study of two Bence-Jones proteins.

Two Bence-Jones proteins, one of kappa and the other of lambda type, from the urine of two myeloma patients were identified by protein electrophoresis (PEP) and immunoelectrophoresis (IEP). Urine specimens were concentrated and dialyzed with Ultrafiltration. The concentrated products were passed through a Sephadex G-100 column, and the fractions of Bence-Jones proteins were recycled in diethylaminoethyl (DEAE) ion exchange chromatography. Purified Bence-Jones proteins were mixed thoroughly with complete Freund adjuvant and inoculated into rabbits. The monospecific antisera to kappa and lambda chains were obtained by absorption with Bence-Jones proteins of the opposite types.

Adult↗
PubMed1978

Bence Jones proteins and light chains of immunoglobulins. XV. Effect of corticosteroids on synthesis and excretion of Bence Jones protein.

The effect of corticosteroids and cytotoxic chemotherapeutic agents on the excretion of Bence Jones protein was determined for periods of 1 - 62 mo in 29 patients with multiple myeloma and Bence Jones proteinuria. The amount of protein present in 24-h urine specimens collected before treatment and at frequent intervals during monthly treatment cycles was determined. Striking variations occurred in the amount of Bence Jones protein excretion; these changes were especially evident when 75 mg of prednisone were given daily for 7 days as part of a monthly chemotherapeutic regimen. Within the 7-day period seven patients showed essentially no decrease (<25%), whereas 13 and 9 patients had a moderate decrease (25-75%) or a marked decrease (>75%), respectively, in Bence Jones proteinuria as compared to pre-treatment values. The decrease in excretion of Bence Jones protein during this period was attributed mainly to corticosteroid therapy because of the transient nature of the response in most patients and the lack of such response in three patients when the hormone was omitted. Biosynthetic studies were performed to determine in vitro the effect of corticosteroids on Bence Jones protein synthesis. Plasma cells obtained from the bone marrow of 13 patients were incubated in a growth medium containing (14)C-labeled lysine and isoleucine and prednisone in concentrations up to 240 mug/ml, and the amount of Bence Jones protein synthesized was determined immunochemically. No differences in viability were apparent between untreated and prednisone-treated cells. The type of response exhibited by an individual patient in the percent decrease of Bence Jones protein excreted after 7 days of prednisone treatment was comparable to the percent decrease in newly-synthesized Bence Jones protein secreted by tumor cells when cultured in the presence of prednisone at a concentration of 120 mug/ml. The marked differences in the capacity of corticosteroids to affect Bence Jones protein synthesis appear to reflect a biochemical heterogeneity among plasma cell neoplasms.

Adult↗
PubMed1966

A study of immunoglobulin structure. II. The comparison of Bence Jones proteins by peptide mapping.

Urinary proteins of patients with myeloma, prepared by precipitation with ammonium sulphate, have been separated by gel filtration on Sephadex G-100 after reduction and aminoethylation. Many specimens separated into a major peak of Bence Jones protein and into minor peaks of albumin, a protein tentatively identified with heavy chain and a smaller molecular weight protein corresponding to the variable portion of the corresponding Bence Jones protein. The Bence Jones protein purified by gel filtration was analyzed by electrophoresis and by peptide mapping after tryptic digestion. The peptide maps of 24 type K and 20 type L Bence Jones proteins were compared. A set of common peptides was identified in the peptide maps of the Bence Jones proteins of the same type; the common peptides of type K proteins were completely different from the common peptides of type L proteins. The patterns of distinctive peptides was compared; no similarities were found between distinctive peptides of type K and of type L proteins. Some similarities were observed in the distinctive peptides of proteins of the same type. The similarities involved in many cases peptides containing cysteine, whereas similarities in other peptides were limited. This observation suggested that the amino acid sequence around the cysteines of the variable NH(2)-terminal half of the Bence Jones proteins may show less variability than other sequences. A few proteins of the same type differed in all their distinctive peptides, an indication that multiple amino acid differences exist between individual Bence Jones proteins. The genetic mechanisms responsible for the variability in the amino acid sequence of the NH(2)-terminal half of the light chains of immunoglobulins are discussed in view of the results of the comparison by peptide mapping of the Bence Jones proteins.

Amino Acid Sequence↗
PubMed1998

DNA-hydrolyzing activity of Bence Jones proteins.

Of 18 monoclonal Bence Jones proteins purified from urine of patients with multiple myeloma, 4 were found to have a DNA-nicking activity. In contrast, all Bence Jones proteins tested showed detectable amidase activity against carbobenzoxy-L-valyl-glycyl-L-arginine p-nitroanilide. No correlation between the two activities was found. Four patients excreting Bence Jones protein with the DNA-nicking activity showed somewhat severe symptoms, suggesting that this activity may be related to the progressive deterioration of clinical status.

Adult↗