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PubMed1976

IgM pyroglobulinemia with erythrocytosis presenting as hyperviscosity syndrome. I. Clinical features and viscometric studies.

The hyperviscosity syndrome is described in a patient with erythrocytosis and an immunoglobulin M with kappa light chain (IgMK) macroglobulinemia. Viscometric studies were carried out on whole blood and demonstrated the contribution of both the increased hematocrit value and the macroglobulinemia to the whole blood viscosity. Clinical improvement followed phlebotomy and was accompanied by a decrease in whole blood viscosity. Continued treatment with chlorambucil has been associated with a long symptom-free period. The macroglobulin was characterized as a monoclonal IgMK pyroglobulin which retained its thermoprecipitability was reduced to 7S monomers. The presence of IgMK aggregates in the serum may have contributed to the increase in blood viscosity.

Aged↗
PubMed1975

A new protein with a particular thermoprecipitability in bovine milk.

A new protein with a particular thermoprecipitability was isolated from bovine milk and tentatively termed milk pyroglobulin. The protein which was soluble at a relatively cold temperature was precipitated by raising the temperature to a certain degree depending on the concentration of the protein. The precipitate disappeared on recooling. This protein had the electrophoretic mobility of gamma globulin but did not carry either antigenic specificities of immunoglobulins or of free secretory component. The molecular weight was estimated to be approximately 60,000 in thin-layer gel filtration on Sephadex G-200 superfine gel, but the protein appeared to be convertible to molecules with a lower molecular weight of approximately 20,000 in the presence of bovine serum albumin. The presence of the albumin inhibited the thermoprecipitation as did alpha-lactalbumin but not IgG immunoglobulin from bovine colostrum. In SDS-polyacrylamide gel electrophoresis, the protein was separated into two components having a molecular weight of 19,000 and 10,000, respectively. Both components were thermoprecipitable and carried identical antigenic determinants.

Animals↗
PubMed2005

Afibrinogenemia and a circulating antibody against fibrinogen in a Bichon Frise dog.

A 1.5-year-old female Bichon Frise dog was evaluated for a life-threatening hemorrhagic condition that occurred after ovariohysterectomy, requiring 4 whole-blood transfusions. A hemostatic profile, including activated clotting time (ACT), one-stage prothrombin time (OSPT), activated partial thromboplastin time (APTT), buccal mucosal bleeding time, and specific assays (heat-precipitation microhematocrit method and electroimmunoassay) for fibrinogen, were performed to investigate the coagulopathy. Clotting times for all tests having a fibrin clot endpoint (ACT, OSPT, APTT) and buccal mucosal bleeding time were prolonged. Plasma fibrinogen was not detected by heat-precipitation microhematocrit method or electroimmunoassay. Using the Ellis-Stransky method, a mixture of patient plasma and normal canine plasma with known fibrinogen content yielded substantially less than the calculated fibrinogen concentration, indicating the presence of an interfering substance. The interferent properties of the patient's plasma were retained following heat precipitation at 56 degrees C indicating the absence of a pyroglobulin or an abnormal fibrinogen molecule. Radial immunodiffusion assay using the patient's plasma and activated thrombin confirmed the existence of an inhibitor to the formation of fibrin. Western blot analysis using the patient's plasma identified an IgG antibody that reacted with the Beta- and gamma- but not the Alpha-subunits of canine fibrinogen. Antibody was detected in samples taken 8, 16, and 68 days after the surgery; peak titers were evident at day 16. These results supported a diagnosis of afibrinogenemia with a circulating antibody inhibitor to fibrin clot formation that developed secondary to blood transfusion.

Afibrinogenemia↗
PubMed1976

Chemical and genetic characterization of a monoclonal IgA(lambda) protein with both cryo- and pyro-precipitability.

Studies of a monoclonal IgA (lambda) protein with both cryo- and pyro-precipitability show that it belongs to the IgA2 subclass and is positive for the A2m(2) allotypic marker. Like other cryoglobulins, this protein also has an unblocked light chain, and its heavy chain belongs to the VHI subgroup. The first 22 N-terminal amino acids of the lambda chain of this protein showed less than 65% homology with those of other human lambda chains but showed 86% identity with that of an amyloid fibril protein reported by others. The alpha chain of this protein appears to have more glutamic acid or glutamine, or both, and less isoleucine residues than other human alpha chains.

Amino Acid Sequence↗
PubMed1995

Human immunoglobulin M paraproteins cross-reactive with Neisseria meningitidis group B polysaccharide and fetal brain.

Three hundred fifty-nine serum samples from patients with immunoglobulin M (IgM) or IgG monoclonal gammopathies were tested for binding to the capsular polysaccharide (PS) of Neisseria meningitidis group B (MenB PS, poly-alpha[2-->8]-N-acetylneuraminic acid). Of 159 IgM paraproteins, 7 (4.4%) were positive, compared with 0 of 200 IgG paraproteins (P < 0.05). Since MenB PS reactivity was limited to the IgM paraproteins, the 159 IgM paraproteins were tested by enzyme-linked immunosorbent assay (ELISA) for reactivity with seven other bacterial PSs. None reacted with meningococcal A or C, Haemophilus influenzae type b, or Streptococcus pneumoniae type 3, 6, 14, or 23 PS. The specificity of the MenB PS-reactive antibodies was confirmed by demonstration of binding to N. meningitidis group B cells but not to a capsular PS-deficient mutant and by specific inhibition of binding to solid-phase MenB PS by soluble MenB PS in an ELISA. Five of five antibodies tested protected infant rats from bacteremia caused by Escherichia coli K1, an organism with a PS capsule that also is composed of poly-alpha[2-->8]-N-acetylneuraminic acid. Each of the seven MenB PS-reactive paraproteins had autoantibody activity as defined by binding to homogenates of calf brain in a radioimmunoassay. For six of the seven antibodies, binding to calf brain was inhibited by the addition of soluble MenB PS. Thus, approximately 4% of human IgM paraproteins have autoantibody activity to poly-alpha[2-->8]-N-acetylneuraminic acid, an antigen expressed in fetal brain and cross-reactive with the MenB capsular PS. The reason for this skewing of the IgM paraprotein repertoire toward reactivity with poly-alpha[2-->8]-N-acetylneuraminic acid antigenic determinants is unknown.

Animals↗
PubMed1978

3. The laboratory investigation of monoclonal gammopathies.

The monoclonal gammopathies are a group of disorders characterized by proliferation of a single clone of plasma cells that produce a homogeneous, monoclonal (M) protein. The structure of immunoglobulins, relationship of normal (polyclonal) immunoglobulins to myeloma and macroglobulin (monoclonal) immunoglobulins, pattern of monoclonal immunoglobulin overproduction, and laboratory methods for the recognition and study of monoclonal proteins in the serum and urine are reviewed. Interpretation of these laboratory tests is emphasized. The demonstration of a monoclonal protein in the serum or urine of a patient suggests multiple myeloma or one of its variants (solitary plasmacytoma of bone, extramedullary plasmacytoma, or plasma cell leukemia); Waldenström's macroglobulinemia or, occasionally, lymphoma; heavy-chain diseases (gamma, alpha, and mu); primary amyloidosis; and monoclonal gammopathies of undertermined significance. The electrophoretic and immunoelectrophoretic patterns found in the monoclonal gammopathies are discussed. Periodic electrophoresis of the serum and urine is essential in the follow-up and management of patients with a monoclonal gammopathy.

Amyloidosis↗