[Identification of anti-centromere antibody and its clinical evaluation].
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Biomedical subjects
Publications and source records attributed to M Kameko.
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This study was undertaken, employing the immunoenzyme method, to confirm the presence of retinol-binding protein in human pancreatic islets, and to compare its distribution with that of prealbumin, insulin, glucagon, somatostatin and pancreatic polypeptide. It was found that most islet cells contained retinol-binding protein, although centrally located cells showed stronger reactivity than those in the peripheral region. The distribution of each of the five polypeptides differed from that of retinol-binding protein, indicating that these peptides did not cross-react with anti-retinol-binding protein antibody. Islet cells which contained prealbumin, on the other hand, were mostly classified as A cells. Further studies are necessary to confirm whether the islet cells produce retinol-binding protein or only store it.
IgM antibody to hepatitis B core antigen (anti-HBc) was assayed using a commercial kit in acute and chronic hepatitis B virus (HBV) infection and evaluated for its diagnostic and clinical significance. IgM anti-HBc was positive in all of 21 cases with type B acute hepatitis in the acute phase, and was also detected in 5 of 20 cases with type B chronic persistent hepatitis, in 4 of 20 patients with type B chronic active hepatitis and in one of 10 with type B liver cirrhosis. The absence of this marker was noted in all of 20 asymptomatic hepatitis B surface antigen (HBsAg) carriers and in 50 with HBsAg-negative patients with liver disease and in 200 healthy blood donors. The cut-off index of IgM anti-HBc was greater than 2.0 in all serum samples obtained in the acute phase of type B acute hepatitis, but was below 2.0 in type B chronic liver disease. A close relationship was found between the presence of IgM anti-HBc and the degree of inflammatory activity in patients with HBsAg-positive chronic liver disease. These data show that examination of IgM anti-HBc is useful in distingushing type B acute hepatitis from type B chronic liver disease, and also in evaluating the severity of disease in type B chronic liver disease.
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The localization of plasma retinol-binding protein (RBP) in the human kidney was determined by two immunocytochemical techniques, the PAP method and the protein A-gold technique. By using the affinity purified antibody against RBP obtained from the urine of the patients with cadmium poisoning (Itai-Itai disease), the immunoreactive substances were located by light microscopy in the proximal tubules of the human kidney. By immuno-electron microscopy, the stained organelles were identified as lysosomes in both S1 and S2 segments of the tubules. These data suggested that the reabsorption of low molecular weight plasma proteins like RBP can occur in the two segments. We inferred a similarity between the S1 and S2 segments concerning the reabsorption of RBP.
Prealbumin, immunoglobulin G, A, and M concentrations in serum and cerebrospinal fluid from patients with familial amyloid polyneuropathy (Japanese type) were determined and compared with those of asymptomatic relatives or controls. Prealbumin concentrations were not significantly different between them. Using polyacrylamide disc-gel electrophoresis, no qualitative difference in the serum prealbumin was found between them. Among the serum immunoglobulins, only the immunoglobulin A concentration was significantly elevated in the patients as compared with asymptomatic relatives.
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Amyloid fibril protein was purified from postmortem organs of patients with familial amyloid polyneuropathy. In immunodiffusion tests, the protein reacted with antihuman prealbumin antibody but not with antihuman retinol-binding protein or antihuman immunoglobulin G (IgG). In immunoelectrophoresis, the amyloid fibril protein gave a single line with a slightly faster mobility than prealbumin. Immunohistochemical analysis, using fluorescent and peroxidase-antiperoxidase methods, showed that the amyloid deposits contained antigenic determinants of human retinol-binding protein and IgG but not prealbumin.
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