Subendocardial hemorrhage of the left ventricle--a study of medicolegal autopsy cases.
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Biomedical subjects
Publications and source records attributed to M Iwasa.
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A new type of progressive muscular dystrophy, autosomal recessive distal muscular dystrophy, is described, based on observations on 17 cases (8 males and 9 females) in 8 families, including an autopsied case. The disease developed in young adults. Muscle weakness and atrophy were most marked in the distal parts of the legs, especially in the gastrocnemius and soleus muscles, and then spread to the thighs and gluteal muscles. Early impairment of standing on tip-toe with retention of the ability to stand on the heels was conspicuous. Difficulty in climbing stairs, standing up and walking subsequently appeared, but rarely progressed to confinement to bed. The forearms became mildly atrophic, with decrease in grip strength, but the small hand muscles were spared. The EMG showed myopathic changes and nerve conduction was normal. Serum creatine kinase activity was characteristically increased up to 100-fold in the early stages of the disease. It was also markedly increased in subjects in the preclinical stage and mildly in some heterozygotes. Muscle biopsies revealed myopathic changes with severe segmental necrosis accompanied by regeneration. The changes were similar to those of Duchenne muscular dystrophy. An autopsied case, aged 68 years, showed generalized muscle abnormalities with a distal predominance. The muscles in the lower legs, especially those of the calves, were severely affected. No lesions were found in the brain, spinal cord or peripheral nerves.
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Amylase activities were detected significantly in saliva from human, macaques and rodents and slightly in the vegetable and fruit extracts. Dried stains on filter paper prepared from human and mammalian saliva, and the vegetable and fruit extracts were subjected to starch-iodine test and blue starch polymer-agar plate test. Both tests showed strong positive reactions with the macaque and rodent saliva stains as well as human, but the vegetable and fruit stains showed clear positive reactions only in the starch-iodine test. The results suggest that these tests are not specific for human saliva and that for screening test of saliva stains, blue starch polymer-agar plate test is more suitable than starch-iodine test. Rabbit antisera against alpha-amylase isolated from the human submaxillary glands were prepared. In double immunodiffusion test with the human and mammalian saliva, human and macaque saliva produced precipitation lines. Human saliva gave patterns of partial identity with saliva from Japanese monkey and crab-eating monkey and these two macaque saliva gave total identity with each other. Anti-alpha-amylase sera absorbed with Japanese monkey saliva reacted only with human saliva. This suggested that the anti-alpha-amylase sera absorbed with macaque saliva make it possible to identify human saliva stain.
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A rabbit anti-saliva hyperimmune serum was raised against pooled human saliva. After absorption with human serum and semen, the immune serum formed two or three distinct precipitation lines with human saliva by the Ouchterlony method. Based on the presence or absence of a precipitation line, close to the antigen well designated as Pl, all human saliva were divided into two groups; Pl+ and Pl-. The incidence of Pl+ saliva was 114 out of 154 samples (74%). By immunoelectrophoresis with anti-saliva serum preabsorbed with Pl- saliva, Pl+ saliva formed a precipitation line in cathodal area. No amylase activity was found in this precipitation line but it was stained with the Schiff's reagent. Pl protein was isolated by Sephadex G-100 and ion-exchange chromatography. Isoelectric focusing of the Pl protein in polyacrylamide slab gel containing urea revealed that the protein differed from any known parotid salivary proteins such as Pr, Db, Pa and Pm.
A antigens of red blood cells and body fluids such as saliva, semen and sweat could be serologically distinguished using rabbit or guinea pig immune anti-A. As for antisera specific for red blood cell A, A+ rabbits were intravenously immunized with A group red blood cells. The resulting antisera were absorbed with O and B red cells and with A. Se saliva. The absorbed anti-A reacted with A red cells (titer 1:32) and was not inhibited with A. Se saliva. Guinea pigs were intramuscularly injected with A. Se saliva. Crude antisera contained agglutinins to human red cells which were abolished by absorption with A red cells. After absorption with O. Se saliva, the antisera were proved to have agglutinin activity with A group saliva using latex coated with A. Se saliva. A antigens from blood or body fluid stains could be distinguished by the elution method with these anti-A sera.
To examine common antigens between human and monkey sera, sera from 19 kinds of monkey were investigated with crossed and rocket immunoelectrophoresis using antisera to human serum proteins. In the crossed immunoelectrophoresis, the number of precipitation lines, 40 in human and 8 in the lower primates, increased according to the order of phylogenetic classification, and the lines due to albumin and gamma-globulin were observed in all the monkey sera examined. Quantitative investigation was performed by rocket immunoelectrophoresis with 8 kinds of mono-specific anti-serum protein. Alpha 2-Macroglobulin, orosomucoid, transferrin, IgG and IgM were not observed in monkeys of Loricidae family. Relatively large amounts of orosomucoid, albumin, IgG and transferrin were detected in monkeys of Cebidae family. It was considered that the distribution of serum proteins possessing antigens common to human is not related with the order of phylogenetic classification.
The present authors have reported that each of ABH antigens of saliva consisted of saliva specific antigen and common antigen between saliva and red cells. Using saliva specific anti-A and B, 77 samples of A,B and AB groups could be determined as strong secretor (Se) or weak secretor (se). Frequency of Se was 62% for A group saliva, 45% for B, and 76% for A antigen and 75% for B antigen of AB group saliva, respectively. The secretor status of twenty-four O salivas could not be determined by saliva specific anti-H. Compared with the ordinary secretor system, some subjects belonging to Se in the ordinary system were typed as se in the new system, whereas all se saliva (three cases) in the ordinary system were typed as se in the new system.
Agglutinability of red blood cells against anti-D increased remarkably when the cells were treated with proteolytic enzymes, such as bromelain, chymotrypsin, ficin, papain, pronase and trypsin. When stroma prepared from normal red blood cells was treated with any of proteolytic enzymes, however, Rh-Hr blood type activities were completely abolished. The similar results were obtained from stroma solubilized with detergents which was treated with enzymes after being prepared. Of all the enzymes, ficin acted more slowly than the others did. Neuraminidase or phospholipase A2 had no effect on Rh-Hr activities at all. SDS-polyacrylamide gel electrophoretic pattern of stroma prepared from bromelain, ficin and pronase-treated red blood cells were quite different from that of normal stroma.
Lea substance or immune complex which was prepared with anti-D and D-active Band 3 was trapped in autologous red cell ghost. The trapped immunogens were administered intravenously to rabbits or guinea pigs. Rabbits immunized with Lea substance loading ghost produced antisera of relatively low titers, but they contained specific incomplete anti-Lea antibody (titer 1:128) after absorption procedure, which were higher than that of antisera prepared by the ordinary method. Guinea pig antiserum to the immune complex contained specific incomplete anti-D (titer 1:128). Immunoglobulin class analyses revealed that the anti-Lea consisted mainly of IgM and the anti-D of IgG. It was considered that intravenous injection of the immunogen trapped in ghost is useful for preparing hemagglutinin of sufficient titers.
In the present study we sought to determine the presence of myoglobin in human thyroid tissue. When reacted with antihuman myoglobin antibody on the Ouchterlony plate, homogenates of human thyroid tissue formed a precipitation line. When the human thyroid extract was included in human myoglobin RIA, the dilution curve of thyroid extract was parallel to the standard curve of myoglobin. When the myoglobin immunoreactivity in thyroid extract was fractionated with Sephadex G 75 column, the immunoreactivity was eluted in a peak identical with authentic myoglobin. The position of the peak was different from that of thyroglobulin. Myoglobin concentration in thyroid tissue was estimated to be 0.7-110 mg/g wet wt, being about 1/6000 to 1/40 of that in skeletal muscle. Histochemical studies demonstrated the presence of myoglobin immunoreactivity in thyroid tissue, especially in the apical border of thyroid epithelial cells, implying a functional role in iodinating process or exocytotic-endocytotic process.
Seminal plasma from 120 subjects was examined by crossed immunoelectrophoresis using anti-seminal plasma. The samples were divided into two groups depending on a precipitation line which migrated fast in the first dimension electrophoresis. This precipitation line showed an incidence of 48 percent and was proved to have no acid phosphatase, esterase or lactate dehydrogenase activity and was not stained with Schiff's reagent. Analysis with column chromatography, Sephadex G-200 and Sephadex G-50, revealed that molecular weight of the protein was about 10,000 dolton. The difference was not identified with the other methods; polyacrylamide gel electrophoresis and agarose immunoelectrophoresis.
To prepare anti-M and -N of a sufficient potency, M or N substance trapped in autologous ghost was intravenously administered to rabbits. The potency and specificity of antisera prepared were compared with antisera prepared by other immunization methods. Rabbits immunized intravenously or intramuscularly with M or N substance alone produced no significant antibodies. Immunization with the substance loading ghost produced crude antisera of relatively low titers, but they were proved to contain specific anti-M and -N after absorption procedure which were higher than those prepared by usual intravenous injection of red cells. There was remarkable difference in immunoglobulin class between antisera prepared with the substance loading ghost and that by red cell immunizations; the former consisted of IgM and IgA, and the latter of IgG and IgA. It was considered that intravenous injection of the antigen trapped in ghost is useful for preparing hemagglutinin of sufficient titers.