Akiko Yamashiro

Kobe City Medical Center General Hospital, Kōbe, Hyōgo, Japan

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Publications (10)0.89 Total impact

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    ABSTRACT: An 84-year-old Japanese man was admitted because of pancytopenia. The bone marrow was hypoplastic with a predominance of abnormal small lymphocytes and grape cells, which were positive for CD19 and CD20, and partially for the surface ĸ-light chain. Systemic CT scanning showed neither lymph node swelling nor hepatosplenomegaly. Serum immunoelectrophoresis and rocket immunoselection assays showed the presence of monoclonal IgG protein without a corresponding light chain and faint IgMĸ monoclonal protein. Histologic analysis of the clot preparation of the bone marrow aspirate facilitated a diagnosis of lymphoplasmacytic lymphoma (LPL). PCR analysis of the marrow cells demonstrated a clonal rearrangement of the immunoglobulin heavy-chain gene. From these results, we made a final diagnosis of γ-heavy-chain disease (γ-HCD) with underlying LPL localized in the bone marrow. We performed only a single course of immunochemotherapy (rituximab and fludarabine) in view of severely impaired hematopoiesis, which resulted in marked reduction of lymphoma cells and improvement of hematopoiesis. This report suggests the efficacy of rituximab plus fludarabine therapy for LPL-associated γ-HCD.
    Acta Haematologica 08/2012; 128(3):139-43. · 0.89 Impact Factor
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    ABSTRACT: A 80-year-old man was admitted because of acute-onset thrombocytopenia and renal failure. He was diagnosed with Bence Jones (lambda) -type multiple myeloma associated with sepsis with methicillin-resistant Staphylococcus aureus. On admission, serum amylase activity was elevated to 1,814 IU/l (98% salivary type; S-amylase). Several days after admission, he developed bilateral myelomatous pleuritis. The activity of S-amylase in the effusion was 5,495 IU/l. Myeloma cells in the pleural effusion were positive for cytoplasmic amylase with an antibody against human amylase. High S-amylase activity was detected in the supernatant of cultured myeloma cells in the effusion. Furthermore, S-amylase gene expression was detected by RT-PCR. A diagnosis of amylase-producing multiple myeloma was made. The patient died of renal insufficiency complicated by severe DIC. We report a rare case of amylase-producing myeloma confirmed by immunocytochemistry, culture method, and gene expression.
    [Rinshō ketsueki] The Japanese journal of clinical hematology 12/2007; 48(11):1484-8.
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    ABSTRACT: Although abnormalities of glycosylation profile in serum IgG have been demonstrated in a variety of inflammatory autoimmune diseases such as rheumatoid arthritis, there are only a few reports describing long term monitoring of N-glycosylation profiles in such patients. Here we report the serial finding of N-glycosylation profiles of IgG-kappa M-protein in a patient with multiple myeloma monitored for two years. In this patient, serum formed a gel precipitation upon exposure to air. The HPLC mapping method demonstrated that IgG M-protein in the patient exhibited a significant decrease in the ratio of fucosyl to afucosyl N-glycans compared with that in a healthy control. With remission, the IgG M-protein showed an increase in this ratio, becoming closer to that in the healthy control. However, the gel-precipitation persisted. This finding suggested that this unique property of serum may not be related to the glycosylation profile of the M-protein.
    Rinsho byori. The Japanese journal of clinical pathology 08/2007; 55(7):626-9.
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    ABSTRACT: Celiac disease is a permanent intolerance to ingested gluten that results in immunologically mediated inflammatory damage of the small intestinal mucosa. Here we report the case of a patient with Celiac disease demonstrating simultaneous macroamylasemia and macrolipasemia. The patient showed persistently elevated levels of serum amylase and lipase. Amylase and lipase in normal serum were eluted from a Superdex-200 column after the 4S protein. These enzymes in the serum from this patient were eluted in the 19S protein. This finding indicated that these enzymes from this patient had a molecular weight greater than that of normal amylase and lipase. Immunoprecipitation assay showed that amylase was bound to polyclonal IgG and IgA, whereas lipase was bound to polyclonal IgA. To our knowledge, the simultaneous presence of macroamylase and macrolipase in the same patient has been previously reported in only four cases. Interestingly, two of those patients had Celiac disease. If macroamylase and macrolipase are present, the possibility of Celiac disease should be considered.
    Rinsho byori. The Japanese journal of clinical pathology 11/2003; 51(10):974-7.
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    ABSTRACT: We report a case of mu-heavy chain disease. A 56-year-old woman presented with anemia and hemorrhagic diathesis. The serum of the patient was found to have free mu-heavy chain. The patient also had a kappa type-Bence Jones protein in serum and urine. Immunoelectrophoresis showed an abnormal precipitin line in the alpha 2-globulin region which reacted with antiserum to mu-chain but not with antiserum for light chains. The molecular weight of the monomer of the patient's mu-heavy chain protein was approximately 67,000 daltons less than that of the normal mu-heavy chain protein.
    Rinsho byori. The Japanese journal of clinical pathology 10/2003; 51(9):847-51.
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    ABSTRACT: We present the case of a 69-years-old man who was admitted to hospital with multiple myeloma. IgG-kappa type monoclonal protein was detected in the serum. When we separated the serum obtained from blood sample of the patient and the lid of the collecting tube was opened, the patient's serum became gelled immediately. When the lid of the collecting tube remained closed, the patient's serum did not become gelled even at 4 degrees C. Moreover, the gelled serum of the patient did not resolve at 56 degrees C. Taken together, these results indicated that gel formation of the patient's serum may not be due to cryoglobulin. It was found that the pH of the patient's serum elevated to pH 8.0 quickly after exposed to air. It was also found that the patient's serum, but not the sera of other IgG-kappa multiple myeloma patients, became gelled as soon as PBS of pH 8.0 was added. These results highly suggest that the patient's serum becomes gelled at pH 8.0. However, the isoelectric focusing of isolated precipitation in the patient showed fractions around the pH 8.5-8.7 zone, which was different from the pH at which the precipitation began to form. We think that this may be the first report of a multiple myeloma patient whose serum becomes gelled after exposed to air.
    Rinsho byori. The Japanese journal of clinical pathology 05/2002; 50(4):404-9.
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    ABSTRACT: Here we report a case demonstrating simultaneous macroamylasemia and macrolipasemia. The patient showed persistently elevated serum amylase and lipase activities. On thin-layer gelfiltration, normal serum amylase migrated as a round spot behind albumin. However, serum amylase from this patient migrated slightly ahead of albumin. This finding indicated that serum amylase from this patient had a molecular weight greater than that of normal amylase. Lipase of normal serum was eluted from a Sephacryl S-300 column after the 4S protein. Lipase in the serum from this patient was eluted from the column slightly behind the 19S protein. This finding indicated that serum lipase from this patient also had a molecular weight greater than that of normal lipase. The conversion of macroamylase and macrolipase was observed when the normal serum was mixed with the patient's serum. To determine the isotypes of immunoglobulin (Ig) that was bound to amylase and lipase in the patient's serum, we investigated the effect of adding various anti-human Ig sera to the patient's serum. Amylase activity was precipitated only with anti-IgA lambda and lipase activity was precipitated both with anti-IgA lambda and anti-IgA kappa (anti-IgA kappa > anti-IgA lambda). Taken together, these data indicate that the material that enhanced amylase and lipase activities in the patient's serum was monoclonal IgA; IgA lambda for amylase and both IgA lambda and IgA kappa for lipase.
    Rinsho byori. The Japanese journal of clinical pathology 04/1997; 45(4):391-4.
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    ABSTRACT: We found extremely low activity of serum lactate dehydrogenase (LDH, EC. 1.1.1.27) in a 70-year-old female patient. The decrease of LDH activity was observed when the normal serum was incubated with the patient's serum. Inhibition rate of LDH activity by the patient's serum was higher at 4 degrees C than at 37 degrees C. The patient's serum inhibited both subunits of LDH, and inhibited more strongly the M-subunit than the H-subunit LDH isoenzymes. IgG (lambda type) in the patient's serum was found to be responsible for the inhibition of LDH activity. The mechanism why IgG inhibiting LDH activity developed in the patient's serum remain undetermined.
    Rinsho byori. The Japanese journal of clinical pathology 10/1992; 40(9):970-6.
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    ABSTRACT: Conventional isoenzyme and enzyme values in serum usually are normal during the first few hours of acute myocardial infarction (AMI). Thus definitive diagnosis may be delayed. Measurement of serum creatine kinase (CK) isoform has begun to attract attention. In this study, we measured CK isoform with an immunoinhibition method in the first available samples from patients with AMI and from healthy subjects. In the 394 healthy subjects, the mean ratio of MM3 to MM1 of CK isoform was 0.494 +/- 0.1495 (SD). The upper limit of the reference values for this ratio was considered to be 0.793 (mean + 2 SD). In 40 of 48 patients, this ratio in the first available samples from patients with AMI was greater than 0.793. In 15 of 20 patients whose total CK activity was less than 260 IU/l, this ratio was greater than 0.793, while CK-MB activity measured with the immunoinhibition method was well within the reference range in all of these patients. Our results show that in the first available samples from patients with AMI, measurement of the ratio of MM3 to MM1 of CK isoform has the highest diagnostic efficiency. Thus, measurement of CK isoform with the immunoinhibition method can be applied for early diagnosis of AMI.
    Rinsho byori. The Japanese journal of clinical pathology 04/1991; 39(3):289-94.
  • T Oita, A Yamashiro, K Fukuda, S Kasakura
    Rinsho byori. The Japanese journal of clinical pathology 11/1987; 35(10):1139-43.