Biomedical subjects

Ichiro Yoshida

Publications and source records attributed to Ichiro Yoshida.

21 records · Page 2Linked to original sources

PubMed2002

Measurement of laminins in the cerebrospinal fluid obtained from patients with Alzheimer's disease and vascular dementia using a modified enzyme-linked immunosorbent assay.

We developed a new enzyme-linked immunosorbent assay (ELISA) system using antibodies against intact human laminin, laminin alpha(5)-chain, laminin beta(1)-chain, laminin gamma(1)-chain and laminin alpha(1)-chain peptide (YFQRYLI). Using this ELISA, we measured the anti-laminin immunoreactivity levels in the cerebrospinal fluid (CSF) obtained from patients with Alzheimer's disease (AD), vascular dementia (VaD), and other disorders. The present study showed the levels of certain laminins in CSF to demonstrate significant differences in the chain levels in different dementias. The AD group showed a significantly lower level of anti-laminin gamma(1) immunoreactivity. The late-onset AD group showed significantly elevated anti-laminin alpha(1)-peptide (YFQRYLI) immunoreactivity levels in comparison with the early-onset AD group and controls. On the other hand, the VaD group showed significantly higher levels of anti-intact human laminin and anti-laminin beta(1) immunoreactivity. The assays of anti-laminin immunoreactivity levels in CSF provided an efficient sensitivity (85.0%) and specificity (93.7%) for the diagnosis of AD by using the ratio of tau to anti-intact human laminin immunoreactivity levels. These results suggest that CSF laminin or its derivatives may correlate with the pathogenesis of AD and VaD, and the prevention of the proteolytic activity may be an effective therapeutic method for either preventing or slowing down the progression of AD. Furthermore, it was shown that performing ELISA for CSF laminins may prove to be useful for detecting the biological markers of AD and VaD.

Aged↗

PubMed2002

Effect of sucrose on formation of the beta-amyloid fibrils and D-aspartic acids in Abeta 1-42.

Beta-amyloid peptide 1-42 is a major peptide constituent of beta-amyloid fibrils. We investigated the role of sucrose on the deposition and the D-aspartic acid formation in an amyloidogenic peptide 1-42 under physiological conditions. From analyses using thioflavine-T fluorometric assay and electronmicroscopic spectroscopy after 60 h incubation at 37 degrees C, it was found that sucrose retarded the fibril formation in the amyloidogenic peptide. The retardation of the formation of amyloid fibrils by sucrose was suggested to be not due to viscosity but due to disturbance of the assemlby of alpha-helix containing peptides. Moreover, we showed that the formation of D-aspartyl residue, which is found in beta-amyloid fibrils from Alzheimer disease brains, in the amyloidogenic peptide was also retarded in the presence of sucrose.

Amyloid beta-Peptides↗

PubMedDate not supplied

A patient with Cotard syndrome who showed an improvement in single photon emission computed tomography findings after successful treatment with antidepressants.

We report the case of a presenile woman with Cotard syndrome, in the context of major depression, who showed an improvement in bilateral frontal hypoperfusion in a SPECT study using 99mTc-HMPAO after undergoing successful treatment with antidepressant therapy. We also retrospectively evaluated her clinical course based on the clinical stages. The symptoms of Cotard syndrome have been reported to change dramatically according to the stages. This peculiarity made it difficult for us to rapidly diagnose Cotard syndrome in the context of major depression, and not dementia, and thereby adequately treat the patient in our case. Differences in the reduced blood flow regions and a time lag from psychiatric remission were observed before the improvement in the SPECT findings when comparing our case with a previously reported case of Cotard syndrome. These differences suggest that the mechanism of Cotard syndrome is still not well understood at the present time.

Antidepressive Agents↗