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N Honma

Publications and source records attributed to N Honma.

29 records · Page 2Linked to original sources

Silent zone on Lorenz plots of the ventricular response before termination of paroxysmal atrial fibrillation--report of a case.

An ambulatory 24 h Holter electrocardiogram was recorded during paroxysmal atrial fibrillation in a 67-year-old man. His paroxysmal atrial fibrillation terminated spontaneously approximately 12 h after the start of recording. The RR variability of this Holter recording was studied using Lorenz plots, frequency domain analysis, and time domain analysis. A silent zone appeared on the Lorenz plots beginning a few hours before the termination of his attack. The coefficient of variance (CV) and the power of the high-frequency component of RR variability (HF) gradually increased toward the termination. The silent zone was closely related to the functional refractory period of the atrioventricular node estimated from the Lorenz plots, and the functional refractory period was significantly correlated with the CV and HF power of RR variability. This case suggests that a silent zone on Lorenz plots reflects increased parasympathetic tone. In addition, such a silent zone may be useful for predicting the course of paroxysmal atrial fibrillation and for evaluating the role of the autonomic nervous system in this condition.

Aged↗

Electron-microscopic and immunohistochemical study of beta-2-microglobulin-related amyloidosis.

beta 2-Microglobulin (beta 2-MG)-related amyloidosis has been reported as a complication in long-term hemodialysis patients. We observed beta 2-MG amyloid deposits in synovial sheaths, bone cysts and gastric mucosa. They showed unique ultrastructural features, that is bundles or nodules consisting of curved or linear amyloid fibrils, associated with various cell reactions. The electron-microscopic histochemical study showed that they strongly stained with periodic acid-silver methenamine stain. A similar phenomenon was noticed in the spicules or bundles of amyloid fibrils in primary and secondary renal amyloidosis. With the cationic reagent toluidine blue 0, proteoglycan-like structures were observed around amyloid bundles and nodules, but not on each fibrils. Based on these results, we postulate that there is a close relationship between ultrastructural features and histochemical characteristics in beta 2-MG amyloid fibrils.

Amyloidosis↗

Beta 2-microglobulin: a new form of amyloid protein associated with chronic hemodialysis.

Carpal tunnel syndrome (CTS) has been associated with amyloid deposits and is now regarded as a major complication in chronic hemodialysis patients. While this new syndrome has been receiving increasing attention, its etiology has not been clarified. We have isolated amyloid fibrils from amyloid laden tissues inside the carpal tunnel in four different hemodialysis patients with CTS. After solubilization in guanidine HCl, a significant amount of the protein was located in a homogeneous, low molecular weight fraction. Each protein was found to be identical to beta 2-microglobulin with regard to its molecular weight of 11,000 on SDS-PAGE, amino acid composition and N-terminal amino acids: Ile-Gln-Arg-Thr-Pro-Lys-Ile-Gln-Val-Tyr-Ser-Arg-His-Pro-Ala-Glu. In direct immunofluorescent study, anti-beta 2-microglobulin did react positively with amyloid deposits. These results demonstrate that the amyloid associated with chronic hemodialysis contains as major component a new form of amyloid fibril protein that is homologous to beta 2-microglobulin. It is postulated that beta 2-microglobulin cannot be removed from the blood by conventional hemodialysis, and accumulates in tissues causing the formation of amyloid fibrils, which, having a relatively high affinity to the carpal tunnel area, thus causes CTS.

Amino Acids↗