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Biomedical subjects

L L Kuo

Publications and source records attributed to L L Kuo.

6 recordsLinked to original sources

Sphenoidal EEG recording using acupuncture needle electrode in complex partial seizure.

Sphenoidal EEG recording using an uninsulated acupuncture needle electrode were performed in 41 patients with or suspected of complex partial seizures of temporal lobe origin. The anterior temporal spikes were detected by the routine EEG in 17 patients (41%) and by the acupuncture sphenoidal needle in 29 patients (70%). The anterior temporal spikes recorded by the acupuncture needle were almost identical in configuration, amplitude and distribution to those recorded by conventional wire or insulated needle sphenoidal electrodes. The sequence in the frequency of spike detection by these 3 types of sphenoidal electrode were SP1-2, T1-2, F7-8 and A1-2 locations. The spikes of maximal amplitude were most frequently recorded by the SP electrode followed by the T1-2 electrode. The placement of the disposable acupuncture needle was simple and safe. Patients experienced minimal discomfort or pain that lasted at most 0.5 h. No complications occurred. The records were generally free of artifacts. It is concluded that the acupuncture needle can be used as sphenoidal electrode in outpatient EEG recording for the diagnosis of complex partial seizures of anterior temporal-origin.

Action Potentials↗

A nested set of eight RNAs is formed in macrophages infected with lactate dehydrogenase-elevating virus.

Total RNA was extracted from primary cultures of mouse macrophages isolated from 10-day-old mice 6 to 12 h postinfection with lactate dehydrogenase-elevating virus (LDV). Poly(A)+ RNA was extracted from spleens of 18-h LDV-infected mice. The RNAs were analyzed by Northern (RNA) blot hybridization with a number of LDV-specific cDNAs as probes. A cDNA representing the nucleocapsid protein (VP-1) gene located at the 3' terminus of the viral genome (E. K. Godeny, D. W. Speicher, and M. A. Brinton, Virology 177:768-771, 1990) hybridized to viral genomic RNA of about 13 kb plus seven subgenomic RNAs ranging in size from about 1 to about 3.6 kb. Two other cDNA clones hybridized only to the four or five largest subgenomic RNAs, respectively. In contrast, two cDNAs encoding continuous open reading frames with replicase and zinc finger motifs hybridized only to the genomic RNA. The replicase motif exhibited 75% amino acid identity to that of the 1b protein of equine arteritis virus (EAV) and 44% amino acid identity to those of the 1b proteins of coronaviruses and Berne virus. Combined, the results indicate that LDV replication involves formation of a 3'-coterminal-nested set of mRNAs as observed for coronaviruses and toroviruses as well as for EAV, with which LDV shares many other properties. Overall, LDV, like EAV, possesses a genome organization resembling that of the coronaviruses and toroviruses. However, EAV and LDV differ from the latter in the size of their genomes, virion size and structure, nature of the structural proteins, and symmetry of the nucleocapsids.

Amino Acid Sequence↗

Effect of injury and total parenteral nutrition on water and electrolytes of RBC, serum, muscle and liver tissue.

Trauma is associated with an increased rate of tissue catabolism which can lead to a heightened cellular requirement for regeneration of adenosine triphosphate (ATP) and to decreased activities of adenosine triphosphatases. The effect of severe trauma and total parenteral nutrition (TPN) on water and electrolyte levels in red cells, serum, muscle and liver was investigated. In this study, 16 subjects formed the normal control (control group). The injured group consisted of 8 subjects who suffered from severe trauma and/or post-operative complications with or without infection. The TPN group consisted of 8 subjects in a severe catabolic period who underwent TPN treatment. Blood, muscle and liver samples were obtained during surgical procedures. In red cells and serum, all measured electrolyte levels were within normal limits except the serum of the injured group which showed decreased calcium and increased magnesium levels. Muscle and liver tissue analyses for the injured group showed an increase in water content and sodium and chloride levels, but calcium, potassium and phosphate levels in muscle were decreased. Hepatic potassium and calcium levels, however, were both increased in the same group. In the TPN regimen, cell mass was restored, primarily in muscle, with a contraction of the water content. The restoration of electrolyte levels, especially potassium levels, in muscle during TPN reflected an increase in muscle cell mass.

Adult↗

Alterations of Na+-K+-ATPase, Ca2+-ATPase, and Mg2+-ATPase activities in erythrocyte, muscle, and liver of traumatic and septic patients.

Na+-K+-ATPase, Ca2+-ATPase and Mg2+-ATPase activities of erythrocyte membrane, microsomal fractions of rectus muscle, and liver were measured colorimetrically in the biopsy specimens of 14 control, 7 uncomplicated trauma (group 2), and 14 severe trauma or septic patients (groups 3-A and 3-B). In erythrocytes, these three ATPase activities in group 2 were not significantly changed but sepsis of both the acute (group 3-A) and ongoing type (group 3-B) decreased all of the ATPase activities. In muscle, there was a significant loss of three ATPase activities in the acute insult of severe trauma or sepsis (group 3-A), while Na+-K+-ATPase and Mg2+-ATPase activities were not significantly changed in ongoing, severe trauma (group 3-B). In the liver, a tendency for all three ATPase activities to decrease is noted in the severe traumatic group. However, a statistical difference between the control and severe traumatic group showed only for Na+-K+ ATPase and Mg2+-ATPase in group 3-A and Ca2+-ATPase in group 3-B. Correlation coefficients between erythrocyte, muscle, and liver for three ATPase activities are between 0.4 and 0.5. The mechanism which alters ATPase activity remains unknown in this study, but it may account for the variation in traumatic insult, in hemodynamic and hormone changes, and in tissue energy stores.

Adenosine Triphosphatases↗