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Biomedical subjects

T Aiba

Publications and source records attributed to T Aiba.

At least 109 records · Page 6Linked to original sources
PubMed1980

[Giant intracranial aneurysm visualized by prolonged injection angiography--case report (author's transl)].

A case of giant intracranial aneurysm which almost completely occluded the internal carotid artery and was diagnosed angiographically by prolonged injection technique was reported. A 62-year-old house-wife was admitted to the Department of Neurosurgery of The Asahi General Hospital, complaining of headache, nausea, and left ptosis. Neurological examination revealed left IInd, IIIrd, IVth, and VIth cranial nerve palsy. Films and laminagrams of the skull demonstrated the double floor of the sella trucica. Plain CT scan showed an oval high density area without surrounding low density area in the left middle cranial fossa. A left carotid angiogram revealed almost complete occlusion of the internal carotid artery at the foramen lacerum. Good cross filling through the anterior communicating artery was seen in the right carotid angiogram. Pre-operative diagnosis was pituitary tumor which extended to the middle cranial fossa. Left fronto-temporal craniotomy was performed and the tumor was suspected to be a giant intracranial aneurysm. Post-operative carotid angiogram by prolonged injection technique also showed a blood channel in the aneurysm and a part of the aneurysm. Left carotid ligation was carried out following intracranial surgery and her symptoms were remarkably improved. Apart from left VIth cranial nerve palsy she showed no abnormal neurological findings at discharge. Usefulness of the prolonged injection technique for differential diagnosis of the parasellar tumor was stressed.

Carotid Artery Diseases↗
PubMed1978

Calcium sensitivity of contractile proteins from chicken gizzard muscle.

Actin, myosin, and "native" tropomyosin (NTM) were separately isolated from chicken gizzard muscle and rabbit skeletal muscle. With various combinations of the isolated contractile proteins, Mg-ATPase activity and superprecipitation activity were measured. It was thus found that gizzard myosin and gizzard NTM behaved differently from skeletal myosin and skeletal NTM, whereas gizzard actin functioned in the same wasy as skeletal actin. It was also found that gizzard myosin preparations were often Ca-sensitive, that is, that the two activities of gizzard myosin plus actin without NTM were activated by low concentrations of Ca2+. The Mg-ATPase activity of a Ca-insensitive preparation of gizzard myosin was not activated by actin even in the presence of Ca2+. When Ca-sensitive gizzard myosin was incubated with ATP (and Mg2+) in the presence of Ca2+, a light-chain component of gizzard myosin was phosphorylated. The light-chain phosphorylation also occurred when Ca-insensitive myosin was incubated with gizzard NTM and ATP (plus Mg2+) in the presence of Ca2+. In either case, the light-chain phosphorylation required Ca2+. Phosphorylated gizzard myosin in combination with actin was able to exhibit superprecipitation, and Mg-ATPase of the phosphorylated gizzard myosin was activated by actin; the actin activation and superprecipitation were found to occur even in the absence of Ca2+ and NTM or tropomyosin. The phosphorylated light-chain component was found to be dephosphorylated by a partially purified preparation of gizzard myosin light-chain phosphatase. Gizzard myosin thus dephosphorylated behaved exactly like untreated Ca-insensitive gizzard myosin; in combination with actin, it did not superprecipitate either in the presence of Ca2+ or in its absence, but did superprecipitated in the presence of NTM and Ca2+. Ca-activated hydrolysis of ATP catalyzed by gizzard myosin B proceeded at a reduced rate after removal of Ca2+ (by adding EGTA), whereas that catalyzed by a combination of actin, gizzard myosin, and gizzard NTM proceeded at the same rate even after removal of Ca2+. However, addition of a partially purified preparation of gizzard myosin light-chain phosphatase was found to make the recombined system behave like myosin B. Based on these findings, it appears that myosin light-chain kinase and myosin light-chain phosphatase can function as regulatory proteins for contraction and relaxation, respectively, of gizzard muscle.

Actins↗