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Biomedical subjects

K Asano

Publications and source records attributed to K Asano.

At least 523 records · Page 29Linked to original sources
PubMed1982

[Treatment of elderly patients with hepatocellular carcinomas with mitomycin C and 5-fluorouracil].

Twenty elderly patients with hepatocellular carcinoma were treated with 5-fluorouracil (5-FU) at a daily dose of 200-300 mg per os, and with a combination of 0.3-0.35 mg/kg of mitomycin C (MMC) iv on day 1 and 8-10 mg/kg of 5-FU iv daily starting on day 1 for 5 consecutive days, repeating at 4 week intervals. According to the Koyama-Saito's criteria, there was no response in the 5-FU treatment, while a 20% (2/10) of response rate (2 partial responses) was obtained in the combination regimen. The durations of response in 2 partial responses were 7.3 and 4.0 months, respectively. The median survival with MMC and 5-FU was 3.4 months compared with 1.5 months with 5-FU alone, and the survival was correlated with tumor response. The combination produced more gastrointestinal toxicities and myelotoxicities compared to a single drug, but they were well tolerated. These results support the superiority of the combination of MMC and 5-FU over 5-FU alone in the treatment of elderly hepatocellular carcinoma.

Aged↗
PubMed1982

Viral proteins in cell fusion.

F (fusion) and HANA (hemagglutinin and neuraminidase) glycoproteins of HVJ (Sendai virus) were purified and characterized. The NH2-terminal hydrophobic region of the F1 (larger) subunit of F (fusion)-glycoprotein seems to be required for the hemolytic and cell fusion-inducing activity of the virus for the following reasons. (1) Selective splitting off of a 2,500-3,500 dalton segment from the NH2-terminal region of F1 by chymotrypsin or thermolysin resulted in inactivation of the biological activities of HVJ. (2) At least a part of this region may be exposed to the surrounding medium, since it is preferentially iodinated and is easily split by aminopeptidase M, chymotrypsin, and thermolysin. Tryptic digestion, which does not remove the NH2-terminal region but produce nicking of F1 subunit to subfragments F1a (larger one) and F1b (smaller one), resulted in substantial structural changes evidenced by circular dichroism measurement and iodination by lactoperoxidase method. Trypsin-digested F seems to have the NH2-terminal hydrophobic region buried within hydrophobic interior of the protein (or in the lipid bilayers). Based on these and other results, we propose a hypothesis featuring direct interaction of the hydrophbic region with the lipid bilayers of the target-cell membrane as an important step in fusion reactions between the viral envelope and cell membranes.

Animals↗