Charles S. Davidson – 1 November 1984

Kenji Fujiwara, Yasuhiko Ohta, Itsuro Ogata, Yuzuru Sato, Yuji Oka, Shigeki Hayashi, Katsuyoshi Takatsuki, Hiroshi Oka – 1 November 1984 – The effect of 4–(3,7,ll,15‐tetramethyl‐6,10,14‐hexadecatrienoyl)morpholine (E‐0712), a new synthetic compound, on liver injury induced by two hepatotoxins in rats was studied. Oral doses of E‐0712 four times at 0, 6, 12 and 18 hr significantly attenuated elevated SGPT values and prolonged prothrombin time (PT) at 24, 36, 48, 60 and 72 hr in rats with a single s.c. dose of D‐galactosamine in which SGPT values and PT reached the peak within 48 hr.

Anne Marie Jezequel, Patrizia Bonazzi, Giuseppe Novelli, Cinzia Venturini, Francesco Orlandi – 1 November 1984 – Valproic acid (VPA) is a simple fatty acid largely used as anticonvulsivant agent. Side effects are uncommon, but cases of fatal hepatic failure have been reported. To elucidate the mechanism of VPA‐induced hepatotoxicity, the functional and structural changes associated with administration of sodium valproate (NaVPA) to rats (200 or 600 mg per kg, i.p.) were analyzed.

Esteban Celis, Tse Wen Chang – 1 November 1984 – HBsAg from plasma of chronic hepatitis B carriers was purified by affinity chomatography using a mouse monoclonal antibody specific for HBsAg. Elution with buffer at two different pH values separated HBsAg into two fractions: one contained high amounts of immune complexes associated with HBsAg; the other contained larger quantities of the HBsAg polypeptides P24 and GP27 and only small amounts of immunoglobulin.

G. Richard Granneman, Shyh‐Ing Wang, James W. Kesterson, Joseph M. Machinist – 1 November 1984 – The role of metabolites in valproic acid (VPA)‐associated hepatotoxicity was studied in rats. The most steatogenic mono‐unsaturated metabolite, 4‐en‐VPA, caused the greatest changes in indicators of β‐oxidation inhibition (dicarboxylic aciduria, β‐hydroxybutyrate reduction); however, the biochemical effects were much less pronounced than those reported for hypoglycin. Steatosis in VPA‐treated rats occurred only at nearly lethal doses.

Yutaka Sasaki, Takenobu Kamada, Norio Hayashi, Nobuhiro Sato, Akinori Kasahara, Hideyuki Fusamoto, Sadao Shiosaka, Masaya Tohyama, Yahe Shiotani – 1 November 1984 – The distribution of immunoreactive glucagon, substance P (SP) and vasoactive intestinal polypeptide (VIP)‐like structures was investigated in the rat liver, with special reference to the hepatic vasculature by means of the indirect immunofluorescence method. Immunoreactive structures of glucagon were seen in the walls of the portal vein, hepatic artery and hepatic vein, but not in the central vein.

Robert E. Kane Iii, Lee J. Chen, M. Michael Thaler – 1 November 1984 – We studied the regulation of hepatic bile salt sulfotransferase activity by gonadal hormones and the effect of gonadal hormones on two bile salt sulfotransferase isoenzymes. Bile salt sulfotransferase enzyme activity was three times greater in the female than in the male rats. Oophorectomy significantly decreased bile salt sulfotransferase activity in the female, but orchidectomy had no effect on bile salt sulfotransferase activity in the male.

Dale C. Snover, Richard K. Sibley, Deborah K. Freese, Harvey L. Sharp, Joseph R. Bloomer, John S. Najarian, Nancy L. Ascher – 1 November 1984 – The histopathological features of orthotopic liver transplants were evaluated in 63 serial biopsy specimens from 17 patients. Biopsies were taken at the time of insertion of the liver (six biopsies), at the time of development of liver function abnormalities (11 biopsies) and as follow‐up to previously abnormal biopsies (46 biopsies).

Charles S. Lieber – 1 November 1984

Alan M. Leichtner, Monty Krieger, Alan L. Schwartz – 1 November 1984 – Low density lipoprotein (LDL) processing was investigated in a human hepatoma‐derived cell line, Hep G2. Hep G2 cells bound, internalized and degraded LDL via a saturable, high affinity (Kd ∼ 2 x 10−8M) pathway similar to that present in other mammalian cells. Although 80% of the uptake and degradation of 125I‐LDL was inhibited by 40‐fold excess native LDL, the same concentration of methylated LDL, which cannot bind to LDL receptors, had virtually no effect on processing.