Actin participates in the structure of liver intermediate filaments

A dominating protein fraction (p45) having molecular weight of 45000 and pI 5.45 was found in the intermediate filaments pellet obtained from rat liver besides the present cytokeratins. Peptide mapping and radioimmunological assays with antibodies against this protein and muscle actin proved that the p45 protein belongs to the actin group. Immunoelectron microscopy revealed that this protein is located on the liver intermediate filaments. By melting of the cytokeratin complexes in urea it was established that p45 protein is complexed with the low molecular weight cytokeratin.     

Selection of HLA compatible donors for patients with HLA antibodies

A strain of 1,507 typised donors enables 15.97 average donors to be selected for a thrombocyte transfusion in one of 75 patients selected at random with HLA antibodies being previously determined (1 to 66 donors per patient). HLA compatible donors were found for 72 patients (97.33 per cent). More than 5 HLA compatible donors could be found for 58 patients. The high number of compatible donors is based on the fact that among 1,507 donors there were 156 HLA homozygotes and 556 donors with 3 HLA-A or B-antigens respectively. Compatibility in the ABO-system was not taken into account.     

Synthesis of intrathecal interferon in systemic lupus erythematosus with neurological complications.

Intrathecal synthesis of interferon in the absence of viral or bacterial infection was detected during the occurrence of neurological complications in two patients with systemic lupus erythematosus. The interferons displayed characteristics similar to those observed in the sera of patients with the disease. No interferon inducing activity was detected in the cerebrospinal fluid or serum of the two patients. These observations support the hypothesis of a localised mechanism of interferon induction in systemic lupus erythematosus which includes the interaction of lymphocytes with damaged tissues.     

Spontaneous Aggregation and Cytotoxicity of the β-Amyloid Aβ1–40: A Kinetic Model

The time dependency of the spontaneous aggregation of the fibrillogenic β-Amyloid peptide, Aβ^1–40, was measured by turbidity, circular dichroism, HPLC, and fluorescence polarization. The results by all methods were comparable and they were most consistent with a kinetic model where the peptide first slowly forms an activated monomeric derivative (AM), which is the only species able to initiate, by tetramerization, the formation of linear aggregates. The anti-Aβ antibody 6E10, raised against residues 1–17, at concentrations of 200–300 nM delayed significantly the aggregation of 50 μM amyloid peptide. The anti–Aβ antibody 4G8, raised against residues 17–24, was much less active in that respect, while the antibody A162, raised against the C-terminal residues 39–43 of the full-length Aβ was totally inactive at those concentrations. Concomitant with the aggregation experiments, we also measured the time dependency of the Aβ^1–40–induced toxicity toward SH-EP1 cells and hippocampal neurons, evaluated by SYTOX Green fluorescence, lactate dehydrogenase release, and activation of caspases. The extent of cell damage measured by all methods reached a maximum at the same time and this maximum coincided with that of the concentration of AM. According to the kinetic scheme, the latter is the only transient peptide species whose concentration passes through a maximum. Thus, it appears that the toxic species of Aβ^1–40 is most likely the same transient activated monomer that is responsible for the nucleation of fibril formation. These conclusions should provide a structural basis for understanding the toxicity of Aβ^1–40 in vitro and possibly in vivo.     

Uteroferrin: A protein in search of a function

Uteroferrin, a purple-colored, iron-containing acid phosphatase, with many of the properties of a lysosomal hydrolase, transports iron from the mother to the conceptus in pregnant pigs. Uteroferrin, however, is but one member of what may be a broad class of iron-containing phosphatases with unusual spectral properties which result from a novel type of di-iron active site. The biological function of uteroferrin is unknown. We argue here that the in vivo function of uteroferrin, despite its undoubted ability to act as a potent acid phosphatase, is that of a transplacental iron transporter.     

The development of anoxia following occlusion

Following arteriolar occlusion, tissue oxygen concentration decreases and anoxic tissue eventually develops. Although anoxia first appears in the region most distal to the capillary at the venous end, it eventually spreads throughout the entire region of supply. In this paper the changing oxygen concentration, from the time of occlusion until the tissue is entirely anoxic, is examined mathematically. The equations governing oxygen transport to tissue are solved by iterating a nonlinear integral equation. This solution is valid until anoxia first appears. After anoxia develops it is necessary to solve a moving boundary problem. This is done using the method of matched asymptotic expansions, and accurate solutions are obtained for a wide range of physiological conditions.     

Metabolism of carbon tetrachloride to phosgene

Aerobic incubation of hepatic microsomal fractions in the presence of carbon tetrachloride, NADPH and cysteine resulted in the formation of phosgene which was identified by gas chromatography/mass spectrometry as the adduct, 2-oxothiazolidine-4-carboxylic acid, formed by its reaction with cysteine. [¹³C]-Carbon tetrachloride was metabolized to 2-[¹³C]-oxothiazolidine-4-carboxylic acid the , when carbon tetrachloride was incubated in the presence of [¹⁸O]-O₂, 2- [¹⁸O]-oxothiazolidine-4-carboxylic acid was formed. The reaction was inhibited by carbon monoxide showing the involvement of the cytochrome P-450-dependent mixed function oxidase system. The metabolism of carbon tetrachloride to phosgene may play a role in the production of hepatotoxicity by this compound.