Concentration of monoamines in the brain of minks differing in their reaction to man

Content of dopamine in the striatum; of serotonin, 5-hydroxyindolacetic acid and noradrenaline in the hypothalamus, striatum and midbrain was studied in three groups of minks from population of an animal farm, differing by their reaction to humans (cowardly, calm, aggressive). The reaction to humans was estimated by a system of marks at the attempt to catch the mink with a mitten. Aggressive animals had a lowered level of serotonin in the hypothalamus and striatum, a lesser content of serotonin metabolite--5-hydroxyindolacetic acid in the striatum. Minks of different groups did not differ by noradrenaline content, but dopamine level in the striatum of cowardly minks was higher than in calm and aggressive animals. Conclusion is made that polymorphism of behaviour corresponds to polymorphism of the state of monoaminergic systems.     

Inhibition of benzoyl peroxide/Cu2+-dependent lipid peroxidation by manganese

1. Formation of peroxides by benxoyl peroxide (BPO) and CuCl2 was examined in the human red blood cell ghost. 2. Amounts of peroxides formed increased with the amount of the ghost solution added. 3. Of all the cations tested only manganese ion inhibited the formation of peroxides in BPO-CuCl2 reaction system. 4. The formation of peroxides was inhibited approx. 50% with 0.4 microM manganese. 5. The inhibitory manner of manganese was non-competitive against copper.     

Changes in the amino acid sequence of hemagglutinin during sequential adaptation of human influenza virus A to replication in mice

The primary structure of hemagglutinin (HA) gene of Influenza virus A/USSR/90/77 (H1N1) variants after 3 and 11 passages has been determined. In the HA1 coding region of mice-adapted virus (11 passages) there are two amino acid substitutions: Thr 89----Ala and Asn 127----Asp. At the first stage of adaptation (3-rd passage) only a single mutation was detected: Asn 127----Asp. The adaptation is accompanied by the loss of specific carbohydrate attachment sites adjacent to the receptor-binding site located at HA1 subunit with a concomitant variation in antigenicity.     

Non-marine Teredolites from the Middle Eocene of southern England

Middle Eocene, non-marine sediments from southern England contain examples of Teredolites borings in two contrasting palaeoenvironmental settings, viz.: (A) as in situ borings in an allochthonous lignite in an abandoned river channel and (B) as bored logs in cross-bedded fluvial sandstones of probable point-bar origin. The lignite is 0.30 m thick, of which the upper 0.20 m is intensely bored. Rounded pebbles of ?charcoal at its base also show small borings. A log in a fluvial sandstone shows densely-packed. radial club-shaped borings. now filled with sandstone. The wood substrate has subsequently been oxidized away. To our knowledge, this is the first detailed account of Teredolites from an ancient freshwater setting.     

Synergism among lysophosphatidic acid, beta1A integrins, and epidermal growth factor or platelet-derived growth factor in mediation of cell migration.

GD25 cells lacking the beta1 integrin subunit or expressing beta1A with certain cytoplasmic mutations have poor directed cell migration to platelet-derived growth factor (PDGF) or epidermal growth factor (EGF), ligands of receptor tyrosine kinases, or to lysophosphatidic acid (LPA), a ligand of G-protein-coupled receptors (Sakai, T., Zhang, Q., F?ssler, R., and Mosher, D. F. (1998) J. Cell Biol. 141, 527-538 and Sakai, T., Peyruchaud, O., F?ssler, R., and Mosher, D. F. (1998) J. Biol. Chem. 273, 19378-19382). We demonstrate here that LPA synergizes with signals induced by beta1A integrins and ligated EGF or PDGF receptors to modulate migration. When LPA was mixed with EGF or PDGF, migration was greater than with EGF or PDGF alone. The enhancement was greater for beta1A-expressing cells than for beta1-null cells. Cells expressing beta1A with mutations of prolines or tyrosines in conserved cytoplasmic NPXY motifs had blunted migratory responses to mixtures of LPA and EGF or PDGF. The major effects on beta1A-expressing cells of LPA when combined with EGF or PDGF were to sensitize cells so that maximal responses were obtained with >10-fold lower concentrations of growth factor and increase the chemokinetic component of migration. Sensitization by LPA was lost when cells were preincubated with pertussis toxin or C3 exotransferase. There was no evidence for transactivation or sensitization of receptors for EGF or PDGF by LPA. EGF or PDGF and LPA caused activation of mitogen-activated protein kinase by pertussis toxin-insensitive and -sensitive pathways respectively, but activation was not additive. These findings indicate that signaling pathways initiated by the cytoplasmic domains of ligated beta1A integrins and tyrosine kinase receptors interact with signaling pathways initiated by LPA to facilitate directed cell migration.     

A comparison of the actions of trypsin and pepsin on porcine immunoglobulin M and their effects on biological activity

The action of trypsin at 55 degree C and pH 8.3 on pig IgM anti-Salmonella has been compared with the action of pepsin at 37 degree C and pH 4.6. Both processes cause the gradual removal of Fab arms and Cmu2 domains to produce eventually an (Fc)5 fragment. However, during tryptic digestion Fab arms are preferentially removed from the same subunit, whereas peptic digestion causes random removal from any subunit. At intermediate stages of digestion both processes produce partially fragmented molecules which consist of an (Fc)5 portion still attached to limited numbers of Fab arms. Both processes cause a gradual decrease in the ability of molecules to agglutinate Salmonella, but complement fixation by the complexes declines much more rapidly. A stage is reached where molecules having four Fab arms can still agglutinate but there is no complement fixation. However, the remaining arms on the tryptic molecules are distributed in pairs on the same subunit, whereas those on the peptic molecules are distributed randomly. Hence the number of remaining Fab arms, rather than their distribution, appears to be the critical factor which influences biological activity. A possible explanation for this is discussed.