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Biomedical subjects

J Kempf

Publications and source records attributed to J Kempf.

81 records · Page 5Linked to original sources
PubMedDate not supplied

Endogenous activation by indirect muta-carcinogens and DNA-repair synthesis in mouse-lung fibroblast cultures.

Cultures of adult mouse-lung fibroblasts have been treated by series of strong and weak muta-carcinogens. Unscheduled DNA synthesis has been measured by quantitative autoradiography using automatic image analysis. Some of the muta-carcinogens (AFB1, DMN, B(a)P, DMBA, MNNG, 4-NQO) yielded a measurable UDS response, whereas others (2-AA, AFB2, B(e)P, ICR-191) usually known as weak carcinogens, gave no response. The response was not improved by addition of liver S9. This shows that mouse-lung fibroblasts possess their own but limited metabolic activation systems.

Animals↗
PubMedDate not supplied

Influence of mouse genotype on responses of central cholinergic neurotransmission to long term alcohol intoxication.

Cholinergic neurotransmission has been followed in striatum and hippocampus in two inbred strains of mice (C57Bl/6 and Balb/c) during long term alcohol exposure (over a 25 month period) and with aging. Marked strain dependent differences in reactivity of pre- and postsynaptic cholinergic markers to chronic alcohol exposure and aging were demonstrated in both structures. The Balb/c strain exhibits a remarkable long lasting tolerance to alcohol injury for striatal and hippocampal cholinergic markers (choline acetyltransferase, high affinity choline uptake, muscarinic receptors affinity, acetyl cholinesterase), whereas C57Bl mice appear more sensitive to alcohol intoxication. Likewise aging affects the C57Bl mouse more severely than the Balb/c, a phenomenon which may be involved in the sensitivity of these mice to alcohol intoxication. Moreover long term alcohol exposure, in addition to aging show unequal effects on the diverse cholinergic markers studied. Also divergences of specific brain areas have been noted and should be related to their particular neuroanatomy. Such discrepancies may, in part, explain differences observed in the behavioral effects of chronic alcohol intoxication in alcoholics.

Acetylcholinesterase↗
PubMedDate not supplied

Influence of mouse genotype on responses of central biogenic amines to alcohol intoxication and aging.

Dopamine and serotonin responses to various periods of alcohol treatment have been followed in striatum and hippocampus of two inbred strains of mice and related to the effect of aging. A striking strain dependency was noted for chronic alcohol effects and also for senescence. For both neurotransmitters studied the C57Bl strain loses tolerance to prolonged alcohol injury earlier than the Balb/c strain. This loss of tolerance accompanying aging may be indicative of more widespread changes in CNS adaptability in this strain. The unequal capacity to adapt also appears to depend on the nervous structure and the neurotransmitter considered. Alcohol and aging induced changes are not identical. In a given mouse strain, significant effects of either drug or aging induced disturbances are noted. A similar molecular process could operate in both aging and alcohol abuse, but the neurochemical effect might depend on the nervous structure or neurotransmitter involved. Such a phenomenon may be the basis of differences in behavioral changes observed in alcoholics.

Aging↗
PubMedDate not supplied

Reduced benzo-a-pyrene activation potential in lymphocytes from chronic alcoholics.

The effect of chronic ethanol consumption on the cellular metabolism of benzo-a-pyrene (BaP) is investigated in human peripheral lymphocytes obtained from 6 proven alcoholic addicts and 5 healthy donors. Lymphocytes convert BaP to dihydrodiols, diol-epoxides, phenols, quinone derivatives and polyhydroxylated forms. Sulfate, glucuronide and glutathione conjugates are also detected. The average production of metabolites is much lower in lymphocytes of alcoholics and a net global decrease of "active" metabolite production, i.e., diols and BPDE, is also observed. In contrast, conjugated metabolites are formed in increased amounts. The data indicate that the metabolism of BaP in lymphocytes from chronic alcoholics is characterized essentially by a lowered rate of metabolized BaP and a reduction of their BaP activation potential, as seen by the increased production of conjugated metabolites and the markedly decreased protein-bound active mutagen.

7,8-Dihydro-7,8-dihydroxybenzo(a)pyrene 9,10-oxide↗
PubMedDate not supplied

Adenosine diphosphate ribosyltransferase and protein acceptors associated with cytoplasmic free messenger ribonucleoprotein particles.

ADP-ribosyltransferase activity has been characterized in free messenger ribonucleoprotein particles (mRNP) from mouse plasmacytoma cells. This enzymatic activity appears to be associated with the free mRNP and not due to nuclear contamination. The enzyme activity is not stimulated by added DNA or histone H1 and represents 34 per cent of the total cellular ADP-ribosyltransferase activity while the DNA contamination in free mRNP is less than 4 per cent of the total cellular DNA. Moreover, the ADP-ribosyltransferase specific activity per mg of DNA is about 75-fold higher in free mRNP than in the nuclei. During CsCl gradient centrifugation of the cytoplasmic fraction, the ADP-ribosylated material separates out at a buoyant density similar to that of free mRNP. This ADP-ribosyltransferase activity is inhibited by thymidine, nicotinamide and 3-aminobenzamide, while it is highly stimulated by exogenous pancreatic RNase. The in vitro synthesized acid insoluble material is rendered partly soluble by treatment by a proteolytic enzyme or by snake venom phosphodiesterase resulting in phosphoribosyl-AMP formation: the pancreatic RNase does not solubilize this material. Several ADP-ribosylated proteins are detected by lithium dodecylsulfate gel electrophoresis. Such an ADP-ribosyltransferase activity has also been detected in free mRNP from rat liver. It is suggested that this ADP-ribosylation of specific free mRNP proteins may be associated with free mRNP structure and/or with some chemical covalent type of modification rendering mRNA available for translation.

Adenosine Diphosphate Ribose↗