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Biomedical subjects

M Schara

Publications and source records attributed to M Schara.

49 records · Page 3Linked to original sources
PubMed1982

Spin-labeled phorbol esters and their interaction with cellular membranes.

A series of homologous spin-labeled fatty acid analogs of the type 12-O-FASL (n,m)-phorbol-13-acetate [(n,m)PA] of 12-O-tetradecanoylphorbol-13-acetate (TPA) with variable chain length N of the fatty acid moiety and various positions of the nitroxide group were synthesized. Their irritant doses 50 (ID50) on the ear and their initiation-promoting activities on the back skin of NMRI mice were determined. The irritancy 1/ID50 of the (n,m)PA follows the simple linear relation ln(1/ID50) = alpha N + beta. In an "equilibrium" approach, the electron paramagnetic resonance (EPR) spectra measured in absence and in presence of erythrocytes (E) were used to determine the partition coefficients KM,0 between the erythrocyte membrane (M) and the extracellular solution (o). The KM,0 depend on the chain length N of the fatty acid moieties following the equation ln KM,0 = aN + b and show that the (n,m)PA are accumulated preferentially in the erythrocyte membrane. In a "kinetic" approach, the decay rate J(t)/J(o) of the EPR signal intensity of (n,m)PA molecules in absence and in presence of equilibrated E was measured during oxidation with ferricyanide and reduction with ascorbate, respectively. From the data obtained by the "kinetic" approach, a "two-compartmental model" is shown to be the most simple approximation to describe the system, in which finite concentrations of the (n,m)PA are postulated for the extracellular and the membrane compartment only. EPR data indicate that generally the (n,m)PA are buried with their acyl chain in the E membrane with the phorbol moiety close to the outer membrane surface. Apparently only in case of (1,12)PA is the acyl chain long enough to be anchored in the lipid layer of the membrane in a way similar to the tetradecanoyl residue of TPA. A possible relationship with biological activities is discussed.

Animals↗
PubMed1980

The caries resistance of human teeth is determined by the spatial arrangement of hydroxyapatite microcrystals in the enamel.

Teeth from different people differ in their susceptibility to caries. The beginning and the development of tooth decay depend on the presence of bacterial plaque and on the structure of the tooth enamel. But it has not been established whether the organic or the inorganic component of the enamel (which is comprised principally of hydroxyapatite microcrystals organized in a firm matrix), is responsible for most of the resistance of teeth to caries. We report here that the electron spin resonance (ESR) lines of the (CO3)3 defect of samples of enamel prepared from caries-resistant teeth differ significantly from the corresponding spectra of the caries-sensitive samples. We have traced these differences to the hydroxyapatite microcrystalline alignment in the tooth enamel, and found that this alignment is specific to individuals and is therefore probably nutritionally or genetically determined.

Crystallography↗
PubMed1976

An ESR study of the influence of some physico-chemical factors on the conformation of a postsynaptic acetylcholinesterase.

1. In a previous ESR study of a membrane acetylcholinesterase (EC 3.1.1.7) we found, contrary to observations by other authors, spectra indicating that the active serine might be located in a pocket of the enzyme surface. In order to inquire into this possibility, ESR spectra were studied under the influence of different physico-chemical factors known to cause an unfolding of proteins. 2. The active serine of the postsynaptic membrane acetylcholinesterase of Torpedo marmorata electric organ was spin labeled using 1-oxyl-2, 2, 6, 6-tetramethyl-4-piperidinyletoxyphosphonofluoridate. 3. The effect of the chosen physico-chemical factors was an increase in the rotational freedom of spin labels; this result corroborates the suggestion that the active center of our acetylcholinesterase preparation is located in a pocket.

Acetylcholinesterase↗
PubMedDate not supplied

Study of the arrangement of crystallites in gamma-irradiated human enamel by electron paramagnetic resonance.

The arrangement of tooth enamel microcrystals has been studied on CO3-3 bound electrons by electron paramagnetic resonance. It was found that noncarious human maxillary central incisors have a greater degree of alignment of tooth enamel microcrystals than the carious ones. The outermost surface layer of enamel showed a greater crystallite degree of alignment than other parts.

Crystallography↗
PubMedDate not supplied

Melatonin and oxidative damage in mice liver induced by the prooxidant antitumor drug, adriamycin.

Antioxidant properties have been attributed to melatonin; it seemed therefore worthwhile to determine its effects in relation to the prooxidant action of adriamycin, which contributes to its toxic and therapeutic effects. Melatonin effectively acts as a direct free radical scavenger in the concentration range of 20-100 microM as determined in vitro, using Fenton reaction as a source of free radicals that were determined by EPR using spin trapping method. Following the administration of a single i.v. dose of 28 mg/Kg or of 3 repeated i. p. doses of 5 mg/Kg adriamycin to CBA mice, glutathione levels in the liver cells were significantly reduced. When the treatment with adriamycin was preceded by the s.c. administration of 2 mg/Kg melatonin, the decrease in total and reduced glutathione concentrations was significantly prevented. A significant increase in lipid peroxidation was observed in liver cells after a single administration of adriamycin which was not attenuated by pretreatment with melatonin. These results indicate that further examination of the possible protective action of melatonin on the toxic effects of prooxidant antitumor drugs on normal and neoplastic tissues would be of interest also in relation to their chronotoxicological properties.

Animals↗