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Biomedical subjects

E Bańkowski

Publications and source records attributed to E Bańkowski.

At least 19 recordsLinked to original sources
PubMed1992

Pharmacological and physicochemical properties of collagen breakdown-products.

It has been found that the pharmacologically active, low molecular products obtained by digestion of telopeptides-deprived type I collagen with bacterial collagenase is a heterogenous mixture of at least 21 peptides of different molecular weight. They contain 3 to 15 amino acid residues. About 80% of them are tripeptides of the sequence Gly-Pro-X. The most abundant are two peptides: Gly-Pro-Hyp and Gly-Pro-Ala. The peptides injected into the lateral cerebral ventricle of the rat evoked some behavioral effects. They decreased the psychomotoric activity (evaluated with Lat's test) and increased the cataleptic action of haloperidol. On the other hand, they did not exert any effect on amphetamine-induced stereotypy and did not counteract the apomorphine-induced stereotypy.

Amino Acid Sequence↗
PubMed1992

[Content and distribution of collagen in aorta double velour DALLON grafts].

The aim of the study was to determine the collagen content, distribution and quantitative ratios between main types of collagen (found in normal vascular walls) in various layers of double velour DALLON grafts at different periods after implantation. Double velour DALLON prostheses were implanted into the abdominal aorta of 24 dogs. These grafts were excised 7 days, 1, 4 and 12 months after implantation and together with normal arteries, after dissection into intimal, medial, and adventitial layers, tested for their hydroxyproline content. Type I, III, V collagen was also determined (fractionation of pepsin digestion products). Already 7 days after implantation collagen appeared in all the newly-formed layers of the grafts. With the passage of time after the operation collagen content was gradually increasing. After 12 months collagen content in the intimal and adventitial layers was significantly higher than in normal arterial wall. Approximate quantitative ratio between collagen types I, III and V in all graft layers was 7:2:1 and did not change during the 1-year-observation. Rise in collagen content results in graft wall stiffening, and the presence of III type collagen increased platelet-aggregating activity. Both these factors created a tendency to the formation of thrombosis in the graft.

Animals↗
PubMed1991

Chronic intoxication with acetaldehyde stimulates collagen biosynthesis in rat liver.

It was found that chronic intoxication of rats with acetaldehyde results in a distinct, progressive increase of 5(3)H-proline incorporation into collagen synthesized by liver. At the same time, biosynthesis of other proline-containing (noncollagenous) proteins does not change significantly. The effects are similar to those induced by chronic intoxication of rats with ethanol. Since acetaldehyde is an intermediary metabolite formed during ethanol oxidation in liver, it may be concluded that acetaldehyde is a factor responsible for alcohol-induced liver fibrosis.

Acetaldehyde↗
PubMed1991

Proteolytic activity of vitreous-humour.

It has been found that the bovine vitreous--humour did not digest in vitro collagen at physiological and acidic pH. A proteolytic activity against haemoglobin in acid pH was found both in bovine and human vitreous-humours. The activity of human vitreous-humour increased significantly in endophtalmitis and glaucoma. In all pathological conditions studied the pH optima were at more acidic values than in control.

Animals↗
PubMed1991

Collagenolytic activity of methylcholanthrene-induced rat fibrosarcoma.

It has been found that the methylcholanthrene-induced rat fibrosarcoma contains an enzyme (probably a cathepsin) which digests type I and type III collagens in acid pH. At physiological pH no proteolytic activity against collagen was found. It may be concluded that the tumour collagen is degraded mainly by the action of cathepsin(s).

Animals↗
PubMed1991

Collagen of breast with benign dysplasia.

Benign dysplasia is a pathological process in the female breast associated with hypertrophy of interlobular and periductal connective tissue. It leads to disappearance of the lobular structure of this organ. It was found that the mammary tumours contain more collagen in comparison to the normal breast. In the normal breast collagen type I and type III constitute 70% and 25% of the total collagen content, respectively. The investigated tumors contain mainly a complex of collagen type I and type III which cannot be dissociated by the methods used for collagen preparation.

Adult↗
PubMed1990

Effect of lathyrogen on collagen of methylcholanthrene-induced sarcoma of rat.

Since the lathyrogen beta-aminopropionitrile is known to affect the fibrogenic and physical properties of collagen polymers, we have examined its effects on collagenous components of methylcholanthrene-induced fibrosarcoma in rat. Lathyrogen treatment reduced total collagen content of tumours from approximately 17 to 12 mg collagen/g tissue. It also proportionately increased the solubility of specific collagen fractions, the summation of all extractable solubilized collagens reflecting 37 and 67% of total collagen content for control and lathyric tumours, respectively. Although lathyrogen had no significant effect on the growth and overall size of fibrosarcoma, histological studies confirmed that changes had occurred to appearance and distribution of collagenous components of extracellular matrix.

Aminopropionitrile↗
PubMed1978

Collagen-bound glycoprotein of Guerin epithelioma.

The polymeric collagen of Guerin epithelioma is strongly bound to a large amount of noncollagenous substance. Almost full dissociation of this complex was achieved by heating in 7 Murea, at 100 degrees C for 4 hours. The collagen bound substance was identified as an acidic glycoprotein containing glucose, galactose, glucosamine, galactosamine and M-acetylneuraminic acid. Heterogeneity of this substance in regard to molecular weight was found.

Amino Acids↗
PubMed1977

Proteolysis of procollagen I.

1. Digestion of procollagen I which trypsin, pepsin or pronase performed at 20 degrees C causes the release of acidic non-collagenous fragments and hydroxyproline-rich fraction. Enzymatic proteolysis performed at 41 degrees C (above the temperature of denaturation) results in degradation of procollagen I to low-molecular peptides. 2. The hydroxyproline-rich fraction obtained by limited proteolysis of procollagen I with pepsin (at 20 degrees C) contains a material corresponding to alpha and beta subunits of tropocollagen. Reduction of the hydroxyproline-rich fraction released by trypsin or pronase (at 20 degrees C) causes the appearance of polypeptides similar to pro-alpha subunits.

Molecular Weight↗