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Biomedical subjects

Z Deyl

Publications and source records attributed to Z Deyl.

At least 127 records · Page 7Linked to original sources

The presence of gamma-carboxyglutamic acid-containing protein in atheromatous aortae.

It has been established that a gamma-carboxyglutamic acid-containing protein is present in rat aortae after long term atherogenic diet administration. A similar protein was proven to be present in turkey tibial tendons that are predisposed to undergo physiological calcification. The molecular weight and amino acid composition of both proteins were identical. They contained six glutamic acid residues per molecule, three of which were gamma-carboxylated. The proteins studied were also identical in their N-terminal sequence over six residues. This sequence was fully coincident with that published for osteocalcin (Price, P.A., Poser, J.W. and Raman, N. (1976) Proc. Natl. Acad. Sci. U.S.A. 73, 3374--3375). In the region corresponding to residues 20--26 in osteocalcin, a single replacement of valine for isoleucine was found in turkey tendon protein. From the physiological point of view it should be mentioned that the level of the gamma-carboxyglutamic acid containing protein in atherogenic diet fet rat aortae exceeds that found normally in bone or in tissues predisposed for physiological calcification.

1-Carboxyglutamic Acid↗

Ways of collagen separation in pathologically altered tissue.

A system of chromatographic methods using two successive DEAE-cellulose chromatographic steps and two successive separations on Bio-Gel A-1.5 m has been worked out for the separation of individual collagen types. The success of the procedure is based on the preliminary removal of proteoglycans during the first DEAE-cellulose run. Alternatively it is possible to replace chromatographic steps, following the removal of proteoglycans, with fraction precipitation.

Chromatography, Agarose↗

Collagen heterogeneity in systemic scleroderma and other diseases.

Proportions of collagen type I and type III were investigated in different tissues (kidney, liver, heart muscle, esophagus, lung and skin) in a single case of malignant systemic scleroderma. The proportion of collagen type III was higher than in healthy controls. Similarly, an increase in the proportion of collagen type III was shown in tissues affected by other inflammatory diseases. Further the authors suggest that the increase in total kidney collagen, especially type III, has important consequences for kidney function; in the described case it had the critical influence on the fatal course of the disease, and the patient died from uremia.

Adult↗

Properties of insoluble collagen from three different types of muscles.

1. Lyotropic solubilization of insoluble collagen from heart, M. longissimus dorsi and M. semimembranosus offers differently polymerized structures. In M. semimembranosus and in heart muscle the degree of polymerization is the highest, whilst in the solubilized portion of M. longissimus dorsi considerable proportions of alpha-and beta-chains can be observed. 2. All the polymeric structures can be broken down by pepsin and dithiothreitol treatment. 3. The proportion of collagen type I to III varies in different muscles. Collagen type I constitutes a considerable portion of the collagenous core in M. longissimus dorsi and in heart muscle, whilst in M. semimembranosus the predominating type is collagen type III.

Animals↗

Investigation on the reaction of molybdenum with collagen in vivo.

Male Wistar rats were treated with Mo in a single dose or over a period of 84 days. The course of molybdenum excretion after a single dose was expressed mathematically. It was shown that various tissues produced different excretion curves and a high retention was observed only in skin. In long-term treatment it was possible to ascribe this retention to direct binding of molybdenum to collagen. In contrast to some other heavy metals molybdenum causes a decrease of collagen stability. The mechanism of this effect is discussed.

Animals↗

Rheumatoid arthritis and collagen antibodies.

By using the complement fixation test, antibodies against collagen were examined. Pronase-solubilized insouble collagen served as antigen (20 degrees, 24 hours, collagen: enzyme ratio 10:1). Of 79 patients suffering from rheumatoid arthritis, the presence of collagen antibodies was demonstrated in 8 cases. 56 patients with degenerative joint disease served as the control group, in which collagen antibodies were detected in only one single patient.

Animals↗

The occurence of collagen type II in bronchogenic carcinoma.

It has been evidenced in a single case of bronchogenic carcinoma, that the proportion of collagen type II is increased in the diseased tissue. During the experimental work the collagenous stroma was isolated, subjected to cyanogen bromide cleavage and the relative proportion of individual types of collagen was judged according to the occurence of alpha1(I)CB3 and alpha1 (II)CB3 peptides. The nature of these peptides was proved by the chromatographic behavior during CM-cellulose chromatography, Ultrogel AcA 54 separation and by their amino acid composition.

Amino Acids↗