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Biomedical subjects

M Adam

Publications and source records attributed to M Adam.

At least 199 records · Page 11Linked to original sources
PubMed1980

Contribution to the mode of action of glycosaminoglycan-polysulphate (GAGPS) upon human osteoarthrotic cartilage. Biochemical study of the collagen and proteoglycan turnover.

The effect of glycosaminoglycan polysulphate (GAGPS) upon the metabolism of proteoglycan (PG) and collagen in chick embryos and human cartilage was studied. GAGPS treatment caused an accumulation of studied compounds. According to the results with osteoarthrotic cartilages the marked increase of radioactivity in collagen and PG (mainly in the fraction containing glycoprotein link) is due to the inhibition of catabolic processes.

Animals↗
PubMed1979

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↗
PubMed1979

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↗
PubMed1979

The treatment of postperfusion bleeding using epsilon-aminocaproic acid, cryoprecipitate, fresh-frozen plasma, and protamine sulfate.

The evaluation of excessive hemorrhage was carried out in 774 patients after cardiopulmonary bypass. Excessive hemorrhage was defined in any adult patient as chest tube drainage of more than 600 ml within the first eight hours after operation. Using the prothrombin time, partial thromboplastin time, fibrinogen level, and tri-F titer tests, it was possible to differentiate medical from surgical bleeding. Hyperfibrinolytic bleeding was the most frequently identifiable coagulation disorder and occurred in 159 patients (20%). All these patients were successfully treated with Amicar (epsilon-aminocaproic acid) alone, or with Amicar supplemented with cryoprecipitate or fresh-frozen plasma. Three patients (0.4%) were noted to have residual heparin and required additional protamine sulfate. Five patients (0.6%) had normal coagulation studies and required immediate reexploration. The overall blood consumption per patient was 2.1 units of packed cells. Whole blood and platelets were not used.

Aminocaproates↗
PubMed1979

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↗
PubMed1979

Cartilage and osteoarthrosis: changes of collagen and proteoglycans.

The authors discuss changes of proteoglycans and collagen in osteoarthrotic cartilage, based on their own results. During osteoarthrosis the proteoglycan molecule diminishes in size, mainly due to a diminution of the carbohydrate portion. The diminution of binding glycoprotein leads to changes in the interaction with hyaluronic acid. Collagen is more soluble and has a reduced resistance to proteolytic enzymes. In the osteoarthrotic cartilage also collagen type I and III is present.

Carbohydrate Metabolism↗
PubMed1978

Effect of cartilage bone-marrow extract on articular cartilage collagen formation.

Cartilage bone-marrow extract has stimulated the collagen formation of articular as well as sternal cartilage collagen in chick embryo. Collagen biosynthesis has been stimulated also in other investigated tissues, i.e. in cornea and sclera of chick embryo as well as in sponge granuloma of rats, where mainly formation of collagen type I was stimulated. Glycosaminoglycans formation has also been increased after administration of cartilage bone-marrow extract.

Animals↗
PubMed1977

Treatment of severe coronary artery disease with 5, 6, and 7 saphenous vein bypasses: review of 131 consecutive patients.

One hundred thirty-one consecutive patients who received 5, 6, and 7 bypass grafts are analyzed. Ages ranged from 31 to 74 years. The male-to-female ratio was 7:1. As an indication of severity of disease, 25% were classified as having impending myocardial infarction and 46.6% were classified in New York Heart Association Functional Class IV. Left ventricular function was impaired in 37.4%, and 30% of the patients had left main coronary obstruction. Nonfatal perioperative myocardial infarction occurred in 4.6%. The hospital mortality was 3%. One hundred percent follow-up (5 to 55 months) revealed 4 late deaths, 3 presumably of cardiac origin. Only 7 patients in the postoperative follow-up group have complained of angina; 1 has since undergone successful reoperation.

Adult↗
PubMed1977

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↗