Summary
Left ventricular collagen of various mammals (cat, cow, dog, pig, and rat) was successively extracted with neutral salt, and dilute acid solutions, and limited pepsin digestion. The distribution of the various types of collagen molecules in pepsin-solubilized ventricular collagen was analyzed electrophoretically on SDS-polyacrylamide gels in the presence of 3.6 M urea.
Yields of dilute-acid-soluble collagen were only 0.4 to 0.6% of the total ventricular collagen, and less than 0.1% with neutral salt solution. Approx. 55–90% of the total collagen was extracted by limited pepsin digestion.
Disc patterns of pepsin-soluble collagen revealed the presence of dimeric and trimeric components, as well as higher-molecular-weight aggregates in all samples of nonreduced and reduced ventricular collagen. Taken together, these findings suggest the presence of an extensive interchain and intermolecular cross-linking network in left ventricular collagen.
Comparison of electrophoretical disc gel patterns of reduced and nonreduced pepsin-solubilized collagen indicated that left ventricular collagen is heterogenous in nature, consisting of a mixture of type I and type III collagen. It was evident that primarily type I components occur in ventricular collagen. The components of type III collagen molecules occurred in all investigated left ventricles in varying and consistently appreciably lower amounts. The proportions of type III and type I collagen vary in left ventricular tissue of different species.
Zusammenfassung
Kollagen aus dem linken Ventrikel verschiedener Säugetiere (Katze, Kuh, Hund, Schwein und Ratte) wurde sukzessiv mit neutraler Salz- und verdünnten Säurelösungen sowie mit limitierter Pepsinverdauung extrahiert.
Die Verteilung verschiedener Kollagentypen in pepsingelöstem Kollagen wurde mit Hilfe der SDS-Plyacrylamid-Gel-Elektrophorese analysiert.
Mit Salz- und Säurelösungen ließ sich weniger als 1% des Gesamtkollagens extrahieren. Begrenzte Pepsinverdauung löste 55–90% des Gesamtkollagens.
Von allen Proben des nichtreduzierten und reduzierten Kollagens wurden in Elektrophorese-Gelen di- und trimere Komponenten sowie auch hochmolekulare Aggregate von Kollagenmolekülen sichtbar. Diese Befunde weisen auf eine umfangreiche intra- und intermolekulare Vernetzung der Kollagenmoleküle im linken Ventrikel der Säugetiere hin.
Der Vergleich von Proteinbanden in Elektrophorese-Gelen von nichtreduziertem und reduziertem Kollagen zeigt, daß Kollagen vom linken Ventrikel heterogen ist, bestehend aus einem Gemisch von Kollagentyp I und-typ III. Vorwiegend ist Kollagentyp I vertreten. Komponenten vom Typ III kommen in allen untersuchten Proben vor, jedoch in unterschiedlichen und erheblich kleineren Proportionen.
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Medugorac, I. Characterization of intramuscular collagen in the mammalian left ventricle. Basic Res Cardiol 77, 589–598 (1982). https://doi.org/10.1007/BF01908312
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DOI: https://doi.org/10.1007/BF01908312