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Lipid-Protein-Wechselwirkungen menschlicher Apolipoproteine — Entwicklung von Lipoprotein-Modellen

Lipid-protein-interactions of human apolipoproteins—structural aspects and models of lipoproteins

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Summary

The plasma lipoproteins are complex macromolecular structures which play an essential role in fat transport and in energy and membrane metabolism of higher organized organisms. Much has been learned in the last decade about the structural and functional interrelationships of the different lipoprotein classes. Their protein moieties, the so-called apolipoproteins, have been purified and characterized, the primary structure of four of them is known. Initial recombination experiments showed a considerable potential of the (unfractionated) lipoprotein protein to bind to lipids and to form particles similar to native lipoproteins. Further binding experiments performed in several laboratories with the purified A- and C-apolipoproteins and different physico-chemically well defined lipids have lead to the identification of lipid binding sites within the protein molecules and the formation of amphipathic helices upon and during lipid binding. This possible common mechanism of lipid-protein fractions forms the basis of a recently proposed model of one lipoprotein class, namely the high density lipoproteins (HDL). The significance of protein-protein-interactions in the formation and maintenance of these lipoprotein particles is still unknown. Whether disturbed lipid protein interactions lead to structural and/or functional alterations of the corresponding lipoproteins is a topic of discussion. The pertinent literature is listed in this paper and the physiological relevance of these studies and their clinical aspects will be presented.

Zusammenfassung

Die menschlichen Plasmalipoproteine sind komplexe makromolekulare Strukturen, die eine entscheidende Rolle im Fettransport und im Energie- und Membranstoffwechsel tierischer Organismen spielen. Die strukturellen und funktionellen Wechselbeziehungen zwischen den einzelnen Lipoproteinklassen sind in den letzten Jahren eingehend untersucht worden. Ihre Proteinbestandteile, die sog. Apolipoproteine, konnten gereinigt und charakterisiert werden; die Primärstruktur von vier von ihnen ist bekannt. Erste Rekombinationsstudien deuteten darauf hin, daß das (unfraktionierte) Apoprotein ein beachtliches Lipid-Bindungsvermögen besitzt und daß dabei Partikel gebildet werden, die den nativen Lipoproteinen ähnlich sind. Spätere Bindungsexperimente, die in einer Reihe von Laboratorien mit den gereinigten A- und C-Apolipoproteinen und verschiedenen, physiko-chemisch gut definierten Lipiden durchgeführt wurden, haben zur Identifizierung von sog. Lipidbindungsstellen (lipid binding sites) innerhalb der Proteinmoleküle geführt. Bei und während der Wechselwirkung mit dem Lipid bilden sich dadurch sog. amphipathische Helices aus. Dieser für alle Apolipoproteine möglicherweise gleichermaßen gültige Mechanismus einer Lipid-Protein-Wechselwirkung bildet die Grundlage eines kürzlich vorgeschlagenen Modells einer der Lipoproteinklassen, nämlich der high density Lipoproteine (HDL). Die Bedeutung von Protein-Protein-Wechselwirkungen für die Bildung und Stabilisierung der Lipoproteine ist noch unbekannt. Ob eine Störung der Lipid-Protein-Wechselwirkungen zu strukturellen und/oder funktionellen Änderungen der entsprechenden Lipoproteine führen kann, wird noch diskutiert. Ob entsprechende Defekte zur Entstehung einer Hyperlipoproteinämie beitragen können, ist ebenfalls noch offen. Die einschlägige Literatur wird in der vorliegenden Arbeit besprochen, und die Fragen der physiologischen Relevanz dieser Studien und ihrer klinischen Aspekte werden diskutiert.

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  1. Klinisches Institut für Herzinfarktforschung an der Medizinischen Universitätsklinik Heidelberg, Germany

    G. Middelhoff, J. Augustin, G. Klose & H. Greten

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  1. G. Middelhoff
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  2. J. Augustin
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  3. G. Klose
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Middelhoff, G., Augustin, J., Klose, G. et al. Lipid-Protein-Wechselwirkungen menschlicher Apolipoproteine — Entwicklung von Lipoprotein-Modellen. Klin Wochenschr 55, 149–160 (1977). https://doi.org/10.1007/BF01469135

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