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Some structural differentiations in the HeLa cell: heavy bodies, annulate lamellae and cotte de maillet endoplasmic reticulum

Zitieren Sie bitte immer diese URN: urn:nbn:de:bvb:20-opus-40614
  • A small fraction of HeLa cells within an exponentially growing culture showed cisternal differentiations, such as cytoplasmic as well as intranuclear annulate lamellae and special smooth surfaced endoplasmic reticulum aggregates with a typical "Cotte de maillet" appearance. Additionally, clusters of dense granules were observed in the cytoplasm which were often associated with polysomes and strongly resembled the so-called "heavy bodies" known in particular in diverse oocytes. The functional meaning of these structures is discussed. Moreover,A small fraction of HeLa cells within an exponentially growing culture showed cisternal differentiations, such as cytoplasmic as well as intranuclear annulate lamellae and special smooth surfaced endoplasmic reticulum aggregates with a typical "Cotte de maillet" appearance. Additionally, clusters of dense granules were observed in the cytoplasm which were often associated with polysomes and strongly resembled the so-called "heavy bodies" known in particular in diverse oocytes. The functional meaning of these structures is discussed. Moreover, it is deduced from the ultrastructural identity of the pore complexes in the nuclear envelope and the cytoplasmic and intranuclear annulate lamellae that the pore complex material with its highly ordered arrangement is not a structure characteristic for nucleocytoplasmically migrating material, but rather is a general structural expression of a tight binding of ribonucleoprotein (RNP) to cisternal membranes. The pore complexes are thought of as representing sites of a RNP-storage. A similar functioning is hypothesized for the "heavy body"like aggregates. To the current hypotheses on the formation of annulate lamellae and the nuclear envelope, which are based on the concept of membrane continuities and constancies, the alternative view of a self assembly mechanism of membrane constituents on nucleoprotein structures is added.zeige mehrzeige weniger

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Metadaten
Autor(en): Werner W. Franke, Ulrich Scheer
URN:urn:nbn:de:bvb:20-opus-40614
Dokumentart:Artikel / Aufsatz in einer Zeitschrift
Institute der Universität:Fakultät für Biologie / Theodor-Boveri-Institut für Biowissenschaften
Sprache der Veröffentlichung:Englisch
Erscheinungsjahr:1971
Originalveröffentlichung / Quelle:In: Cytobiologie (1971) 4, 2, 317-329.
Allgemeine fachliche Zuordnung (DDC-Klassifikation):5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Normierte Schlagworte (GND):Cytologie
Datum der Freischaltung:14.01.2010