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Fibronectin — Mediator between cells and connective tissue

Fibronektin — Mittler zwischen Zellen und Bindegewebe

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Summary

Fibronectin, previously also termed LETS-protein, is a high-molecular-weight protein (mol. w. ca. 450,000) present in the form of thin fibrils in the pericellular space of fibroblasts and other adherent cells, as well as in distinct areas of the connective tissue. A soluble form, immunologically identical and chemically at least very similar to the cell-attached protein, is found in plasma in a concentration of about 300 µg/ml. It is also denominated cold-insoluble globulin. The protein has affinity both to cell surfaces and to various matrix substances such as fibrin and collagen and, therefore, is capable of mediating cell attachment to these substrates. In addition, it serves as an opsonin for the phagocytosis of gelatin-containing compounds and probably is essential for the removal of soluble fibrin from the circulating blood by the reticulo-endothelial system. Bacterial cell walls are also recognized by fibronectin.

A conversion of soluble fibronectin to fibrils is achieved by heparin which also enhances the binding of soluble fibronectin to cells. Heparin or, as suggested, the related heparansulfate present on the surface of various cells, appears to function as a cofactor in the formation of pericellular fibrils. The fibronectin fibrils precipitated with heparin, compared to soluble fibronectin, show a considerably improved affinity to native collagen, especially to type III. Hyaluronic acid has an antagonistic function which, at higher concentrations, prevents the fibronectin fibrils from interacting with collagen and cell surfaces. Masking of fibronectin fibrils was also achieved by sulfated proteoglycans of cartilage.

Virus-transformed fibroblasts produce less fibronectin and are less capable of maintaining surface pericellular fibrils. A reasonable explanation is that they have an elevated secretion of hyaluronic acid. The transformed cells attach only weakly to a surface and exhibit a rounded shape in contrast to healthy ones. This phenotype can be corrected to a great extent with fibronectin.

It is suggested that fibronectin also influences the formation of connective tissue by accumulating collagen precursors on the surface of fibroblasts and facilitating fibrillogenesis.

Zusammenfassung

Fibronektin, früher auch LETS-Protein genannt, ist ein hochmolekularer Eiweißkörper (Mol-Gew. ca. 450 000), welcher im perizellulären Bereich von Fibroblasten und anderen adhärenten Zellen aber auch sonst im Bindegewebe in Form dünner Fibrillen auftritt. Eine lösliche Form, die mit dem Oberflächenprotein der Zellen immunologisch identisch und chemisch zumindest sehr ähnlich ist, kommt im Blutplasma in einer Konzentration von etwa 300 µg/ml vor. Sie wird auch als Kälte-unlösliches Globulin bezeichnet. Fibronektin besitzt Affinität zu Zelloberflächen und zu verschiedenen Matrixsubstanzen wie Fibrin und Kollagen und vermittelt dadurch das Anhaften von Zellen an diese Substrate. Es wirkt außerdem als Opsonin für die Phagozytose gelatinehaltiger Verbindungen und ist vermutlich wichtig für die Ausschleusung von löslichem Fibrin aus dem Blutkreislauf durch das retikulo-endotheliale System. Auch Bakterienoberflächen werden von Fibronektin erkannt.

Eine Umwandlung von löslichem Fibronektin in Fibrillen gelingt mit Heparin, das gleichzeitig die Bindung von löslichem Fibronektin an die Zellen verstärkt. Heparin oder, wie vermutet wird, das an Oberflächen verschiedener Zellen vorhandene Heparansulfat scheinen somit als Cofaktoren für die Ausbildung der perizellulären Fibrillen wesentlich zu sein. Die mit Heparin abgeschiedenen Fibronektinfibrillen weisen auch eine bessere Affinität zu nativem Kollagen, besonders zu Typ III, auf als lösliches Fibronektin. Als Antagonist wirkt Hyaluronsäure, die in höheren Konzentrationen die Wechselwirkung der Fibronektinfibrillen mit Kollagen und Zelloberflächen verhindert. Auch sulfatierte Proteoglykane aus Knorpelgewebe maskieren Fibronektinfibrillen.

Virus-transformierte Fibroblasten erzeugen weniger Fibronektin und vermögen perizelluläre Fibrillen nur schlecht festzuhalten. Eine Erklärung dafür könnte die erhöhte Abscheidung von Hyaluronsäure sein. Die transformierten Zellen haften nur schlecht an einer Unterlage und weisen im Gegensatz zu gesunden eine runde Form auf. Dieser Phänotyp kann durch Fibronektin zum größten Teil korrigiert werden.

Es wird vermutet, daß Fibronektin auch auf die Bildung von Bindegewebe Einfluß nimmt, indem es kollagene Vorstufen an der Oberfläche von Fibroblasten akkumuliert und dadurch die Fibrillogenese beeinflußt.

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  1. Max Planck-Institut für Biochemie, Martinsried bei München, Germany

    Helmut Hörmann

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  1. Helmut Hörmann
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Hörmann, H. Fibronectin — Mediator between cells and connective tissue. Klin Wochenschr 60, 1265–1277 (1982). https://doi.org/10.1007/BF01727483

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  • DOI: https://doi.org/10.1007/BF01727483

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