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The organization of tissues of the eye by different collagen types

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Albrecht von Graefes Archiv für klinische und experimentelle Ophthalmologie Aims and scope Submit manuscript

Summary

Bovine cornea, sclera, iris, ciliary body, choroid, zonular fibers, lens capsule, lens nucleus, vitreous body, and retina were investigated for collagen content and type.

Cornea, sclera, iris, ciliary body, choroid, lens capsule, and vitreous body contain hydroxyproline, whereas in zonular fibers, lens nucleus, and retina no hydroxyproline was detectable.

Preparative isolation of collagen was achieved by digestion of the different eye tissues with pepsin. The pepsin-solubilized collagen was separated by differential salt precipitation into different collagen types.

The polyacrylamide gel electrophoresis of the pepsin-solubilized collagens revealed type I collagen in cornea, sclera, iris, ciliary body, and choroid. As well as type I collagen, type III collagen was isolated from cornea, sclera, and uveal tissues. The identification of types I and III collagen was supported by the CNBr-derived peptides of these collagens. Lens capsule collagen consisted mainly of type IV collagen.

Zonular fibers contained no hydroxyproline but when examined by polyacrylamide gel electrophoresis, a band migrating in the α-position of collagen was observed. Polyacrylamide gel electrophoresis of both the pepsinsolubilized component and the CNBr-derived peptides of vitreous body protein showed no relation to any of the four common collagen types.

Zusammenfassung

Hornhaut, Lederhaut, Regenbogenhaut, Ziliarkörper, Aderhaut, Zonulafasern, Linsenkapsel, Linsenkern, Glaskörper und Netzhaut werden auf ihren Kollagengehalt untersucht. Auch soll festgestellt werden, welche Kollagentypen diese Gewebe aufbauen. Hornhaut, Lederhaut, Regenbogenhaut, Ziliarkörper, Aderhaut, Linsenkapsel und Glaskörper enthalten Hydroxyprolin. Hingegen ist in Zonulafasern, Linsenkern und Netzhaut kein Hydroxyprolin nachzuweisen. Aus den verschiedenen Augengeweben wurde mit Pepsin Kollagen gelöst, das durch Präzipitation mit NaCl-Lösungen verschiedener Molarität in verschiedene Kollagentypen getrennt werden kann.

Die Polyacrylamidgel-Elektrophorese des pepsin-gelösten Kollagens zeigte Type I Kollagen in Hornhaut, Lederhaut, Regenbogenhaut, Ziliarkörper und Aderhaut. Neben Typ I Kollagen wurde aus Hornhaut, Lederhaut und den Geweben der Uvea Typ III Kollagen isoliert. Typ I und Typ III Kollagen wurden durch die Peptide, die man mit CNBr-Spaltung erhalten kann, identifiziert. Die Linsenkapsel besteht hauptsächlich aus Typ IV Kollagen.

Zonulafasern enthalten kein Hydroxyprolin, zeigen aber in der Polyacrylamidgel-Elektrophorese eine Farblinie, die im α-Bereich von Kollagen wandert.

Die Polyacrylamidgel-Elektrophorese des pepsin-gelösten Kollagens des Glaskörpers sowie die CNBr-Spaltprodukte dieses Kollagens zeigten keine Identität mit einem der vier bisher isolierten Kollagentypen.

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  1. Universitäts-Augenklinik Graz, Auenbruggerplatz 4, A-8036, Graz, Austria

    Otto Schmut

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Schmut, O. The organization of tissues of the eye by different collagen types. Albrecht von Graefes Arch. Klin. Ophthalmol. 207, 189–199 (1978). https://doi.org/10.1007/BF00411053

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