Fixed fragments of bovine nasal septum cartilage were digested for six hours either with testicular hyaluronidase or streptomyces hyaluronidase or flavobacter chondroitinase ABC, and observed with a transmission electron microscope. Collagen fibril diameters (D) were measured to evaluate the effect of enzymatic digestion on the fibril size. This resulted in an increased frequency (17 % to 47 %) of "thin" fibrils (80 to 32 nm), followed by a decrease (65 % to 31 %) of the frequency of "mid" fibrils (32 to 64 nm). The frequency of "thick" fibrils (over 64 nm) showed a moderate increase (18 % to 22 %). Considering the relationship between fibril diameter, fibril volume and collagen content, the apparently relevant increase in number of the "thin" fibrils corresponds to an alteration of only 4 % of the total collagen. On the other hand the increase of the "thick" fibrils implies a conspicuous alteration of 20 % of the total collagen. The observed fibril rearrangement after digestion may be explained in terms of the wrap of matrix proteoglycans around each fibril. The enzymatic removal of the proteoglycans could make "mid" collagen fibrils free to regress into "thin" as well as to merge together into "thick" fibrils.

COLLAGEN FIBRIL ULTRASTRUCTURE ALTERS AFTER GLYCANOLYTIC DIGESTION

DIAZ, GIACOMO
1992-01-01

Abstract

Fixed fragments of bovine nasal septum cartilage were digested for six hours either with testicular hyaluronidase or streptomyces hyaluronidase or flavobacter chondroitinase ABC, and observed with a transmission electron microscope. Collagen fibril diameters (D) were measured to evaluate the effect of enzymatic digestion on the fibril size. This resulted in an increased frequency (17 % to 47 %) of "thin" fibrils (80 to 32 nm), followed by a decrease (65 % to 31 %) of the frequency of "mid" fibrils (32 to 64 nm). The frequency of "thick" fibrils (over 64 nm) showed a moderate increase (18 % to 22 %). Considering the relationship between fibril diameter, fibril volume and collagen content, the apparently relevant increase in number of the "thin" fibrils corresponds to an alteration of only 4 % of the total collagen. On the other hand the increase of the "thick" fibrils implies a conspicuous alteration of 20 % of the total collagen. The observed fibril rearrangement after digestion may be explained in terms of the wrap of matrix proteoglycans around each fibril. The enzymatic removal of the proteoglycans could make "mid" collagen fibrils free to regress into "thin" as well as to merge together into "thick" fibrils.
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11584/39250
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo

Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 7
  • ???jsp.display-item.citation.isi??? 5
social impact