The interactiion of a trypsin-dependent neutral protease and its inhibitor found in tumour cells Analysis of complex kinetic data involved in a thiol-disulphide exchange mechanism

Steven, F. S.; Podrazký, V.; Itzhaki, S.

doi:10.1016/0005-2744(78)90115-8

Cited by 17 publications

(2 citation statements)

References 12 publications

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“…Thus the removal of the denatured collagen is dependent on the balance of natural protease activity on the one hand and inhibition of this activity on the other. The complex kinetics of a similar system have been fully analysed (Steven et al, 1978a) and verified by computer analysis (Steven et al, 1978b).…”

Section: Dislussionmentioning

confidence: 99%

“…It may be possible to overcome this situation by injecting a solution of trypsin directly into the region of the stump ends, so as to overcome the local excess of inhibitor by increasing the concentration of neutral protease with additional trypsin, which also binds the inhibitor (Steven et al, 1978a). If this treatment proves to be capable of cleaning the stump ends of denatured collagen and exposing the native collagen fibril ends, there is a good chance that the repair process may be better orientated and result in a primary repair process taking place between the stump ends directed by the existing native fibrils protruding from the ends, initiating the laying down of parallel collagen fibrils.…”

Section: Dislussionmentioning

confidence: 99%

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Local denaturation of collagen fibres during the mechanical rupture of collagenous fibrous tissue.

Minns¹,

Steven²

1980

Annals of the Rheumatic Diseases

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SUMMARY Human extensor tendons of the hand were pulled to rupture, and the torn ends, when observed in the scanning electron microscope, appeared to be knotted, possibly owing to the denaturation of the collagen. This was confirmed by fluorimetry assays of both the ruptured ends and the middle unbroken sections of the same tendons. The use of a proteolytic enzyme, trypsin, to remove the denatured material and enhance the repair of organised collagen fibres from both ends is suggested if the ruptured ends have the denatured knotted appearance commonly observed clinically.Tendons that have become ruptured in vivo have usually failed because of 2 conditions: because an unusually large force has been applied through the tendon before muscular control has resisted the load, or because the tendon, in particular the collagen fibre network, which resists tensile loads transmitted through the tendon, has undergone biochemical attack substantially weakening the collagen. Tendons that have become divided as a result of trauma show a lesion at the rupture in which the ends have become atrophic and rounded producing a blunt amputation stump. After several months of repair histological evidence shows the junction of the new and old tendon and no regeneration from the proximal stump (Peacock, 1977).Clinical evidence and our interests in degeneration of collagenous tissue led to us conduct a preliminary study on the morphology of tendon ends after mechanical rupture (Steven et al., 1975). A hypothesis we put forward during that study was that the appearance of the ruptured end was a result of denaturation at the fibre ends, so the ends of the distal portions were exposed to trypsin for 24 hours. The tapered and knotted ends were not evident on the trypsin-exposed preparations, suggesting that the ruptured ends contained a substantial amount of denatured collagen.

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Section: Dislussionmentioning

confidence: 99%

Section: Dislussionmentioning

confidence: 99%