Collagen treated with (+)-catechin becomes resistant to the action of mammalian collagenase

Abstract

Treatment of radioactively labeled guinea-pig skin soluble collagen or calf skin collagen with the flavonoid (+)-catechin makes the collagen resistant to the action of mammalian collagenase but not to the action of bacterial collagenase. Complete resistance to the action of the mammalian enzyme may be achieved by incubating 0.6 mg of collagen (dry weight) with 0.1 mM (+)-catechin, followed by dialysis to remove the unbound flavonoid. Since incubation of the mammalian enzyme with (+)-catechin does not inhibit its activity, it is postulated that (+)-catechin binds tightly to collagen and modifies its structure sufficiently to make it resistant to enzyme degradation.

Comparative study of Venostasin� and Pycnogenol� in chronic venous insufficiency

“…It has been demonstrated in vitro that collagen is protected from degradation by collagenase when collagen fibres had been pretreated with catechin, one of the constituents of Pycnogenol 1 (Kuttan et al, 1981). The same has been found for elastin, which is rendered resistant towards elastase degradation after pretreatment with oligomeric procyanidins (Tixier et al, 1984).…”

Effect of Different Flavonoids on Collagen Synthesis in Human Fibroblasts

“…Similarly, catechins, in particular ( − )epigallocatechin gallate (EGCG) has been shown to inhibit membrane type I matrix metalloproteinase which hydrolyzes type I collagen [20]. Additionally, certain flavonoids have the ability to bind directly to collagen fibers, thus making them resistant to the action of mammalian collagenase [21]. Flavonoids of subclass proanthocyanidins display high affinity for collagen and elastin fiber in addition to preventing their enzymatic hydrolysis by matrix metalloproteinases [22,23].…”

In vivo autofluorescence spectroscopy of oral premalignant and malignant lesions: Distortion of fluorescence intensity by submucous fibrosis

“…In these regards, the differences in autofluorescence spectra of NOM, OSF, EH, ED, and SCC samples might be attributed to the differences of collagen and NADH content in these samples. OSF mucosa has increased deposition of collagen in the subepithelial connective tissue and the atrophic oral epithelium [20,21]. Therefore, it was easy to explain why OSF samples had a higher 380-nm emission peak and a lower 460-nm emission peak than NOM samples.…”