Oligogalacturonic acid inhibit bone resorption and collagen degradation through its interaction with type I collagen.

Abstract:

:In this study, we showed that oligogalacturonic acid (OGA) purified from flax pectin inhibit in vitro osteoclastic bone resorption in a dose-dependent manner. The OGA inhibitory effect was neither linked to an effect on osteoclast apoptosis, nor to an inhibition of cathepsin K activity. By means of an in vitro collagen degradation assay we demonstrated that OGA prevented triple-helical type I collagen cleavage by cathepsin K in a dose and chain length dependent manner. This inhibition was not restricted to cathepsin K, since collagenolytic activity of other lysosomal cysteine proteases, such as cathepsin B and cathepsin L, as well as matrixmetalloproteinases such as MMP-9 were also inhibited. Interestingly, using non-collagen substrates we demonstrated that OGA does not inhibit the proteolytic activity of cathepsin B and L, suggesting that OGA inhibits collagen degradation without affecting the lysosomal cysteine enzyme proteolytic activity. Finally, preliminary study using surface plasmon resonance (SPR) showed that OGA binds to type I collagen but not to albumin, consistent with a specific effect on collagen. These results suggest that the observed inhibition of collagen degradation by OGA may be due to its ability to bind to the collagen molecule. By masking the collagen surface, OGA may render the collagen cleavage site less accessible to enzymes and thus prevent its enzymatic degradation.

journal_name

Biochem Pharmacol

journal_title

Biochemical pharmacology

authors

Lion JM,Mentaverri R,Rossard S,Jullian N,Courtois B,Courtois J,Brazier M,Mazière JC,Kamel S

doi

10.1016/j.bcp.2009.07.014

subject

Has Abstract

pub_date

2009-12-15 00:00:00

pages

1448-55

issue

12

eissn

0006-2952

issn

1873-2968

pii

S0006-2952(09)00663-7

journal_volume

78

pub_type

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