Crosslinked CNBr-activated hyaluronan-collagen matrices: effects on fibroblast contraction.
Previously we demonstrated that the contraction of collagen fibrillar matrices (CFM) by fibroblasts was significantly reduced when high concentrations (> 1 mg/ml) of hyaluronan were present in the media. This highlights the prominent role of hyaluronan in preventing scar formation during fetal wound healing. In the present study, we covalently crosslinked different concentrations of CNBr-activated hyaluronan to CFM and investigated the ability of fibroblasts to contract these matrices. Matrices are not contracted when optimal concentrations of CNBr-activated hyaluronan are crosslinked to collagen. Biochemical and cytological analysis of these matrices suggests that hyaluronan strengthens the collagen fibrils and blocks direct communication between fibroblasts and the collagen fibrils. Based on current evidence we are able to propose two molecular crosslinking models, multiple point attachment and simple point attachment between CNBr-activated hyaluronan and collagen molecules, hypotheses supported by the susceptibility of these matrices to digestion by collagenase.
Huang-Lee
L L
LL
Department of Biochemistry and Molecular Biology, School of Medicine, University of Southern California, Los Angeles.
Nimni
M E
ME
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002478:Cells, Cultured; D003094:Collagen; D003488:Cyanogen Bromide; D005109:Extracellular Matrix / Q000502:physiology*; D005347:Fibroblasts / Q000166:cytology / Q000502:physiology*; D006801:Humans; D006820:Hyaluronic Acid; D006821:Hyaluronoglucosaminidase; D008297:Male; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D012879:Skin Physiological Phenomena; D014574:Uronic Acids / Q000032:analysis
D010446:Peptide Fragments; D014574:Uronic Acids; D006820:Hyaluronic Acid; D003094:Collagen; D006821:Hyaluronoglucosaminidase; D003488:Cyanogen Bromide