The pentapeptide NKISK affects collagen fibril interactions in a vertebrate tissue.
The pentapeptide NKISK has been reported to inhibit the binding of decorin, a proteoglycan on the surface of collagen fibrils, to fibronectin, a tissue adhesion molecule. Because of our interest in fibril-fibril binding as it relates to changes in length of ligament or tendon (during growth or contracture), we investigated the potential of this peptide to dissociate fibrils. The peptide permitted the release of intact fibrils into suspension for examination under the electron microscope (which has not previously been possible in mature vertebrate tissues).
Dahners
L E
LE
University of North Carolina School of Medicine, Chapel Hill 27599-7055, USA. led@med.unc.edu
Lester
G E
GE
Caprise
P
P
D000818:Animals; D003094:Collagen / Q000378:metabolism* / Q000648:ultrastructure; D058575:Decorin; D016326:Extracellular Matrix Proteins; D005353:Fibronectins / Q000378:metabolism / Q000494:pharmacology; D017888:Medial Collateral Ligament, Knee; D008854:Microscopy, Electron; D010446:Peptide Fragments / Q000378:metabolism* / Q000494:pharmacology*; D011485:Protein Binding / Q000187:drug effects / Q000502:physiology; D011509:Proteoglycans / Q000378:metabolism*; D051381:Rats; D017207:Rats, Sprague-Dawley; D013623:Tail; D014714:Vertebrates
D058575:Decorin; D016326:Extracellular Matrix Proteins; D005353:Fibronectins; D010446:Peptide Fragments; D011509:Proteoglycans; D003094:Collagen