Abstract
Link protein (Mr = 42,000) is an integral component of cartilage as well as of some noncartilagenous tissues. In cartilage, it forms a macromolecular complex with cartilage proteoglycan and hyaluronic acid, but its function in other tissues is unknown. We provide evidence here that the link protein of cartilage binds well to native collagen types I and III. The binding occurs only if both link protein and collagen are native. The binding of link protein to collagen type fibrils is higher than to monomeric collagen. Link protein binding to collagen fibrils is saturable and occurs at molar ratio of collagen to link protein of 7-13:1. These data suggest that the link protein binds to collagen and that the binding requires the collagen to be in its native triple helical structure. This interaction may play a role in collagen fibril formation.
Highlights
Of cartilage as well oafssome noncartilagenous tissues
Linkprotein (M,= 42,000) was first discovered inthe extracellular matrix of cartilage [1,2,3,4,5]. It was originally found in reassociateddissociative extracts of cartilage and was shown to be present asa macromolecular complex along with the cartilage proteoglycan and hyaluronic acid [1,2,3,4,5,6,7,8]
In order to rule out this possibility, we have carried out coated with collagens (20 pg/well) overnight a t 4 "C, and the studies in which we tested the binding of fibronectin to native and coated wells were incubated with various amountsof the link protein denatured collagen applied to microtiter plates aswell as to nitroceldissolved in PBS plus 0.05% Tween 20 (v/v) at room temperature. lulose paper
Summary
Of cartilage as well oafssome noncartilagenous tissues. Preparation of Collagens-Type I collagen was prepared from an In cartilage, it forms a macromolecular complex with acid extract of rat tail tendon [18]; type I1 collagen was prepared cartilage proteoglycan and hyaluronic acid, but its from the Swarm chondrosarcoma grown in lathyritic rats [19]; type function in other tissues is unknown. In order to rule out this possibility, we have carried out coated with collagens (20 pg/well) overnight a t 4 "C, and the studies in which we tested the binding of fibronectin to native and coated wells were incubated with various amountsof the link protein denatured collagen applied to microtiter plates aswell as to nitroceldissolved in PBS plus 0.05% Tween 20 (v/v) at room temperature. Protein bands were made visible by staining with Coomassie blue R-250
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