The isolation of glycoproteins from bovine achilles tendon and their interaction with collagen

Abstract

Two glycoprotein fractions, A and B, were isolated from bovine achilles tendon. Glycoprotein A was prepared from a 0.2m-sodium chloride extract and glycoprotein B was isolated from a 3m-magnesium chloride extract. They were free from serum proteins. Glycoprotein A was essentially free of collagen, but glycoprotein B contained about 8% collagen. Both glycoproteins gave several bands on isoelectric focusing. This technique was also used to demonstrate that both glycoprotein fractions interacted strongly with acid-soluble calf skin tropocollagen. It is concluded that these fractions are true components of tendon, and that they may have some function in the macromolecular organization of the tissue.

The Role of Mechanical Loading in Tendon Development, Maintenance, Injury, and Repair

“…1), tendons exhibit high tensile strength [4][5][6] , allowing for the efficient transmission of large loads, a result of the local cell population to adapt to changes in loading conditions 7 . Further contributing to the structure and biomechanical properties are proteoglycans and glycoproteins, which function to regulate the process of collagen fibrillogenesis and control fibril diameter throughout tendon development and homeostasis [8][9][10][11][12][13] . Studies using genetically manipulated mouse models, in which decorin has been knocked out, have investigated the role of decorin, a small leucine-rich proteoglycan important to tendon structure, and have shown that the absence of decorin results in improper collagen fibril formation and decreases mechanical properties 13 .…”

The periodic wave pattern in native tendon collagen: correlation of polarizing with scanning electron microscopy

“…The answer to the planar crimping phenomenon may lie in directionally specific interfibril interactions perhaps involving acidic structural proteins or glycoproteins (Wolff et al, 1971;Anderson & Jackson, 1972;Dixon, Hunter & Steven, 1972) or mucopolysaccharides (Bychkov, Nikolaeva & Kharlomova, 1968) or both. The collagen fibril itself might have an underlying planarity resulting from the packing of microfibrils within it; this planarity would be reflected in the planar waveform exhibited by the successive hierarchies.…”

Isolation and Chemical Composition of Four Glycoproteins of the Renal Cortex of the Wistar Rat

“…Interesting, too, is the absence of sialic acid, an argument in favor of its collagen nature. The second, GP2, which contains no hydroxylysine, but glucose and sialic acids (2.5%), is probably related to a mixture of collagen structures and non collagen glycoproteins, analogous to those which A nderson and Jackson [29] recently found in the Achilles tendon of bovines.…”