Somatic cell mutants distinguish CD44 expression and hyaluronic acid binding

1991 ◽  
Vol 33 (5-6) ◽  
pp. 392-395 ◽  
Author(s):  
Robert Hyman ◽  
Jayne Lesley ◽  
Roberta Schulte

2014 ◽  
Vol 29 (9) ◽  
pp. 1866-1874 ◽  
Author(s):  
Z. Molnar ◽  
A. Mokanszki ◽  
Z. Kassai Bazsane ◽  
H. P. Bhattoa ◽  
M. Benyo ◽  
...  


1980 ◽  
Vol 187 (3) ◽  
pp. 687-694 ◽  
Author(s):  
J Wieslander ◽  
D Heinegárd

Antibodies specifically reacting with the link proteins, the hyaluronic acid-binding region and chondroitin sulphate-peptides were used to design specific radioimmunoassay procedures. The sensitivity of the method used for the link protein was about 20 ng/ml, and the other two components could be determined at concentrations of about 2 ng/ml. The radioimmunoassay procedures were tested by using proteoglycan subfractions or fragments thereof. The procedures used to quantify link protein and hyaluronic acid-binding region showed no cross-interference. Fragments of trypsin-digested proteoglycan monomers still reacted in the radioimmunoassay for hyaluronic acid-binding region. Subfractions of proteoglycan monomers separated according to size had a gradually higher relative content of the hyaluronic acid-binding region compared with both chondroitin sulphate-peptides and uronic acid, when the molecules were smaller. The proteoglycans therefore may contain a variably large chondroitin sulphate-rich region, which has a constant substitution with polysaccharide side chains.



1985 ◽  
Vol 232 (1) ◽  
pp. 111-117 ◽  
Author(s):  
M T Bayliss ◽  
P J Roughley

Proteoglycan was extracted from adult human articular cartilage from both the knee and the hip, and A1 preparations were prepared by CsCl-density-gradient centrifugation at starting densities of 1.69 and 1.5 g/ml. Irrespective of whether the cartilage was diced to 1 mm cubes or sectioned to 20 micron slices there was always a lower proportion of both protein and proteoglycan aggregate in the A1 preparation prepared at 1.69 g/ml. Furthermore, the addition of exogenous hyaluronic acid to the extracts before centrifugation did not improve the yield of aggregate at 1.69 g/ml. These results were not affected by the presence of proteinase inhibitors in the extraction medium. It appears that adult human articular cartilage contains a high proportion of low-density proteoglycan subunits and hyaluronic acid-binding proteins that make most of the re-formed proteoglycan aggregates of a lower density than is usually encountered with younger human and mammalian hyaline cartilages.





2000 ◽  
Vol 94 (3) ◽  
pp. 173-178 ◽  
Author(s):  
Mieko Fukui ◽  
Kevin Whittlesey ◽  
Dean D. Metcalfe ◽  
Jaroslaw Dastych


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