Premium
Kurloff cell proteoglycans: presence of two main size‐populations of intracellular protease‐resistant proteochondroitin sulphate. Effect of D‐xyloside
Author(s) -
Letaíef SlimEric,
Landemore Gérard,
Bocquet Jean,
Izard Jacques
Publication year - 1989
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1111/j.1768-322x.1989.tb00797.x
Subject(s) - papain , pronase , sepharose , glycosaminoglycan , size exclusion chromatography , intracellular , chromatography , biology , protease , incubation , biochemistry , chemistry , trypsin , enzyme
This paper reports that the Kurloff cell sulphated and chondroitinase AC sensitive material previously described filtered on Sepharose CL4B columns as 2 main populations with Kav of 0.25 and 0.44. Its alkaline treatment resulted in the elution of 2 peaks with Kav of 0.52 and 0.78. Their reduction in size observed after alkaline treatment and the 6‐fold increase in the ( 35 S) sulphate incorporation after addition of 0.1 mM xyloside to the incubation medium indicate that these intracellular sulphated glycosaminoglycans exist in the form of proteoglycans. They were characterized by their resistance to degradation by pronase, papain or cathepsin D, as assessed by gel filtration chromatography on Sepharose CL6B or CL4B. After the glycosaminoglycans were digested with chondroitinase AC, thin‐layer chromatography analysis indicated the presence of Δ di‐4S and Δ di‐6S in a ratio of 7:1. The presence of such protease‐resistant proteochondroitin sulphate in intracytoplasmic granules of both Kurloff cells and other natural killer cell types is emphasized.