Evidence of a small hydrophobic domain in the core protein of the heparan sulfate proteoglycan from human colon carcinoma cells

FEBS Letters

Ketterer, Cynthia L.¹  Iozzo, Renato V.¹  Slaymaker, Diana J.¹ 

[1] Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, 3400 Spruce Street/G1, Philadelphia, PA 19104, USA

关键词: Heparan sulfate proteoglycan;    Hydrophobic peptide;    Core protein;    (Human colon carcinoma cell);    Octyl-Sepharose;   

DOI  :  10.1016/0014-5793(86)81001-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We demonstrate that the cell surface heparan sulfate proteoglycan of human colon carcinoma cells has an affinity for a hydrophobic matrix. This property is mediated by sequences in the core protein, since papain-or alkaline borohydride-released heparan sulfate chains do not bind to the matrix. Trypsin releases a [³H]leucine-rich, unsulfated, hydrophobic peptide, with M _r ~ 5000. This domain is present in neither the proteoglycan released into the medium nor in the intracellular degradation products. It is proposed that this peptide may represent the portion of the core protein intercalated into the plasma membrane.

【 授权许可】

Unknown