منابع مشابه
Heparanase Facilitates Cell Adhesion and Spreading by Clustering of Cell Surface Heparan Sulfate Proteoglycans
Heparanase is a heparan sulfate (HS) degrading endoglycosidase participating in extracellular matrix degradation and remodeling. Apart of its well characterized enzymatic activity, heparanase was noted to exert also enzymatic-independent functions. Non-enzymatic activities of heparanase include enhanced adhesion of tumor-derived cells and primary T-cells. Attempting to identify functional domai...
متن کاملHeparanase regulates immune cell functions
Immune cells can modify surrounding extracellular matrices by producing matrix degradation enzymes. Heparan sulfate proteoglycans, a major component of basement membrane, play a key role in the self-assembly, insolubility, and barrier properties of the matrix. Some immune cell subsets express heparanase, the sole mammalian endoglycosidase that cleaves heparan sulfate chains and thereby potentia...
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متن کاملTelomeres, A Busy Platform for Cell Signaling
Telomeres are the terminal structures at the ends of linear chromosomes that represent a solution to the end replication problem. Specific binding of the six-protein subunit complex shelterin to telomeric, repetitive TTAGGG DNA sequences contributes to the stable architecture and maintenance of telomeres. Proteins involved in the DNA damage response are also localized at telomeres, and play a r...
متن کاملCell surface localization of heparanase on macrophages regulates degradation of extracellular matrix heparan sulfate.
Extravasation of peripheral blood monocytes through vascular basement membranes requires degradation of extracellular matrix components including heparan sulfate proteoglycans (HSPGs). Heparanase, the heparan sulfate-specific endo-beta-glucuronidase, has previously been shown to be a key enzyme in melanoma invasion, yet its involvement in monocyte extravasation has not been elucidated. We exami...
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ژورنال
عنوان ژورنال: Trends in Biochemical Sciences
سال: 2009
ISSN: 0968-0004
DOI: 10.1016/j.tibs.2009.06.005