Abstract
Endostatin is a C-terminal proteolytic fragment of collagen XVIII that is localized in vascular basement membrane zones in various organs. It binds to heparin/heparan sulfate and to a number of proteins, but its molecular mechanisms of action are not fully elucidated. We have used surface plasmon resonance (SPR) arrays to identify new partners of endostatin, and to give further insights on its molecular mechanism of action. New partners of endostatin include glycosaminoglycans (chondroitin and dermatan sulfate), matricellular proteins (thrombospondin-1 and SPARC), collagens (I, IV, and VI), the amyloid peptide Abeta-(1-42), and transglutaminase-2. The biological functions of the endostatin network involve a number of extracellular proteins containing epidermal growth factor and epidermal growth factor-like domains, and able to bind calcium. Depending on the trigger event, and on the availability of its members in a given tissue at a given time, the endostatin network might be involved either in the control of angiogenesis, and tumor growth, or in neurogenesis and neurodegenerative diseases.
Highlights
The broad molecular targets of endostatin suggest that multiple signaling systems are involved in mediation of its antiangiogenic action
Proteins and glycosaminoglycans selected for surface plasmon resonance (SPR) analysis were present in the same tissues or structures, such as basement membranes [17], brain [18], cartilage [19], or they were involved in the same physiopathological processes as endostatin, and they were available as full-length molecules
We report that endostatin binds to other endogenous angiogenesis inhibitor, the matricellular proteins thrombospondin-1 and SPARC, and to several collagens (I, IV, and VI)
Summary
Endostatin is a C-terminal proteolytic fragment of collagen XVIII that is localized in vascular basement membrane zones in various organs It binds to heparin/heparan sulfate and to a number of proteins, but its molecular mechanisms of action are not fully elucidated. It inhibits angiogenesis and tumor growth [1,2,3]. We have shown that ␣51, ␣v3, and ␣v5 integrins bind to heparin/heparan sulfate [11]
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