Structure and Function of Angiogenin
1997; Elsevier BV; Linguagem: Inglês
10.1016/b978-012588945-2/50015-7
Autores Tópico(s)Cell Adhesion Molecules Research
ResumoThis chapter focuses on structure and functions of angiogenin. In many ways, angiogenin is the most unusual member of the ribonuclease superfamily. It shares 33% sequence identity with bovine pancreatic RNase A and has structurally equivalent counterparts for the two histidines and one lysine that comprise the catalytic residues for ribonucleolytic activity. It cleaves preferentially on the 3′ side of pyrimidines to generate a cyclic phosphate product that is subsequently hydrolyzed, but it is 4–6 orders of magnitude less active in routine assays. Despite such seemingly minuscule potency, this ribonucleolytic activity is absolutely critical to the biological function of angiogenin. This chapter discusses in depth about angiogenesis and angiogenic molecules, human angiogenin, and bovine angiogenin. Characterization as a member of the ribonuclease family is explained. The chapter also elaborates the relationship of RNase activity and angiogenic activity. The chapter discusses about binding to endothelial cells, induction of second messengers, and effect on endothelial cell growth. The chapter concludes with a discussion on antiangiogenin antibody suppression of tumor growth.
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