Angiogenin (E8O6J) Rabbit mAb #62224

Angiogenin (ANG, RNase 5) is a member of the ribonuclease A superfamily (1,2). It plays many diverse roles in cell and tissue function, including angiogenesis, innate immune function, signal transduction, and cellular stress responses. Angiogenin has been shown to promote tumor development, but has also been implicated in protection against neurodegenerative diseases (3-6). Angiogenin may be secreted into plasma, but it is also found within various tissues and cell types. It is a highly pleiotropic protein, acting through many diverse mechanisms. In the extracellular matrix, angiogenin promotes actin polymerization, and interacts with members of the plasminogen activation system to stimulate plasmin generation and promote cell migration (7,8). At the cell surface, angiogenin binds to receptors, such as plexin B2 and EGFR, activating signal transduction pathways (e.g., ERK and Akt) that promote cell proliferation and survival (9,10). Angiogenin also enters cells via receptor-mediated endocytosis; it may accumulate in nucleoli under growth conditions, or in the cytoplasm under stress conditions. Within nucleoli, angiogenin has been shown to epigenetically activate the promoter regions of rDNA, stimulating rRNA transcription. In conditions of cellular stress, angiogenin has been reported to translocate to the cytoplasm, and cleave tRNA in anticodon loops to produce tiRNA fragments. These stress-induced tiRNA fragments initiate cellular stress responses that serve to protect the host cell from apoptosis (11).