Nerve Growth Factor. A Structural Relationship Between Its Proteolytic and Leukocyte-Chemotactic Active Sites
Document Type
Article
Publication Date
2-1-1985
Description
High molecular weight mouse nerve growth factor(H M W-NGF), in addition to its effects on certain neural elements, is also chemotactic for human polymorphonuclear leukocytes. One of the subunits of H M W-NGF is a protease of the serine family and its active site contains a serine residue and a closely-neighboring histidine residue that are both essential for proteolysis. Elimination of enzyme activity by irreversibly blocking the single serine has no effect on leukotaxis, but blocking the histidine abolishes leukotaxis. These results suggest the possibility that part of the proteolytic active site of this enzyme may have evolved to perform more than one, completely different, biologic function - proteolysis as well as nonproteolytically mediated chemotaxis.
Citation Information
Younga, Michael; Gee, Adrian P.; Boyleb, Michael D.P.; Lawman, Michael J.P.; and Mungera, Kathy L.. 1985. Nerve Growth Factor. A Structural Relationship Between Its Proteolytic and Leukocyte-Chemotactic Active Sites. Molecular and Cellular Biochemistry. Vol.66(1). 65-69. https://doi.org/10.1007/BF00231825 PMID: 3982403 ISSN: 0300-8177