New developments in the genetics and activation of mast cell proteases.
Mast cell chymases and tryptases exhibit an intriguing but potentially confusing variety of forms and functions. Thanks to recent genetic and biochemical advances, a clearer picture of phylogenetic and functional relationships in this large group of mammalian enzymes is emerging. Furthermore, there is increasing appreciation of the diversity of these enzymes among human populations. In humans, there appears to be just one mast cell chymase but multiple expressed tryptases, some of which are allelic variants and others of which are products of separate gene loci. New biological tools, including the dipeptidyl peptidase I (DPPI)-null mouse in which the entire class of mast cell chymases appears to be functionally knocked out, are helping to clarify the importance and specific roles of these most abundant of secreted mast cell proteins.
Caughey
George H
GH
Department of Medicine, Cardiovascular Research Institute, University of California at San Francisco, San Francisco, CA 94143-0911, USA. ghc@itsa.ucsf.edu
D000818:Animals; D020789:Cathepsin C / Q000502:physiology; D056649:Cathepsin G; D002403:Cathepsins / Q000235:genetics; D002877:Chromosomes, Human; D053818:Chymases; D053804:Granzymes; D006801:Humans; D008407:Mast Cells / Q000201:enzymology*; D051379:Mice; D005810:Multigene Family; D010802:Phylogeny; D012697:Serine Endopeptidases / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D053802:Tryptases
C509190:Tpsb2 protein, mouse; D002403:Cathepsins; D020789:Cathepsin C; C509213:GZMB protein, human; D053804:Granzymes; C509214:Gzmb protein, mouse; D012697:Serine Endopeptidases; C534094:CTSG protein, human; D056649:Cathepsin G; C534096:Ctsg protein, mouse; D053818:Chymases; C509222:Tpsab1 protein, mouse; D053802:Tryptases