Regulation of a membrane-bound proteinase in mammalian cells.
Cellular proteolytic enzymes are regulated by multiple mechanisms that affect gene expression, enzyme concentration, and enzyme activity. The expression of the membrane-bound metallo-endopeptidase, meprin, in different mammalian species, strains, tissues and cell types is highly variable. Meprin is exclusively localized to the plasma membrane, and this determines the types of substrates the enzyme will encounter and the microenvironment for activity. Recent studies have revealed an inactive form of a meprin-like proteinase that can be activated in vitro by proteases, and this raises the possibility of regulation of enzyme activity at the cell surface in response to environmental stimuli. In this chapter, the current knowledge about meprin, and the meprin-like inactive forms in mouse kidney is discussed.
Bond
J S
JS
Department of Biochemistry & Nutrition, State University, Blacksburg 24061-0308.
Butler
P E
PE
Macadam
G
G
Beynon
R J
RJ
D000818:Animals; D002451:Cell Compartmentation; D002462:Cell Membrane / Q000201:enzymology; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism; D007425:Intracellular Membranes / Q000502:physiology; D007668:Kidney / Q000201:enzymology / Q000648:ultrastructure; D008562:Membrane Glycoproteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D008666:Metalloendopeptidases / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D051379:Mice
D004792:Enzyme Precursors; D008562:Membrane Glycoproteins; D008666:Metalloendopeptidases