Abstract
Kallikreins comprise a family of serine proteases that are required for the processing of hormone precursors, thereby controlling many physiological processes including blood flow, ion transport, and inflammation. In rodents such as mouse, rat, and Mastomys, many kallikreins are expressed in the submandibular gland (SMG), but only a limited number, notably true tissue (glandular) kallikrein, are expressed in the kidney. We report here the cloning and characterization of kallikrein cDNAs from the Mastomys SMG. Two of these are expressed in the kidney as well as in the SMG, and one may code for the true tissue kallikrein of Mastomys. A third kallikrein is expressed only in the SMG and bears some resemblance to a murine nerve growth factor-associated protein. The existence of a family of Mastomys SMG kallikreins suggests that these enzymes act as prohormone-processing enzymes in Mastomys. DNA sequence analysis and hybridization studies demonstrate that, although Mastomys kallikreins are very similar in structure to both mouse and rat kallikreins, their expression patterns differ. The expression of more than one Mastomys glandular kallikrein in the kidney is similar to that in the rat, but the sequence and nonsexually dimorphic expression of the putative tissue kallikrein most closely resembles mouse. Mastomys represents an interesting hybrid between mouse and rat, providing an important animal model for studies of kallikrein expression and regulation.