Role of the COOH-terminal domains of meprin A in folding, secretion, and activity of the metalloendopeptidase.

@article{Tsukuba1998RoleOT,
  title={Role of the COOH-terminal domains of meprin A in folding, secretion, and activity of the metalloendopeptidase.},
  author={Takayuki Tsukuba and Judith S. Bond},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 52},
  pages={35260-7}
}
Secreted forms of the alpha subunit of recombinant mouse meprin A include an NH2-terminal prosequence, a catalytic domain, and three COOH-terminal domains designated as MAM (meprin, A-5 protein, receptor protein-tyrosine phosphatase mu), MATH (meprin and TRAF homology), and AM (after MATH). In this study, the importance of these COOH-terminal domains for biosynthesis of secreted, activable forms of the protease was investigated. Transcripts of the meprin subunit truncated after the protease… CONTINUE READING