SCIENCE@home

Cysteine Array Matrix Metalloproteinase (CA-MMP)/MMP-23 Is a Type II Transmembrane Matrix Metalloproteinase Regulated by a Single Cleavage for Both Secretion and Activation*

D. Pei,Tiebang Kang,Huaxiong Qi

Published 2000 in Journal of Biological Chemistry

ABSTRACT

Matrix metalloproteinases characterized so far are either secreted or membrane anchored via a type I transmembrane domain or a glycosylphosphatidylinositol linkage. Lacking either membrane-anchoring mechanism, the newly discovered CA-MMP/MMP-23 was reported to be expressed as a cell-associated protein. In this report, we present evidence that CA-MMP is expressed as an integral membrane zymogen with an N-terminal signal anchor, and secreted as a fully processed mature enzyme. We further demonstrate that L20GAALSGLCLLSALALL36 is required for this unique membrane localization as a signal anchor and its secretion is regulated by a proprotein convertase motif RRRR79sandwiched between its pro- and catalytic domains. Thus, CA-MMP is a type II transmembrane MMP that can be regulated by a single proteolytic cleavage for both activation and secretion, establishing a novel paradigm for protein trafficking and processing within the secretory pathway.

PUBLICATION RECORD

CITATION MAP

EXTRACTION MAP

CLAIMS

  • No claims are published for this paper.

CONCEPTS

  • No concepts are published for this paper.

REFERENCES

Showing 1-53 of 53 references · Page 1 of 1

CITED BY

Showing 1-100 of 160 citing papers · Page 1 of 2

12
Next