Unknown

Dataset Information

0

LMAN1 (ERGIC-53) is a potential carrier protein for matrix metalloproteinase-9 glycoprotein secretion.


ABSTRACT: Matrix metalloproteinase-9 (MMP-9) is a secreted glycoprotein with a major role in shaping the extracellular matrix and a detailed understanding of the secretory mechanism could help identify methods to correct diseases resulting from dysregulation of secretion. MMP-9 appears to follow a canonical secretory pathway through a quality control cycle in the endoplasmic reticulum (ER) before transport of the properly folded protein to the Golgi apparatus and beyond for secretion. Through a complementation assay, we determined that LMAN1, a well-studied lectin-carrier protein, interacts with a secretion-competent N-glycosylated MMP-9 in the ER while N-glycosylation-deficient secretion-compromised MMP-9 does not. In contrast, co-immunoprecipitation demonstrated protein interaction between LMAN1 and secretion-compromised N-glycosylation-deficient MMP-9. MMP-9 secretion was reduced in the LMAN1 knockout cell line compared to control cells confirming the functional role of LMAN1. These observations support the role of LMAN1 as a lectin-carrier protein mediating efficient MMP-9 secretion.

SUBMITTER: Duellman T 

PROVIDER: S-EPMC4697752 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

LMAN1 (ERGIC-53) is a potential carrier protein for matrix metalloproteinase-9 glycoprotein secretion.

Duellman Tyler T   Burnett John J   Shin Alice A   Yang Jay J  

Biochemical and biophysical research communications 20150703 3


Matrix metalloproteinase-9 (MMP-9) is a secreted glycoprotein with a major role in shaping the extracellular matrix and a detailed understanding of the secretory mechanism could help identify methods to correct diseases resulting from dysregulation of secretion. MMP-9 appears to follow a canonical secretory pathway through a quality control cycle in the endoplasmic reticulum (ER) before transport of the properly folded protein to the Golgi apparatus and beyond for secretion. Through a complement  ...[more]

Similar Datasets

| S-EPMC7193514 | biostudies-literature
| S-EPMC6404861 | biostudies-literature
| S-EPMC2265576 | biostudies-literature
| S-EPMC1891983 | biostudies-literature
| EMPIAR-11646 | biostudies-other
| S-EPMC7464876 | biostudies-literature
| S-EPMC10944485 | biostudies-literature
| S-EPMC11360742 | biostudies-literature
| EMPIAR-11645 | biostudies-other
| S-EPMC2366877 | biostudies-literature