Characterizing the function-related specific assembly pattern of matrix metalloproteinase-14 by dSTORM imaging

Dian Ge; Junling Chen; Zhiyong Zhao; Binglin Sui; Feng Liang; Hongda Wang

doi:10.1016/j.talanta.2023.124523

Characterizing the function-related specific assembly pattern of matrix metalloproteinase-14 by dSTORM imaging

Talanta. 2023 Aug 1:260:124523. doi: 10.1016/j.talanta.2023.124523. Epub 2023 Apr 20.

Authors

Dian Ge¹, Junling Chen², Zhiyong Zhao¹, Binglin Sui¹, Feng Liang³, Hongda Wang⁴

Affiliations

¹ Improve-WUST Joint Laboratory of Advanced Technology for Point-of-Care Testing and Precision Medicine, School of Chemistry & Chemical Engineering, Wuhan University of Science and Technology, 947 Heping Street, Wuhan, Hubei, 430081, China.
² Improve-WUST Joint Laboratory of Advanced Technology for Point-of-Care Testing and Precision Medicine, School of Chemistry & Chemical Engineering, Wuhan University of Science and Technology, 947 Heping Street, Wuhan, Hubei, 430081, China. Electronic address: chenjunling@wust.edu.cn.
³ Improve-WUST Joint Laboratory of Advanced Technology for Point-of-Care Testing and Precision Medicine, School of Chemistry & Chemical Engineering, Wuhan University of Science and Technology, 947 Heping Street, Wuhan, Hubei, 430081, China. Electronic address: feng_liang@whu.edu.cn.
⁴ State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Research Center of Biomembranomics, 5625 Renmin Street, Changchun, Jilin, 130022, China. Electronic address: hdwang@ciac.ac.cn.

PMID: 37105082
DOI: 10.1016/j.talanta.2023.124523

Abstract

As transmembrane proteolytic enzyme, matrix metalloproteinase-14 (MMP14) regulates cell migration and cancer metastasis, but how it works at the single molecule level is unclear. Molecular localization is closely related to its function, and revealing its spatial assemble details is thus helpful to understand bio-function. Here, we apply aptamer probe and dSTORM to characterize MMP14 distribution. With demonstrating labeling properties of the probe, we investigate the specific distributed pattern of MMP14 on various cell membranes with different migratory capacities, and find that MMP14 mostly aggregate in clustering state, which becomes more significant with enhancing its hydrolysis efficiency on high-migratory cells. Lots of MMP14 are revealed to be co-localized with its substrate PTK7, and this colocalization decreases with weakening cell migration, suggesting that MMP14 may coordinate cell migration by altering its spatial relationship with substrate proteins. This work will promote a deep understanding of the roles of MMP14 in cell migration and cancer metastasis.

Keywords: Cell migration; Cluster; Direct stochastic optical reconstruction microscopy; MMP14; Single molecule.

MeSH terms

Cell Adhesion Molecules / metabolism
Cell Membrane / metabolism
Humans
Matrix Metalloproteinase 14*
Neoplasms* / metabolism
Receptor Protein-Tyrosine Kinases / metabolism

Substances

Matrix Metalloproteinase 14
PTK7 protein, human
Cell Adhesion Molecules
Receptor Protein-Tyrosine Kinases