Quantitative Mass Spectrometry-Based Secretome Analysis as a Tool to Investigate Metalloprotease and TIMP Activity

Yang, Chun-Yao, Troeberg, Linda and Scilabra, Simone D (2019) Quantitative Mass Spectrometry-Based Secretome Analysis as a Tool to Investigate Metalloprotease and TIMP Activity. In: ADAMTS Proteases. Methods in Molecular Biology, 2043 . Springer, pp. 265-273.

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Abstract

Cell surface proteolysis controls numerous biological processes including cell-cell attachment and the communication between cells. The membrane-tethered families of matrix metalloproteinases (MT-MMPs) and disintegrin metalloproteinases (ADAMs) are major enzymes involved in the cleavage of molecules at the cell surface, and their activity is finely regulated by their endogenous inhibitors, the tissue inhibitors of metalloproteinases (TIMPs). The biological function of a metalloproteinase closely depends on the subset of substrates that it cleaves. Similarly, molecular processes that are regulated by a specific TIMP strictly depend on its unique inhibitory profile.Herein, we describe a mass spectrometry-based method for the quantitative analysis of protein abundance in conditioned media of cultured cells that is particularly suited for substrate identification of membrane-tethered metalloproteinases and for the identification of membrane proteins whose cleavage is regulated by TIMPs. This unbiased proteomic method represents a valuable tool to investigate biological functions of metalloproteinases and TIMPs at the "omic" level.

Item Type: Book Section
Faculty \ School: Faculty of Medicine and Health Sciences > Norwich Medical School
Depositing User: LivePure Connector
Date Deposited: 13 Sep 2019 00:07
Last Modified: 22 Apr 2020 11:23
URI: https://ueaeprints.uea.ac.uk/id/eprint/72155
DOI: 10.1007/978-1-4939-9698-8_22

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