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Characteristics of matrix metalloproteinases and their role in embryogenesis of the mammalian respiratory system Cover

Characteristics of matrix metalloproteinases and their role in embryogenesis of the mammalian respiratory system

Open Access
|Jan 2021

Figures & Tables

Fig. 1

Diagram of the structure and activation of the MMP proenzyme (on the example of MMP-9). The domains present in the gelatinases are: propeptide, a catalytic domain with a zinc atom (Zn), a hinge region and a hemopexin-like domain. A – non-proteolytic activation using, for example, mercury (Hg) compounds or some denaturing compounds. During this process, there is no disconnection of the propeptide (no change in mass in relation to the proenzyme). If the propeptide activating agent is removed, the propeptide rejoins the active site preventing catalysis (“cysteine switch”). B – proteolytic activation involves the detachment of the propeptide. It is an irreversible process associated with a reduction in the mass of the enzyme by the mass of the propeptide
Diagram of the structure and activation of the MMP proenzyme (on the example of MMP-9). The domains present in the gelatinases are: propeptide, a catalytic domain with a zinc atom (Zn), a hinge region and a hemopexin-like domain. A – non-proteolytic activation using, for example, mercury (Hg) compounds or some denaturing compounds. During this process, there is no disconnection of the propeptide (no change in mass in relation to the proenzyme). If the propeptide activating agent is removed, the propeptide rejoins the active site preventing catalysis (“cysteine switch”). B – proteolytic activation involves the detachment of the propeptide. It is an irreversible process associated with a reduction in the mass of the enzyme by the mass of the propeptide

Fig. 2

Stages of human respiratory system development
Stages of human respiratory system development

Fig. 3

The mutual interactions of MMPs, TIMPs and cytokines
The mutual interactions of MMPs, TIMPs and cytokines

Matrix metalloproteinases, their substrates and tissue inhibitors [15, 82, 91, 93]

Matrix metalloproteinasesNameSubstratesDominant types of tissue inhibitors
MMP-1collagenase 1collagen type I, II, III, V, VII, VIII, X gelatine, entactin, aggrecanTIMP-1, TIMP-3
MMP-2gelatinase Acollagen type I, IV, V, VII, X, XI, XIV, gelatine, elastin, fibronectin, laminin, aggrecanTIMP-2, TIMP-3, TIMP-4
MMP-3stromelysin 1, proteoglycanasecollagen type III, IV, V, IX, X, XI, elastin, laminin, fibronectin, aggrecan, gelatine, proMMP-1, -8, -9TIMP-1, TIMP-3
MMP-7matrilysin, metalloendopeptidasecollagen type IV, X, gelatine, lamininTIMP-1, TIMP-3
MMP-8collagenase 2collagen type I, II, III, V, VII, VIII, X, proteoglycans, fibronectinTIMP-3
MMP-9gelatinase Bcollagen type IV, V, VII, X, XIV, gelatine, aggrecan, elastin, entactin, fibronectinTIMP-1, TIMP-2, TIMP-3, TIMP-4
MMP-10stromelysin 2collagen type III, IV, V, gelatine, casein, elastin, laminin, aggrecan, fibronectinTIMP-1, TIMP-2
MMP-11stromelysin 3collagen type IV, fibronectin, laminin, aggrecan, casein, gelatineTIMP-1, TIMP-2, TIMP-3
MMP-12elastase, macrophage metaloelastasecollagen type IV, elastin, gelatine, fibronectin, vitronectin, lamininTIMP-3
MMP-13collagenase 3collagen type I, II, IIITIMP-1, TIMP-2, TIMP-3
Language: English
Page range: 24 - 34
Submitted on: Jun 16, 2019
Accepted on: Jul 10, 2020
Published on: Jan 25, 2021
Published by: Hirszfeld Institute of Immunology and Experimental Therapy
In partnership with: Paradigm Publishing Services
Publication frequency: 1 times per year

© 2021 Sławomir Wątroba, Tomasz Wiśniowski, Jarosław Bryda, Jacek Kurzepa, published by Hirszfeld Institute of Immunology and Experimental Therapy
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.