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

Sławomir Wątroba
Sławomir Wątroba
, 
Tomasz Wiśniowski
Tomasz Wiśniowski
, 
Jarosław Bryda
Jarosław Bryda
 e 
Jacek Kurzepa
Jacek Kurzepa
   | 25 gen 2021
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Article Category: Review
Pubblicato online: 25 gen 2021
Pagine: 24 - 34
Ricevuto: 16 giu 2019
Accettato: 10 lug 2020
DOI: https://doi.org/10.5604/01.3001.0014.6933
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© 2021 Sławomir Wątroba et al., published by Sciendo
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

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 metalloproteinases Name Substrates Dominant types of tissue inhibitors
MMP-1 collagenase 1 collagen type I, II, III, V, VII, VIII, X gelatine, entactin, aggrecan TIMP-1, TIMP-3
MMP-2 gelatinase A collagen type I, IV, V, VII, X, XI, XIV, gelatine, elastin, fibronectin, laminin, aggrecan TIMP-2, TIMP-3, TIMP-4
MMP-3 stromelysin 1, proteoglycanase collagen type III, IV, V, IX, X, XI, elastin, laminin, fibronectin, aggrecan, gelatine, proMMP-1, -8, -9 TIMP-1, TIMP-3
MMP-7 matrilysin, metalloendopeptidase collagen type IV, X, gelatine, laminin TIMP-1, TIMP-3
MMP-8 collagenase 2 collagen type I, II, III, V, VII, VIII, X, proteoglycans, fibronectin TIMP-3
MMP-9 gelatinase B collagen type IV, V, VII, X, XIV, gelatine, aggrecan, elastin, entactin, fibronectin TIMP-1, TIMP-2, TIMP-3, TIMP-4
MMP-10 stromelysin 2 collagen type III, IV, V, gelatine, casein, elastin, laminin, aggrecan, fibronectin TIMP-1, TIMP-2
MMP-11 stromelysin 3 collagen type IV, fibronectin, laminin, aggrecan, casein, gelatine TIMP-1, TIMP-2, TIMP-3
MMP-12 elastase, macrophage metaloelastase collagen type IV, elastin, gelatine, fibronectin, vitronectin, laminin TIMP-3
MMP-13 collagenase 3 collagen type I, II, III TIMP-1, TIMP-2, TIMP-3
eISSN:
1732-2693
Lingua:
Inglese
Frequenza di pubblicazione:
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Argomenti della rivista:
Life Sciences, Molecular Biology, Microbiology and Virology, Medicine, Basic Medical Science, Immunology
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