Matrix metalloproteinases in COPD

Churg, Andrew; Zhou, Shaoyu; Wright, Joanne L.

doi:10.1183/09031936.00121611

Cited by 240 publications

(133 citation statements)

References 137 publications

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“…Whether or not it is central to the process remains to be determined as it remains possible that several proteinases may play a role in the pathogenesis of COPD. In addition to NSPs, both matrix metalloproteinases [45] and cysteine proteinases [46,47] have been associated with tissue destruction in emphysema both directly and indirectly via their interactions with NSPs and their inhibitors. Strategies to reduce the burden of proteinases in the lungs could potentially offer novel therapies for COPD.…”

Section: Staphylococcus Aureus 2mentioning

confidence: 99%

Proteinase 3 activity in sputum from subjects with alpha-1-antitrypsin deficiency and COPD

Sinden

Stockley²

2012

Eur Respir J

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Chronic obstructive pulmonary disease (COPD) is associated with tissue damage believed to result from an imbalance between serine proteinases and their inhibitors. Although the role of neutrophil elastase (NE) has been studied, it is likely that other proteinases play a role. The importance of proteinase 3 (PR3) has not been established, as specific substrates have only recently been available.We studied clinically stable subjects with either alpha-1-antitrypsin (A1AT) deficiency or usual COPD with chronic bronchitis. Sol phase sputum was analysed for PR3 activity and concentration, NE activity and concentration, concentrations of airway inhibitors (A1AT, secretory leukoproteinase inhibitor and elafin) and markers of neutrophilic inflammation. 12 patients were also studied during exacerbations.PR3 activity was present in most sputum samples and greater than NE activity (which was largely undetectable) in both subject groups (A1AT deficiency median PR3 128 nM, interquartile range (IQR) 33-558 nM; NE 0 nM, IQR 0-0 nM; p50.0043; COPD PR3 22 nM, IQR 0-103 nM; NE 0 nM, IQR 0-0 nM; p50.015). PR3 activity was greater during exacerbations than in the stable state (p50.037) and correlated with markers of neutrophilic inflammation.The regular identification of PR3 activity in sputum from stable subjects with A1AT deficiency or usual COPD suggests it may play a greater role in the pathophysiology than previously thought.

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Section: Staphylococcus Aureus 2mentioning

confidence: 99%

Proteinase 3 activity in sputum from subjects with alpha-1-antitrypsin deficiency and COPD

Sinden

Stockley²

2012

Eur Respir J

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“…However, common biological pathways, such as inflammation, oxidative stress and enzymatic remodelling of the extracellular matrix (for review see [25,26]), are described as driving progression of disease. Since MMPs are key players in the phenomena, and since their expression and activity can be induced by such stimuli [27][28][29], it is highly probable that MMPs could be involved in these effects of pollutants.…”

Section: Underlying Mechanisms Of Pollutant Effectsmentioning

confidence: 99%

“…Moreover, it was associated sometimes with lung injury and oedema [39] or tissue remodelling [25,43], depending on the duration of ozone exposure. Finally, these studies also show that exposures to ozone shorter than 24 h are not able to induce protein expression or activate the different MMPs examined.…”

Section: Mmp-12mentioning

confidence: 99%

Interaction of matrix metalloproteinases with pulmonary pollutants: Table 1–

Dagouassat¹,

Lanone²,

Boczkowski³

2012

Eur Respir J

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An air pollutant consists of any atmospheric substance that may harm humans, animals, vegetation or material. Various air pollutants have been reported, differing in their physicochemical characteristics. They can be grouped into four categories: gaseous pollutants (e.g. ozone, sulfur dioxide, oxides of nitrogen, carbon monoxide and volatile organic compounds), persistent organic pollutants, heavy metals (e.g. cadmium, lead and mercury) and particulate matter (coarse, fine and ultrafine). These pollutants can reach the respiratory system, eliciting pulmonary and/or systemic effects. These effects include inflammation, tissue remodelling and carcinogenesis: all phenomena where matrix metalloproteases (MMPs) play critical roles, given their broad effects on matrix remodelling and modulation of inflammation and cell signalling. Moreover, since expression and activity of MMPs can be induced by such stimuli, the hypothesis has been raised that MMPs could be involved in the health effects of pollutants. Until now, the implication of MMPs in these effects has been studied only for some pollutants and for a restricted selection of MMPs (mainly MMP-1, -2, -9 and -12), while evidence for a link between MMP induction/activation and health effects remains scarce. A larger number of studies is, therefore, needed in order to better understand the implication of MMPs in health effects associated with air pollution.

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“…With regards to reproduction, MMP2 and MMP9 have been associated with ovulation [17] and implantation of the embryo [18]. These two proteins exhibit three gelatin binding fn2 domains at the catalytic site as compared two fn2 domain in BSP proteins and their homologs [19]. These domains are mainly essential for binding with substrates of MMP-2 and MMP-9, such as gelatins, collagens and laminine [20].…”

Section: Mmp 2 and Mmpmentioning

confidence: 99%

Gelatin Binding Proteins in Reproductive Physiology

Kumar¹,

Tinson²,

Mulligan³

et al. 2016

Indian J Microbiol

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In order to advance the assisted reproductive technologies used in animals and human beings, it is important to accumulate basic informations about underlying molecular mechanisms that shape the biological processes of reproduction. From within seminal plasma, proteins perform a wide variety of distinct functions that regulate major reproductive events such as fertilization. The ability of such proteins to bind and interact with different antagonistic ions and biomolecules such as polysaccharides, lipids, and other proteins present in the male and female reproductive tract define these capabilities. Over the last two decades, extensive work has been undertaken in an attempt to define the role of seminal plasma proteins, of which, Gelatin binding proteins (GBPs) represent a large family. GBPs comprise of known group of Bovine seminal plasma (BSP) protein family, matrix metallo proteinases (MMP 2 and MMP 9) and fibronectin, which have been widely studied. The presence of a type II repeat is a characteristic feature of GBPs, which is similar in structure to the fibronectin type II domain (fn2), which has ability to bind multiple ligands including gelatin, glycosaminoglycans, choline phospholipids, and lipoproteins. Two fn2 domains are present within the BSP protein family, while, three fn2 domains are found in gelatinases (MMP-2 and MMP9), and ELSPBP1 (Epididymosomes Transfer Epididymal Sperm Binding Protein 1) contains four long fn2 domains. For the most part BSP proteins are exclusively expressed in seminal vesicles although mBSPH1, mBSPH2 and hBSPH1 are all expressed in the epididymis. The expression of gelatinases has been demonstrated in several organs and tissues such as the prostate, testis, epididymis, ovary, human placenta, cervix and endometrial wall. This review intends to bring current updates on the role of GBPs in reproductive physiology to light, which may act as basis for future studies on GBPs.

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Matrix metalloproteinases in COPD

Cited by 240 publications

References 137 publications

Proteinase 3 activity in sputum from subjects with alpha-1-antitrypsin deficiency and COPD

Proteinase 3 activity in sputum from subjects with alpha-1-antitrypsin deficiency and COPD

Interaction of matrix metalloproteinases with pulmonary pollutants: Table 1–

Gelatin Binding Proteins in Reproductive Physiology

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