The gelatinase MMP-9like is involved in regulation of LPS inflammatory response in Ciona robusta

Falco, Felicia Di; Feo, Salvatore; Arizza, Vincenzo; Vizzini, Aiti

doi:10.1016/j.fsi.2018.11.028

Cited by 15 publications

(17 citation statements)

References 55 publications

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“…The MMPs identified in vertebrates are structurally similar to each other, indicating that they arose by duplication of a common ancestral gene followed by divergent evolution [94]. The phylogenetic analysis comparing human MMPs with their ortholog genes in the chordate Ciona intestinalis, recently recognized as Ciona robusta [95] and considered the closest invertebrate relatives of vertebrates, revealed the presence of six MMPs in this species: MMP-21, MMP-24, MMP-24-2 MMP-14, MMP-14-2, and only one equivalent to gelatinase MMP-9 like [96].…”

Section: Mmp-28 Caseinementioning

confidence: 98%

Profile of Matrix-Remodeling Proteinases in Osteoarthritis: Impact of Fibronectin

Pérez‐García

Carrión

Gutiérrez‐Cañas

et al. 2019

Cells

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The extracellular matrix (ECM) is a complex and specialized three-dimensional macromolecular network, present in nearly all tissues, that also interacts with cell surface receptors on joint resident cells. Changes in the composition and physical properties of the ECM lead to the development of many diseases, including osteoarthritis (OA). OA is a chronic degenerative rheumatic disease characterized by a progressive loss of synovial joint function as a consequence of the degradation of articular cartilage, also associated with alterations in the synovial membrane and subchondral bone. During OA, ECM-degrading enzymes, including urokinase-type plasminogen activator (uPA), matrix metalloproteinases (MMPs), and a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTSs), cleave ECM components, such as fibronectin (Fn), generating fibronectin fragments (Fn-fs) with catabolic properties. In turn, Fn-fs promote activation of these proteinases, establishing a degradative and inflammatory feedback loop. Thus, the aim of this review is to update the contribution of ECM-degrading proteinases to the physiopathology of OA as well as their modulation by Fn-fs.

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Section: Mmp-28 Caseinementioning

confidence: 98%

Profile of Matrix-Remodeling Proteinases in Osteoarthritis: Impact of Fibronectin

Pérez‐García

Carrión

Gutiérrez‐Cañas

et al. 2019

Cells

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“…Apparent bands formed, revealing that the purified aNtMMP-9 bounded to the anti-His Tag antibody via Western Blotting ( Figure S5B). The activity levels of MMP-9 were also assessed by zymography [3,42]. A white band of aNtMMP-9 was also found via gelatin zymography with a molecular weight of approximate 63.4 kDa ( Figure S5C), confirming the protease activity of NtMMP-9 in the biological function.…”

Section: Heterologous Expression and The Enzyme Activity Of Ntmmp-9mentioning

confidence: 62%

“…The protease activity of the purified aNtMMP-9 was tested by gelatin zymography according to the described method [3]. Band intensity was also monitored using the software ImageJ 1.48 (National Institutes of Health, Bethesda, MD, USA) and the formed band intensity represented the protease activity.…”

Section: Protease Activity Assaymentioning

confidence: 99%

“…Furthermore, during the pulmonary infection of mice by Francisella tularensis, MMP-9 can generate proinflammatory ECM-derived peptides against the infection [44]. Similarly, Ciona MMP-9 is involved in inflammatory responses induced by a lipopolysaccharide based on the elevated mRNA levels and enzymatic activity of MMP-9 [3]. MMP-9 is also the most upregulated gene following the Listeria infection in zebrafish, and can be used a protective molecule [12].…”

Section: Heterologous Expression and The Enzyme Activity Of Ntmmp-9mentioning

confidence: 99%

“…Matrix metalloproteinases (MMPs) are a family of 28 zinc-dependent endopeptidases [1], and they are widely distributed in all kingdoms of life [2]. MMPs are secreted as a form of zymogens, and can be activated through the conformational change or cysteine-switch proteolysis [3], which contributes to cleave an extracellular matrix (ECM) and to regulate pathological processes such as inflammation and innate immune defense [4,5] by degradation of the ECM, alteration of cell-cell and cell-ECM interactions, and cleavage of membrane proteins of cell surface and cleavage of proteins in the extracellular environment. Meanwhile, tissue inhibitors of matrix metalloproteinases (TIMPs) inhibit the MMP activity [6].…”

Section: Introductionmentioning

confidence: 99%

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Characterization of Matrix Metalloprotease-9 Gene from Nile tilapia (Oreochromis niloticus) and Its High-Level Expression Induced by the Streptococcus agalactiae Challenge

et al. 2020

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The bacterial diseases of tilapia caused by Streptococcus agalactiae have resulted in the high mortality and huge economic loss in the tilapia industry. Matrix metalloproteinase-9 (MMP-9) may play an important role in fighting infection. However, the role of MMP-9 in Nile tilapia against S. agalactiae is still unclear. In this work, MMP-9 cDNA of Nile tilapia (NtMMP-9) has been cloned and characterized. NtMMP-9 has 2043 bp and encodes a putative protein of 680 amino acids. NtMMP-9 contains the conserved domains interacting with decorin and inhibitors via binding forces compared to those in other teleosts. Quantitative real-time-polymerase chain reaction (qPCR) analysis reveals that NtMMP-9 distinctly upregulated following S. agalactiae infection in a tissue- and time-dependent response pattern, and the tissues, including liver, spleen, and intestines, are the major organs against a S. agalactiae infection. Besides, the proteolytic activity of NtMMP-9 is also confirmed by heterologous expression and zymography, which proves the active function of NtMMP-9 interacting with other factors. The findings indicate that NtMMP-9 was involved in immune responses against the bacterial challenge at the transcriptional level. Further work will focus on the molecular mechanisms of NtMMP-9 to respond and modulate the signaling pathways in Nile tilapia against S. agalactiae invasion and the development of NtMMP-9-related predictive biomarkers or vaccines for preventing bacterial infection in the tilapia industry.

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Ammonia exposure induces oxidative stress and inflammation by destroying the microtubule structures and the balance of solute carriers in the trachea of pigs

Wang

Zeng²,

Zhang³

et al. 2021

Ecotoxicology and Environmental Safety

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The gelatinase MMP-9like is involved in regulation of LPS inflammatory response in Ciona robusta

Cited by 15 publications

References 55 publications

Profile of Matrix-Remodeling Proteinases in Osteoarthritis: Impact of Fibronectin

Profile of Matrix-Remodeling Proteinases in Osteoarthritis: Impact of Fibronectin

Characterization of Matrix Metalloprotease-9 Gene from Nile tilapia (Oreochromis niloticus) and Its High-Level Expression Induced by the Streptococcus agalactiae Challenge

Ammonia exposure induces oxidative stress and inflammation by destroying the microtubule structures and the balance of solute carriers in the trachea of pigs

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