Purification, characterization, and cDNA cloning of a matrix metalloproteinase from the skeletal muscle of silver carp (Hypophthalmichthys molitrix) with collagen degradation activity

Wu, Jiulin; Wang, Shuang; Sun, Xinyu; Cao, Min‐Jie; Chen, Mingmao; Wang, Jia-Bin; Zhang, Qiqing

doi:10.1016/j.procbio.2016.04.004

Cited by 6 publications

(5 citation statements)

References 24 publications

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“…coli and refolded. The optimum temperature of rMMP1c protein was 37 °C, which is similar to that of most common MMPs ,, and consistent with reported data; the optimum pH is 7.0. Generally, metal ions participate in the catalytic process of enzymes by binding substrates for reaction orientation, reversibly changing the oxidation state of metal ions to regulate redox reactions, and electrostatically stabilizing or shielding negative charges.…”

Section: Discussionsupporting

confidence: 90%

“…To further confirm the MP characteristics of rMMP1c, different metal ions or proteinase inhibitors were added into the reaction system at certain concentrations, and the residual activity was measured. Based on our previous studies, 7,29 the concentration of metal ions was set as 10 mM. The concentration setting of proteinase inhibitors referred to the effective concentrations of proteinase inhibitors published by Dominique M. 30 In the case of metal ion experiments, Zn 2+ and Ca 2+ in the reaction buffer were substituted by the specific ion.…”

Section: Effects Of Metal Ions and Proteinase Inhibitors On Rmmp1cmentioning

confidence: 99%

“…MMPs have a wide range of proteolytic functions and low expression levels under normal physiological conditions, but the expression is significantly elevated in various physiological and pathological processes such as embryogenesis, inflammation, angiogenesis, tumor invasion, and metastasis . MMPs, such as MMP-2 and MMP-9, are involved in collagen degradation and can cause postmortem fish muscle softening. − They induce autolysis in fresh sea cucumbers by degrading interfibrillar proteoglycan bridges between adjacent collagen fibrils. − MMP-1 from Hyriopsis cumingii could completely or partially hydrolyze type I, II, and IV collagen, other than fibronectin and laminin . Previous studies show that MMP-1 was involved in the immune defense of abalone against Vibrio infection. − It was translocated into the nucleus and might act as a transcriptional regulator or activate/inactivate other proteins through proteolysis .…”

Section: Introductionmentioning

confidence: 99%

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Relationships of Matrix Metalloproteinase 1 and a Tissue Inhibitor of Metalloproteinase to Collagen Metabolism in Haliotis discus hannai

Chen

Zhang

et al. 2022

J. Agric. Food Chem.

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In response to physical, chemical, and/or biological stimuli, considerable tissue self-degradation occurs in abalone, causing severe post-harvest quality loss. During this process, the extracellular matrix (ECM) is greatly degraded by endogenous proteases. The main component of the ECM is collagen, primarily type I collagen. Although the activity of matrix metalloproteinases (MMPs), which can specifically degrade collagen, is precisely regulated by tissue inhibitors of MPs (TIMPs), indicating that MMPs and TIMPs play crucial roles in the regulation of tissue self-degradation, few studies have reported the interaction between MMPs and TIMPs. In this study, we reveal collagenases to participate in postmortem tissue self-degradation of Haliotis discus hannai by degrading type I collagen. The recombinant MMP-1 catalytic domain (rMMP1c) of abalone with high purity and enzyme activity is expressed using a prokaryotic expression system. The optimum temperature and pH for rMMP1c are 37 °C and 7.0, respectively. The thermal denaturation temperature of rMMP1c is 67.0 ± 0.9 °C. Ethylenediamine tetraacetic acid (EDTA) and 1,10phenanthroline can completely inhibit rMMP1c activity, while Ba 2+ , Ca 2+ , and Mg 2+ can significantly elevate it. TIMP is also expressed using HEK 293F cells. Recombinant TIMP (rTIMP) shows good inhibitory activity toward rMMP1c. Inhibition kinetics analyses reveal rTIMP to be a competitive inhibitor of rMMP1c. Biolayer interferometry reveals that rTIMP can effectively bind with rMMP1c, with an equilibrium dissociation constant value of 263 nM. rMMP1c effectively degrades type I collagen γ−β−α chains in turn, and rTIMP can significantly inhibit rMMP1c degradation activity. These results provide a theoretical basis for the study of MMP and TIMP interaction and elucidate the possible mechanism for abalone tissue self-degradation.

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Section: Discussionsupporting

confidence: 90%

Section: Effects Of Metal Ions and Proteinase Inhibitors On Rmmp1cmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Relationships of Matrix Metalloproteinase 1 and a Tissue Inhibitor of Metalloproteinase to Collagen Metabolism in Haliotis discus hannai

Chen

Zhang

et al. 2022

J. Agric. Food Chem.

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“…Our study showed that rcMMP‐9 was activated by Ca 2+ , whereas Zn 2+ revealed inhibitory effect, which suggests that calcium binding has a direct effect on the activity of rcMMP‐9. The inhibitory effect of Zn 2+ on the activity of rcMMP‐9 may be due to the binding of zinc hydroxide to the ionized carboxylate in a glutamate residue nearby the active‐site which bridged the catalytic zinc by displacing the bound water molecule (Wu et al., 2016). Our previous studies on carp MMP‐2 also revealed that 5 mM of Zn 2+ inhibited both native and recombinant MMP‐2 (Wang et al., 2014; Xu et al., 2015).…”

Section: Resultsmentioning

confidence: 99%

Involvement of MMP‐9 in collagen degradation of sea bass (Lateolabrax japonicus): Cloning, expression, and characterization

Yang

Chen

Sun

et al. 2022

Journal of Food Science

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Disintegration of intramuscular connective tissue is responsible for postmortem tenderization of fish muscles during chilled storage. Matrix metalloproteinase‐9 (MMP‐9) was reported to be involved in this process, whereas the mechanism has not been revealed. In the present study, purified type I and V collagens from the connective tissues of sea bass (Lateolabrax japonicus) muscles were first prepared. These two kinds of collagens comprise three polypeptide chains (α), forming a typical triple‐helical domain as determined by circular dichroism. The complete coding region of MMP‐9 containing an open reading frame of 2070 bp encoding 689 amino acid residues was then cloned. The recombinant MMP‐9 catalytic domain (rcMMP‐9) was expressed in Escherichia coli and exhibited high hydrolyzing activity toward gelatin. Besides, rcMMP‐9 was effective in degrading type V collagen rather than type I collagen at 4°C. The enzymatic activity of rcMMP‐9 was highly pH‐dependent, and its enzymatic activity under neutral and basic conditions was higher than that under acidic conditions. Metal ion Ca2+ was necessary for the maintenance of rcMMP‐9 activity, whereas Zn2+ inhibited its activity. Our present study indicated that MMP‐9 is responsible for the disintegration of intramuscular connective tissues by cleaving type V collagen during postmortem tenderization of fish muscle. Practical Application Elucidation the involvement of MMP‐9 in collagen degradation will deliver a reference for the prevention of muscular protein decomposition during chilled storage of fish fillets.

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“…Matrix metalloproteinases (MMPs) are capable of degrading all types of extracellular matrix proteins including collagen, laminin and fibronectin (Wu et al ., ) and play remarkably both protective and pathological roles in inflammation such as arthritis and periodontitis (Borghaei et al ., ). Kim‐Park et al .…”

Section: Inhibitory Effects Of the Tea Or Tea Components On The Enzymesmentioning

confidence: 99%

Stop for tea? Enzyme inhibitors from tea – what good are they?

Zhao

et al. 2016

Int J of Food Sci Tech

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Summary Tea possesses many bioactive components including polyphenols, theanine and caffeine. Inhibitory effect of these components on the various enzymes involved in some chronic diseases was reviewed in this study. Many studies revealed that anti‐obesity of tea was mainly ascribed to the polyphenols which could inhibit the activity of the enzymes related to diet metabolism such as α‐amylase, α‐glucosidase and lipase. Inhibitory effect of catechins and caffeine against β‐ and γ‐secretase, acetylcholinesterase, protein kinase C and histone deacetylase might be responsible for the prevention from nervous system diseases. Cytochrome P450 enzymes, cytosolic sulfotransferases, cyclooxygenase‐2 and phosphoinositide‐3‐kinase could be efficiently suppressed by catechins, which would decrease the risk of cancer initiation and proliferation; theanine could lower the activity of some anticarcinogen‐activated enzymes and alleviate the adverse effect of cancer cure. Catechins and caffeine exhibited significant inhibition against the matrix metalloproteinases, histidine decarboxylase and many kinases related to inflammation. Thus, catechins, theanine and caffeine might be employed as inhibitors of the enzymes associated with these chronic diseases.

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Purification, characterization, and cDNA cloning of a matrix metalloproteinase from the skeletal muscle of silver carp (Hypophthalmichthys molitrix) with collagen degradation activity

Cited by 6 publications

References 24 publications

Relationships of Matrix Metalloproteinase 1 and a Tissue Inhibitor of Metalloproteinase to Collagen Metabolism in Haliotis discus hannai

Relationships of Matrix Metalloproteinase 1 and a Tissue Inhibitor of Metalloproteinase to Collagen Metabolism in Haliotis discus hannai

Involvement of MMP‐9 in collagen degradation of sea bass (Lateolabrax japonicus): Cloning, expression, and characterization

Stop for tea? Enzyme inhibitors from tea – what good are they?

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