Chip gel electrophoresis as a tool for study of matrix metalloproteinase 9 interaction with metallothionein

Zítka, Ondřej; Křížková, Soňa; Húska, Dalibor; Adam, Vojtěch; Hubálek, Jaromír; Eckschlager, Tomáš; Kizek, René

doi:10.1002/elps.201000526

Cited by 18 publications

(11 citation statements)

References 19 publications

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“…Several studies have reported that metallothioneins are capable of mediating MMP9 expression [29][30][31]. Our results have demonstrated that the DC-SIGNR protein could significantly increase the expression of metallothioneins after 4 h of incubation.…”

Section: Dc-signr Significantly Induces the Expression Of Metallothiosupporting

confidence: 63%

“…MMP9, a gene in the family of zinc-dependent enzymes and capable of degrading various extracellular matrix components, is associated with colon cancer liver metastasis [46,47]. Ondrej Zitka et al [29] showed that the activity of MMP9 was higher in the presence of metallothioneins compared with an experimental collagen-MMP9 mixture by chip-based gel electrophoresis, which was similar to the temperature effect. Metallothionein-2A, a member of the metallothioneins, could promote breast cancer cell invasion by increasing the expression level of MMP9.…”

Section: Discussionmentioning

confidence: 99%

“…In addition, several studies have reported the function of metallothioneins in the regulation of MMP9 [29][30][31]. MMP9, a gene in the family of zinc-dependent enzymes and capable of degrading various extracellular matrix components, is associated with colon cancer liver metastasis [46,47].…”

Section: Discussionmentioning

confidence: 99%

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Novel roles of DC-SIGNR in colon cancer cell adhesion, migration, invasion, and liver metastasis

Liu

et al. 2017

J Hematol Oncol

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BackgroundTumor metastasis is an essential cause of the poor prognosis of colon cancer. DC-SIGNR is a C-type lectin that is frequently found on human liver sinusoidal endothelial cells. LSECtin, which is a homologue of DC-SIGNR, has been demonstrated to participate in colon cancer liver metastasis. Due to the similarities in the expression pattern and structure of the two proteins, we speculated that DC-SIGNR could also be involved in this process.MethodsColon cancer cells were treated with the DC-SIGNR protein or control IgG, after which cell migration, invasion, and morphology were assayed. Xenograft mouse models were used to determine the role of DC-SIGNR in colon cancer liver metastasis in vivo. In addition, a human gene expression array was used to detect differential gene expression in colon cancer cells stimulated with the DC-SIGNR protein. The serum level of DC-SIGNR was examined in colon cancer patients by ELISA, and the significance of DC-SIGNR was determined.ResultsIn our research, we investigated whether DC-SIGNR promotes colon cancer cell adhesion, migration, and invasion. Knocking down mouse DC-SIGNR decreased the liver metastatic potency of colon cancer cells and increased survival time. Expressing human DC-SIGNR enhanced colon cancer liver metastasis. Furthermore, DC-SIGNR conferred metastatic capability on cancer cells by upregulating various metallothionein isoforms. To validate the above results, we also found that the serum DC-SIGNR level was statistically higher in colon cancer patients with liver metastasis compared with those without metastasis.ConclusionsThese results imply that DC-SIGNR may promote colon carcinoma hepatic metastasis and could serve as a promising therapeutic target for anticancer treatment.Electronic supplementary materialThe online version of this article (doi:10.1186/s13045-016-0383-x) contains supplementary material, which is available to authorized users.

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Section: Dc-signr Significantly Induces the Expression Of Metallothiosupporting

confidence: 63%

Section: Discussionmentioning

confidence: 99%

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Novel roles of DC-SIGNR in colon cancer cell adhesion, migration, invasion, and liver metastasis

Liu

et al. 2017

J Hematol Oncol

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“…The authors also noted that the reduction in the expression of metallothionein-2A completely inhibited tumor migration and invasion in the MDA-MB-231 cell line. Zitka et al 45 also demonstrated that the activity of MMP-9 in collagen degradation increases in the presence of metallothionein in vitro, causing a similar effect to that promoted by temperature in the activity of this protein ( Figure 1). …”

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confidence: 77%

Zinc and metalloproteinases 2 and 9: What is their relation with breast cancer?

Holanda

Oliveira²,

Cruz³

et al. 2017

Rev. Assoc. Med. Bras.

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Zinc is the catalytic component of proteins that regulate responses to DNA damage, intracellular signaling enzymes, and matrix metalloproteinases, which are important proteins in carcinogenesis. The objective of this review is to bring current information on the participation of zinc and matrix metalloproteinases types 2 and 9 in mechanisms involved in the pathogenesis of breast cancer. We conducted a literature review, in consultation with the PubMed, Lilacs, and Scielo databases. The zinc and cysteine residues are structural elements shared by all members of the family of matrix metalloproteinases, and these proteins appear to be involved in the propagation of various types of neoplasms, including breast cancer. Moreover, transported zinc is likely to be used for the metalation of the catalytic domain of the newly synthesized metalloproteinases before the latter are secreted. Accordingly, increase in zinc concentrations in cellular compartments and the reduction of this trace element in the blood of patients with breast cancer appear to alter the activity of metalloproteinases 2 and 9, contributing to the occurrence of malignancy. Thus, it is necessary to carry out further studies with a view to clarify the role of zinc and metalloproteinases 2 and 9 in the pathogenesis of breast cancer.

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“…MT plays a role in maintaining homeostasis of metals and in their storage. MT is an intracellular source of zinc for various metalloenzymes, for example matrix metalloproteinase‐9 (MMP‐9), δ‐aminolevulinic dehydratase (ALAD), and cooper for superoxide dismutase (SOD) . Zn transfer from MT to carbonic anhydrase, SDH, and alkaline phosphatase was also observed.…”

Section: Mt As a Metals Transportermentioning

confidence: 99%

The role of metallothionein interactions with other proteins

2014

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Metallothionein (MT) is a protein involved in numerous key processes, and the most important include zinc ion homeostasis, detoxification of heavy metals, and protection against oxidative stress. MT by interaction with other proteins fulfills its function, resulting in different effects in the body. Interaction of MT with ferritin, which causes a redox reaction, resulting in the reduction of Fe(3+) stored in ferritin and a release of harmful Fe(2+) , was observed. Referring to the redox function of MT, it has been shown that the pair of GSH/GSSG modulates transfer of Zn between MT and Zn-binding proteins. Furthermore, it was shown that GSSG, in the presence of GSH, interacts directly with MT. Apothionein-MT can retrieve Zn from the transcription factors or Zn-containing enzymes. Apothionein-MT by taking Zn can deactivate metal-dependent enzymes while Zn-MT has the opposite effect. As the effect of MT interaction with low-density lipoprotein receptors-megalin and lipoprotein receptor related protein 1, the uptake of Cd-MT occurs and results in the disruption of many functions of proximal tubules. MT is involved in numerous processes and many of them are regulated by protein-protein interactions. Possibly in the future MT will become a therapeutic agent, which will result in a breakthrough in the field of pharmacy and medicine.

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Chip gel electrophoresis as a tool for study of matrix metalloproteinase 9 interaction with metallothionein

Cited by 18 publications

References 19 publications

Novel roles of DC-SIGNR in colon cancer cell adhesion, migration, invasion, and liver metastasis

Novel roles of DC-SIGNR in colon cancer cell adhesion, migration, invasion, and liver metastasis

Zinc and metalloproteinases 2 and 9: What is their relation with breast cancer?

The role of metallothionein interactions with other proteins

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