The Matrix Metalloproteinases and Cerebral Ischemia

Yang, Wan Seok; Li, Guangqin

doi:10.5772/33861

Cited by 3 publications

(4 citation statements)

References 26 publications

(39 reference statements)

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“…The binding assay study revealed the K d of four hit compounds (11, 12, 13 and 14) in low micromolar inhibitions (0.6 μM, 0.8 μM, 0.9 μM and 0.8 μM, respectively). The structure of those four compounds (11)(12)(13)(14) are presented in Fig. 7.…”

Section: Computational Drug Modelling Targeting Hemopexin Of Mmp9mentioning

confidence: 99%

“…This 7 shows solvent exposure surrounds difluoromethoxyphenol which decreases the free energy of Fig. 7 The four hit compounds active against PEX9 selected from NCI database (11)(12)(13)(14) [98], the derivatives of 7 (15 [98] binding. In addition, the planar quinazolinone was said to improve the ligand-binding efficiency as well as the longer flexible propyl chain.…”

Section: Computational Drug Modelling Targeting Hemopexin Of Mmp9mentioning

confidence: 99%

“…Structurally, MMPs are zinc-dependent endopeptidases classified as protease enzymes [9]. The main function of these enzymes is to degrade the ECM, which is involved in various physiological processes such as wound healing, inflammation, angiogenesis, vasculogenesis and metastasis [10][11][12][13].…”

Section: Introductionmentioning

confidence: 99%

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Matrix metalloproteinase9 as the protein target in anti-breast cancer drug discovery: an approach by targeting hemopexin domain

et al. 2019

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Background: The discovery and development of anticancer still remain a challenge especially regarding the problem of cancer cell selectivity. Matrix metalloproteinase (MMP) was broadly studied as one of the protein targets to stop cancer angiogenesis as well as its cell migration. Main text: The MMP degrades extracellular matrix (ECM) such as collagen and gelatin which are important to control the cell migration from one to other sites. In cancer, this cell migration is regarded with metastasis, which is essential for the formation of new blood vessels called angiogenesis. The most common target in MMP, i.e. the catalytic site, is currently reported as being the non-selective target for inhibitor compounds that inhibit all MMPs but is associated with adverse side effects. Hemopexin, especially in MMP9 (PEX9) was found to be different from other domains in the MMP family which could potentially be the next target for anticancer due to the availability of its crystal structure in the Protein Data Bank (PDB). Conclusion: The PEX9 crystal structure was resolved as a homodimer connected by a hydrophobic area between two blades along the β-propeller which its structure and function for computational drug modelling can be studied.

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Section: Computational Drug Modelling Targeting Hemopexin Of Mmp9mentioning

confidence: 99%

Section: Computational Drug Modelling Targeting Hemopexin Of Mmp9mentioning

confidence: 99%

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Matrix metalloproteinase9 as the protein target in anti-breast cancer drug discovery: an approach by targeting hemopexin domain

et al. 2019

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“…Moreover, it is the biggest reason for serious long-term disability. Several studies suggests that elevated matrix metalloproteinases (MMPs) play a detrimental role in various types of CNS pathology, including ischemic stroke [1][2][3]. Our recent studies demonstrated the predominant upregulation of MMP-12 and its pathological role in acute brain damage after ischemic stroke [4,5].…”

Section: Introductionmentioning

confidence: 99%

Mesenchymal Stem Cell Treatment Prevents Post-Stroke Dysregulation of Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases

Chelluboina

Nalamolu

Mendez

et al. 2017

Cell Physiol Biochem

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Background/Aims: Stem cell treatment is one of the potential treatment options for ischemic stroke. We recently demonstrated a protective effect of human umbilical cord blood-derived mesenchymal stem cells (HUCB-MSCs) in a rat model of ischemic stroke. The treatment attenuated apoptosis and prevented DNA damage. A collection of published studies, including several from our laboratory, indicated the induction and detrimental role for several matrix metalloproteinases (MMPs) in post-stroke brain injury. We hypothesized that the HUCB-MSCs treatment after focal cerebral ischemia prevents the dysregulation of MMPs and induces the expression of endogenous tissue inhibitors of metalloproteinases (TIMPs) to neutralize the elevated activity of MMPs. Methods: To test our hypothesis, we administered HUCBMSCs (0.25 million cells/animal and 1 million cells/animal) intravenously via tail vein to male Sprague-Dawley rats that were subjected to a transient (two-hour) right middle cerebral artery occlusion (MCAO) and one-day reperfusion. Ischemic brain tissues obtained from various groups of rats seven days after reperfusion were subjected to real-time PCR, immunoblot, and immunofluorescence analysis. Results: HUCB-MSCs treatment prevented the induction of MMPs, which were upregulated in ischemia-induced rats that received no treatment. HUCBMSCs treatment also prevented the induction of TIMPs expression. The extent of prevention of MMPs and TIMPs induction by HUCB-MSCs treatment is similar at both the doses tested. Conclusion: Prevention of stroke-induced MMPs upregulation after HUCB-MSCs treatment is not mediated through TIMPs upregulation.

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In silico modeling and molecular docking insights of kaempferitrin for colon cancer-related molecular targets

Govindarasu

Ganeshan

Ansari

et al. 2021

Journal of Saudi Chemical Society

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The Matrix Metalloproteinases and Cerebral Ischemia

Cited by 3 publications

References 26 publications

Matrix metalloproteinase9 as the protein target in anti-breast cancer drug discovery: an approach by targeting hemopexin domain

Matrix metalloproteinase9 as the protein target in anti-breast cancer drug discovery: an approach by targeting hemopexin domain

Mesenchymal Stem Cell Treatment Prevents Post-Stroke Dysregulation of Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases

In silico modeling and molecular docking insights of kaempferitrin for colon cancer-related molecular targets

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