New approaches to selectively target cancer-associated matrix metalloproteinase activity

Tauro, Marilena; McGuire, Jeremy; Lynch, Conor C.

doi:10.1007/s10555-014-9530-4

Cited by 65 publications

(52 citation statements)

References 106 publications

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“…Cancer cell migration and invasion are promoted by a degradation of matrix collagen by metalloproteinases (20)(21)(22). In our previous paper, we reported suppression of MDA-MB-231 cell migration into type I collagen gels in the presence of galardin which is known as an MMP inhibitor (12).…”

Section: Resultsmentioning

confidence: 99%

Toad skin extract cinobufatini inhibits migration of human breast carcinoma MDA-MB-231 cells into a model stromal tissue

Nakata

Mori

Kamoshida

et al. 2015

BST

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Section: Resultsmentioning

confidence: 99%

Toad skin extract cinobufatini inhibits migration of human breast carcinoma MDA-MB-231 cells into a model stromal tissue

Nakata

Mori

Kamoshida

et al. 2015

BST

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“…Disruption of the interaction of the CSCs with the ECM by inhibiting the MMPs [147] and integrins [148] as well as by the application of collagenase and hyaluronidase have also shown promising results in hindering the disease progress [149].…”

Section: Aim Towards Developing a Targeted Therapy Against The Cancermentioning

confidence: 99%

Cancer stem cells, their origin and niche: A search for the therapeutic target

Das¹,

Dutta²,

Paul³

et al. 2017

J Stem Cell Res Med

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Cancer is a general term to define a group of genetic alterations and the subsequent phenotypic and physiological changes at the cellular level, leading to accelerated death of the host. According to The World Health Organisation (WHO), it is the second leading factor for human deaths globally. Cancer is such a difficult challenge for mankind because of its ability to relapse even after detailed treatments with chemotherapeutic agents and ionizing radiations. This can be explained by the emerging concept of 'tumor initiating cells' or 'cancer stem cells' (CSCs) which comprise a pluripotent and genomically dynamic subpopulation of the tumor microenvironment, occupying only 0.1%-3% of the total tumor population. Despite their emerging significance in disease progression and recurrence, the origin of these CSCs and their complex interaction with the corresponding CSC niche still remain to be elusive. In this review, we make an attempt to unwind the mystery of the origin of the CSCs as well as focus on the well-established cross-talk mechanisms between the CSCs and their niche components. Lastly, we try to find alternative therapeutic strategies to combat CSC resistance by targeting the various components of the CSC niche.

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“…Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that can degrade numerous types of ECM components (5,6). Among others, MMP-2 basally expresses while MMP-9 is an inducible enzyme, both of which primarily degrade types-I and -IV collagen and laminin, major components of ECM (7)(8)(9).…”

Section: Introductionmentioning

confidence: 99%

“…Among others, MMP-2 basally expresses while MMP-9 is an inducible enzyme, both of which primarily degrade types-I and -IV collagen and laminin, major components of ECM (7)(8)(9). Generally, MMP-2 and MMP-9 are involved in tumor metastasis (6,10). Furthermore, it has been shown that insufficient MMP-2 and MMP-9 may be a contributor of ECM accumulation in DN (11).…”

Section: Introductionmentioning

confidence: 99%

C-peptide exhibits a late induction effect on matrix metallopeptidase-9 in high glucose-stimulated rat mesangial cells

Wang

et al. 2016

Experimental and Therapeutic Medicine

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Abstract. Insufficient matrix metalloproteinase (MMP)-9 and MMP-2 is considered to be a contributor of extracellular matrix (ECM) accumulation in diabetic nephropathy (DN). C-peptide can reverse fibrosis, thus exerting a beneficial effect on DN. Whether C-peptide induces MMP-9 and MMP-2 to reverse ECM accumulation is not clear. In the present study, in order to determine ECM metabolism, rat mesangial cells were treated with high glucose (HG) and C-peptide intervention, then the early and late effects of C-peptide on HG-affected MMP-9 and MMP-2 were evaluated. Firstly, it was confirmed that HG mainly suppressed MMP-9 expression levels. Furthermore, C-peptide treatment induced MMP-9 expression at 6 h and suppressed it at 24 h, revealing the early dual effects of C-peptide on MMP-9 expression. Subsequently, significant increase in MMP-9 expression at 72, 96 and 120 h C-peptide treatment was observed. These changes in MMP-9 protein content confirmed its expression changes following late C-peptide treatment. Furthermore, at 96 and 120 h C-peptide treatment reversed the HG-inhibited MMP-9 secretion, further indicating the late induction effect of C-peptide on MMP-9. The present results demonstrated that C-peptide exerted a late induction effect on MMP-9 in HG-stimulated rat mesangial cells, which may be associated with the underlying mechanism of C-peptide's reversal effects on DN. IntroductionDiabetic nephropathy (DN), the leading cause of end stage renal disease, is the major cause of mortality in type 1 diabetes mellitus (DM) and the second most severe complications in type 2 diabetes (1,2). Deposition of extracellular matrix (ECM) in mesangial areas is a feature of DN, and mesangial cells have been proposed to be the determinant of ECM accumulation (3,4). However, the mechanism underlying ECM accumulation in DN is not fully clarified.Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that can degrade numerous types of ECM components (5,6). Among others, MMP-2 basally expresses while MMP-9 is an inducible enzyme, both of which primarily degrade types-I and -IV collagen and laminin, major components of ECM (7-9). Generally, MMP-2 and MMP-9 are involved in tumor metastasis (6,10). Furthermore, it has been shown that insufficient MMP-2 and MMP-9 may be a contributor of ECM accumulation in DN (11). However, the expression levels of MMP-2 and MMP-9 in DN remain controversial, and even short-and long-term hyperglycemia may exert differential effects (8,(12)(13)(14). As an inducible enzyme, MMP-9 may be more easily affected in patients with DN (15). Therefore, the changes of MMP-2, and particularly MMP-9, for high glucose (HG) stimulation require clarification.C-peptide is the linker between the A-chain and B-chain of insulin. Lack of C-peptide along with insulin is the primary feature of type 1 DM and late stage of type 2 DM (16). C-peptide has been found to have unique beneficial effects on DN, attenuating glomerular and tubular injury (17)(18)(19). Physiological concentration of C-peptide ca...

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New approaches to selectively target cancer-associated matrix metalloproteinase activity

Cited by 65 publications

References 106 publications

Toad skin extract cinobufatini inhibits migration of human breast carcinoma MDA-MB-231 cells into a model stromal tissue

Toad skin extract cinobufatini inhibits migration of human breast carcinoma MDA-MB-231 cells into a model stromal tissue

Cancer stem cells, their origin and niche: A search for the therapeutic target

C-peptide exhibits a late induction effect on matrix metallopeptidase-9 in high glucose-stimulated rat mesangial cells

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