Inhibition of plasmin-mediated prostromelysin-1 activation by interaction of long chain unsaturated fatty acids with kringle 5

Huet, Eric; Cauchard, Jean-Hubert; Berton, Alix; Robinet, Arnaud; Decarme, Martine; Hornebeck, William; Bellon, Georges

doi:10.1016/j.bcp.2003.09.033

Cited by 26 publications

(38 citation statements)

References 65 publications

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“…The discrepancy could result from the multiple modes of action of the MMP inhibitor. OA-HY is a hydroxamate derivative of oleic acid that has been shown to inhibit multiple MMPs, including MMP-1, MMP-3, and MMP-9 [15,42,43]. Although we did not detect MMP-9 activity in our co-culture experiments, we could not rule out the possibility that other MMPs were affected during the drug treatment, which complicated the results.…”

Section: Discussioncontrasting

confidence: 71%

A role for endothelial-derived matrix metalloproteinase-2 in breast cancer cell transmigration across the endothelial-basement membrane barrier

Kargozaran

Yuan

Breslin

et al. 2007

Clin Exp Metastasis

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Invasive cancer cells utilize matrix metalloproteinases (MMPs) to degrade the extracellular matrix and basement membrane in the process of metastasis. Among multiple members of the MMP family, the gelatinase MMP-2 has been implicated in the development and dissemination of malignancies. However, the cellular source of MMP-2 and its effect on metastatic extravasation have not been well characterized. The objective of this study was to test the hypothesis that active MMP-2 derived from endothelial cells facilitated the transmigration of breast cancer cells across the microvascular barrier. Gelatin zymography was used to assess latent and active MMP-2 production in conditioned media from MDA-MB-231 human breast cancer cells, human lung microvascular endothelial cells (HLMVEC) and co-culture of these two cells. Transmigrated cancer cells were measured during MMP-2 knockdown with siRNA and pharmacological inhibition of MMP activity with OA-HY. The results showed consistent MMP-2 secretion by the HLMVECs, whereas a low level production was seen in the MDA-MB-231 cells. Inhibition of MMP-2 expression or activity in HLMVECs significantly attenuated the transmigration of MDA-MB-231 cells across an endothelial monolayer barrier grown on a reconstituted basement membrane. The data provide evidence supporting a potential role for the endothelial production of MMPs in promoting cancer cell extravasation. We suggest that the interaction between malignant cells and peritumoral benign tissues including the vascular endothelium may serve as an important mechanism in the regulation of tumor invasion and metastasis.

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Section: Discussioncontrasting

confidence: 71%

A role for endothelial-derived matrix metalloproteinase-2 in breast cancer cell transmigration across the endothelial-basement membrane barrier

Kargozaran

Yuan

Breslin

et al. 2007

Clin Exp Metastasis

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“…The model supports the findings that the K1-and K4-LBS act as independent and complementary domains both able to support Pgn binding and activation, and both seem to be required to ensure Pgn anchorage and subsequent proteolytic activity [62]. The remaining kringles seem to be involved in the modulation of Plm activity rather than anchorage of Pgn to the target surface since it has been shown that K5 interacts with longchain fatty acids [63] as well as various cell surface proteins [64][65][66] and that K3 exhibits a heparin-binding site (Prof. Dr. M. Llinás, personal communication). The model is also consistent with our findings, that isolated rK1 and K4 exhibit a strong affinity for C-terminal Lys 452 , which supports the independence of both domains [62], and that the reinforced interaction between C-terminal Lys 452 and internal Lys 436 in the interaction with the isolated K1-3 domain (two-to threefold increase compared to rK1) underscores the high flexibility of multi-kringle domains (reviewed in [27]) allowing Lys 436 to interact with the LBS of K2.…”

Section: Discussionsupporting

confidence: 70%

The human α2-plasmin inhibitor: functional characterization of the unique plasmin(ogen)-binding region

Gerber

Lejon

Locher

et al. 2010

Cell. Mol. Life Sci.

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The human alpha(2)-plasmin inhibitor (A2PI) possesses unique N- and C-terminal extensions that significantly influence its biological activities. The C-terminal segment, A2PIC (Asn(398)-Lys(452)), contains six lysines thought to be involved in the binding to lysine-binding sites in the kringle domains of human plasminogen, of which four (Lys(422), Lys(429), Lys(436), Lys(452)) are completely and two (Lys(406), Lys(415)) are partially conserved. Multiple Lys to Ala mutants of A2PIC were expressed in Escherichia coli and used in intrinsic fluorescence titrations with kringle domains K1, K4, K4 + 5, and K1 + 2 + 3 of human plasminogen. We were able to identify the C-terminal Lys(452) as the main binding partner in recombinant A2PIC (rA2PIC) constructs with isolated kringles. We could show a cooperative, zipper-like enhancement of the interaction between C-terminal Lys(452) and internal Lys(436) of rA2PIC and isolated K1 + 2 + 3, whereas the other internal lysine residues contribute only to a minor extent to the binding process. Sulfated Tyr(445) in the unique C-terminal segment revealed no influence on the binding affinity to kringle domains.

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“…The disadvantage of using chlorhexidine as an irrigant is that it leads to the production of a potential carcinogenic substance when it reacts with sodium hypochlorite (para-chloroaniline) (James 2011). Several natural substances have been shown to have MMP inhibitory activity such as green tea and avocado (Demeule 2000;Garbisa 2001;Sartor 2002, Kut 1998, Huet 2004). Further research is required on these natural inhibitors before they can be used in the root canal to inhibit the MMPs leading to long term success of post endodontic restorations and obturation materials.…”

Section: Discussionmentioning

confidence: 99%

Identification TIMP-1 and TIMP-2 in Human Radicular Dentine - In Vitro Study

Kandaswamy

Ismail

Rosaline

et al. 2014

JADE

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Aim: To identify TIMP -1 and TIMP -2 in human radicular dentine using confocal laser scanning microscopy. Materials and Methods: Thirty freshly extracted non carious human single rooted pre molars were obtained and stored in isotonic saline at -70°C prior to use. All the teeth were decoronated at the CEJ using a diamond. Teeth were divided into 2 groups (Group 1: TIMP-1 analysis n = 15; Group 2: TIMP-2 analysis n = 15). Teeth were sectioned using a hard tissue microtome, mounted and viewed under confocal laser scanning microscopy. Results: TIMP-1 and TIMP-2 were detected in radicular dentine and were seen to be distributed more towards the inner dentine layer closer to the pulp. Conclusion: Due to a shorter half life of TIMP-1 and 2 as compared to the MMP, there is a need to use MMP inhibitors prior to obturation of the root canal.

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Inhibition of plasmin-mediated prostromelysin-1 activation by interaction of long chain unsaturated fatty acids with kringle 5

Cited by 26 publications

References 65 publications

A role for endothelial-derived matrix metalloproteinase-2 in breast cancer cell transmigration across the endothelial-basement membrane barrier

A role for endothelial-derived matrix metalloproteinase-2 in breast cancer cell transmigration across the endothelial-basement membrane barrier

The human α2-plasmin inhibitor: functional characterization of the unique plasmin(ogen)-binding region

Identification TIMP-1 and TIMP-2 in Human Radicular Dentine - In Vitro Study

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