Some of the amino acid chemistry going on in the Laboratory of Amino Acids, Peptides and Proteins

Bouifraden, S.; Drouot, C.; Hadrami, El Mestafa El; Guenoun, Farhate; Lecointe, L.; Mai, Nathalie; Paris, Marielle; Pothion, Catherine; Sadoune, M.; Sauvagnat, Bérengère; Amblard, Muriel; Aubagnac, Jean‐Louis; Calmès, Monique; Chevallet, Pierre; Daunis, Jacques; Enjalbal, Christine; Fehrentz, Jean‐Alain; Lamaty, Frédéric; Lavergne, Jean‐Pierre; Lázaro, R.; Rolland, Valérie; Roumestant, M. L.; Viallefont, Ph.; Vidal, Y.; Martinez, Jean

doi:10.1007/bf01388176

Cited by 28 publications

(8 citation statements)

References 126 publications

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“…It was obtained by solid-phase synthesis using a FMOC (N-(9-fluorenyl)methoxy-carbonyl) derivative procedure. It was then purified by reverse phase high performance liquid chromatography using a C18 column, eluted by a gradient of acetonitrile in trifluoroacetic acid, and finally lyophilized [ 59 ]. The NC1(XIX) peptide sequence was NPEDCLYPVSHAHQRTGGN.…”

Section: Methodsmentioning

confidence: 99%

The anti-tumor NC1 domain of collagen XIX inhibits the FAK/ PI3K/Akt/mTOR signaling pathway through αvβ3 integrin interaction

et al. 2015

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Type XIX collagen is a minor collagen associated with basement membranes. It was isolated for the first time in a human cDNA library from rhabdomyosarcoma and belongs to the FACITs family (Fibril Associated Collagens with Interrupted Triple Helices). Previously, we demonstrated that the NC1 domain of collagen XIX (NC1(XIX)) exerts anti-tumor properties on melanoma cells by inhibiting their migration and invasion. In the present work, we identified for the first time the integrin αvβ3 as a receptor of NC1(XIX). Moreover, we demonstrated that NC1(XIX) inhibits the FAK/PI3K/Akt/mTOR pathway, by decreasing the phosphorylation and activity of the major proteins involved in this pathway. On the other hand, NC1(XIX) induced an increase of GSK3β activity by decreasing its degree of phosphorylation. Treatments targeting this central signaling pathway in the development of melanoma are promising and new molecules should be developed. NC1(XIX) seems to have the potential for the design of new anti-cancer drugs.

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Section: Methodsmentioning

confidence: 99%

The anti-tumor NC1 domain of collagen XIX inhibits the FAK/ PI3K/Akt/mTOR signaling pathway through αvβ3 integrin interaction

et al. 2015

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“…They were further purified by reverse-phase high-performance liquid chromatography with a C18 column eluted by a gradient of acetonitrile in trifluoroacetic acid and then lyophilized (24). Animals C57Bl6 mice (average body weight, 16 -18 g) were purchased from Harlan France (Gannat, France).…”

Section: Methodsmentioning

confidence: 99%

The NC1 domain of type XIX collagen inhibits in vivo melanoma growth

Ramont

Brassart‐Pasco

Thévenard

et al. 2007

Molecular Cancer Therapeutics

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Type XIX collagen is a minor collagen that localizes to basement membrane zones, together with types IV, XV, and XVIII collagens. Because several NC1 COOH-terminal domains of other chains from basement membrane collagens were reported to exhibit antitumor activity, we decided to study the effects of the NC1(XIX) collagen domain on tumor progression using an experimental in vivo model of mouse melanoma. We observed a 70% reduction in tumor volume in NC1(XIX)-treated mice compared with the corresponding controls. Histologic examination of the tumors showed a strong decrease in tumor vascularization in treated mice. In vitro, NC1(XIX) inhibited the migrating capacity of tumor cells and their capacity to invade Matrigel. It also inhibited the capacity of human microvascular endothelial cells to form pseudotubes in Matrigel. This effect was accompanied by a strong inhibition of membrane type-1 matrix metalloproteinase (matrix metalloproteinase-14) and vascular endothelial growth factor expression. Collectively, our data indicate that the NC1 domain of type XIX collagen exerts antitumor activity. This effect is mediated by a strong inhibition of the invasive capacities of tumor cells and antiangiogenic effects. NC1(XIX) should now be considered as a new member of the basement membrane collagen-derived matrikine family with antitumor and antiangiogenic activity. [Mol Cancer Ther 2007;6(2):506 -14]

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“…(Ivry, France). The NC1 ␣3(IV)-(185-191) peptides CNYYSNS, MNYYSNS, and DNYYSNS were obtained by solid phase synthesis using a Fmoc (N-(9-fluorenyl)methoxycarbonyl) derivative procedure and were purified further by reverse phase high performance liquid chromatography with a C18 column by elution with a gradient of acetonitrile in trifluoroacetic acid, then lyophilized (25).…”

Section: Peptidesmentioning

confidence: 99%

The Antitumor Properties of the α3(IV)-(185-203) Peptide from the NC1 Domain of Type IV Collagen (Tumstatin) Are Conformation-dependent

Floquet¹,

Brassart‐Pasco

Ramont

et al. 2004

Journal of Biological Chemistry

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Tumor progression may be controlled by various fragments derived from noncollagenous 1 (NC1) C-terminal domains of type IV collagen. We demonstrated previously that a peptide sequence from the NC1 domain of the ␣3(IV) collagen chain inhibits the in vitro expression of matrix metalloproteinases in human melanoma cells through RGD-independent binding to ␣ v ␤ 3 integrin. In the present paper, we demonstrate that in a mouse melanoma model, the NC1 ␣3(IV)-(185-203) peptide inhibits in vivo tumor growth in a conformation-dependent manner. The decrease of tumor growth is the result of an inhibition of cell proliferation and a decrease of cell invasive properties by down-regulation of proteolytic cascades, mainly matrix metalloproteinases and the plasminogen activation system. A shorter peptide comprising the seven N-terminal residues 185-191 (CNYYSNS) shares the same inhibitory profile. The three-dimensional structures of the CNYYSNS and NC1 ␣3(IV)-(185-203) peptides show a ␤-turn at the YSNS (188 -191) sequence level, which is crucial for biological activity. As well, the homologous MNYYSNS heptapeptide keeps the ␤-turn and the inhibitory activity. In contrast, the DNYYSNS heptapeptide, which does not form the ␤-turn at the YSNS level, is devoid of inhibitory activity. Structural studies indicate a strong structure-function relationship of the peptides and point to the YSNS turn as necessary for biological activity. These peptides could act as potent and specific antitumor antagonists of ␣ v ␤ 3 integrin in melanoma progression.Tumor growth and metastasis require cross-talk between tumor cells and host stromal cells as well as interactions between tumor cells and the environmental extracellular matrix (ECM), 1 especially basement membranes (1). Basement membranes are thin layers of a specialized ECM which not only provide a supporting structure for various cell types but also largely influence their physiologic behavior. Basement membrane components can also regulate neovascularization, an important process of tumor growth (2, 3). During tumor invasion, the reinforced interactions of tumor cells with basement membranes lead to a sequential proteolytic degradation of their components (4).The degradation of basement membrane macromolecules involves various proteolytic cascades, such as matrix metalloproteinases (MMPs) and the plasminogen activation system. MMPs are a large family of at least 25 members of zinccontaining endopeptidases that degrade ECM macromolecules. Among them, gelatinase A (MMP-2), gelatinase B (MMP-9), and stromelysin (MMP-3) have widely been shown to play a crucial role in the degradation of basement membranes during melanoma progression (5-7). MMPs are secreted as inactive zymogens. Their activation, a major step of tumor invasion, results from an imbalance between levels of tissue inhibitors of metalloproteinases (TIMPs) and the MMP activators, such as urokinase, plasmin, or membrane-type MMPs (MT-MMPs). MT-MMPs constitute a new subgroup of MMPs containing an additional domain for anchorage to th...

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Some of the amino acid chemistry going on in the Laboratory of Amino Acids, Peptides and Proteins

Cited by 28 publications

References 126 publications

The anti-tumor NC1 domain of collagen XIX inhibits the FAK/ PI3K/Akt/mTOR signaling pathway through αvβ3 integrin interaction

The anti-tumor NC1 domain of collagen XIX inhibits the FAK/ PI3K/Akt/mTOR signaling pathway through αvβ3 integrin interaction

The NC1 domain of type XIX collagen inhibits in vivo melanoma growth

The Antitumor Properties of the α3(IV)-(185-203) Peptide from the NC1 Domain of Type IV Collagen (Tumstatin) Are Conformation-dependent

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