Lumican core protein inhibits melanoma cell migration via alterations of focal adhesion complexes

Brézillon, Stéphane; Radwańska, Agata; Zeltz, Cédric; Małkowski, Andrzej; Ploton, Dominique; Bobichon, Hélène; Perreau, Corinne; Malicka-Błaszkiewicz, Maria; Maquart, François‐Xavier; Wegrowski, Yanusz

doi:10.1016/j.canlet.2009.03.032

Cited by 61 publications

(76 citation statements)

References 45 publications

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“…LUM is an extracellular matrix protein and belongs to the family of small leucine-rich proteoglycans. In addition to regulating collagen fibrillogenesis, LUM has been reported to inhibit cell migration in melanoma cells and human mesenchymal stem cells via integrin ␤1 (64,65). PDLIM1/Elfin binds to filamentous actin-associated proteins and regulates organ development (66,67).…”

Section: Lys-464 Mutations Alter Markedly Pr-mediated Progestin Respomentioning

confidence: 99%

Lysine Methylation of Progesterone Receptor at Activation Function 1 Regulates both Ligand-independent Activity and Ligand Sensitivity of the Receptor

Chung

Sze

Woo

et al. 2014

Journal of Biological Chemistry

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Background: Activation function 1 (AF-1) is important for the activity of progesterone receptor (PR), but its functional motif is not known. Results: AF-1 of progesterone receptor (PR) is monomethylated at Lys-464. Lys-464 mutation markedly alters PR properties and ligand sensitivity. Conclusion: Lys-464 is critical for AF-1 function. Significance: Lys-464 is a potential target for modulating AF-1 activity of PR.

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Section: Lys-464 Mutations Alter Markedly Pr-mediated Progestin Respomentioning

confidence: 99%

Lysine Methylation of Progesterone Receptor at Activation Function 1 Regulates both Ligand-independent Activity and Ligand Sensitivity of the Receptor

Chung

Sze

Woo

et al. 2014

Journal of Biological Chemistry

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“…It is a member of the small leucine-rich repeat proteoglycans (10); these were initially investigated in the context of binding collagen and regulating tissue structure and biomechanics (11,12). A body of literature is beginning to indicate that these proteoglycans interact with cytokines, growth factors, and cell surface receptors to modulate cell adhesion, proliferation, and migration (13)(14)(15)(16). Lumican and biglycan, another member of this family of proteoglycans, have been recently shown to regulate host response to pathogenassociated molecular patterns (17,18).…”

mentioning

confidence: 99%

Extracellular Matrix Lumican Deposited on the Surface of Neutrophils Promotes Migration by Binding to β2 Integrin

Lee¹,

Bowrin²,

Hamad

et al. 2009

Journal of Biological Chemistry

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) and LFA-1 (␣ L / ␤ 2 ), the two major PMN surface integrins. We detected lumican on the surface of peritoneal PMNs and not bone marrow or peripheral blood PMNs. This suggests that PMNs must acquire lumican during or after crossing the endothelial barrier as they exit circulation. We also found that peritoneal PMNs do not express lumican, whereas endothelial cells do. Taken together these observations suggest a novel endothelial lumican-mediated paracrine regulation of neutrophils early on in their migration path.Polymorphonuclear neutrophils (PMNs) 3 play a major role in the development of inflammatory responses to host injury and infection. Their functions include destruction of invading bacteria and recruitment of macrophages and lymphocytes to the affected site (1). Circulating PMNs sense injury and pathogen signals, cross the vascular endothelium, and migrate to the target tissue; two series of events control this process. The first leads to the slowing down and adherence of circulating PMNs on the vascular endothelium followed by their transendothelial migration or extravasation and activation (2). The second controls the directional migration of PMNs to the injured site through the endothelial basement membrane, a specialized type of ECM, and subsequently the deeper interstitial ECM, along chemokine and cytokine gradients. Leukocyte-to-leukocyte and leukocyte-to-endothelium interactions are important before extravasation. These are mediated by interactions between selectins and their ligands and by ␤ 2 (MAC-1 and LFA-1) and ␤ 1 (VLA-4 -6) integrin interactions with cell adhesion proteins ICAM and PECAM (3). The directional migration of PMNs through the ECM is a complex, multistep process that involves several ␣ and ␤ integrin interactions with ECM proteins. Thus far, a few basement membrane proteins, laminins, entactin, and fibronectin have been identified as specific ligands in regulating migration of PMNs after extravasation (4 -6). Additional interstitial ECM proteins and their receptors that modulate PMN migration have yet to be identified. Here we show that the ECM protein lumican is a novel regulator of PMN migration.Lumican is a secreted collagen-binding ECM protein of the corneal, dermal, and tendon stroma, arterial wall, and the intestinal submucosa (7-9). It is a member of the small leucine-rich repeat proteoglycans (10); these were initially investigated in the context of binding collagen and regulating tissue structure and biomechanics (11,12). A body of literature is beginning to indicate that these proteoglycans interact with cytokines, growth factors, and cell surface receptors to modulate cell adhesion, proliferation, and migration (13-16). Lumican and biglycan, another member of this family of proteoglycans, have been recently shown to regulate host response to pathogenassociated molecular patterns (17, 18). Thus, lumican-deficient (Lum Ϫ/Ϫ ) mice are hyporesponsive to bacterial lipopolysaccharide (LPS) endotoxins, and Lum Ϫ/Ϫ macrophages in culture produce lower levels of pro-inflammato...

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“…These results suggest that the mechanism of action of lumican on melanoma cells is different from that of decorin [36]. Lumican, as well as leucine-rich repeat peptide from human lumican, inhibits melanoma cell migration [37,38].…”

Section: Discussionmentioning

confidence: 78%

Identification of Small Peptides of Acidic Collagen Extracts from Silver Carp Skin and Their Therapeutic Relevance

et al. 2016

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Background. Low-temperature techniques that prevent protein denaturation are being used to extract collagen from fish skin for cosmetic purposes. These extracts contain collagen with its triple helix structure preserved, as well as a number of other proteins. Objectives. The aim of the study was to investigate collagen extracts from the skin of silver carp for the presence of small-molecule peptides. Material and Methods. Liquid chromatography-mass spectrometry (HPLC-MS) was performed to analyze collagen extracts from silver carp skin for the presence of small-molecule peptides. Results. A large number of different peptides were detected in the silver carp skin collagen extracts analyzed. Among the smaller peptides, the most abundant were those of 7-29 aminoacids originating from the following proteins: collagen Iα1, collagen Iα2, collagen Iα3, collagen VIα3, decorin, lumican, histone H2A, histone H2B and histone H4. Conclusions. The study demonstrated that, in addition to high-molecular-weight collagen proteins, acidic collagen extracts acquired from the skin of silver carp at temperatures up to 16°C also contain considerable amounts of small 7-29 amino-acid peptides. The application of these peptides could therefore be expected to result in beneficial clinical effects in patients in need of reconstructive treatment (Adv Clin Exp Med 2016, 25, 2, 227-235).

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Lumican core protein inhibits melanoma cell migration via alterations of focal adhesion complexes

Cited by 61 publications

References 45 publications

Lysine Methylation of Progesterone Receptor at Activation Function 1 Regulates both Ligand-independent Activity and Ligand Sensitivity of the Receptor

Lysine Methylation of Progesterone Receptor at Activation Function 1 Regulates both Ligand-independent Activity and Ligand Sensitivity of the Receptor

Extracellular Matrix Lumican Deposited on the Surface of Neutrophils Promotes Migration by Binding to β2 Integrin

Identification of Small Peptides of Acidic Collagen Extracts from Silver Carp Skin and Their Therapeutic Relevance

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