Lumican – Derived Peptides Inhibit Melanoma Cell Growth and Migration

Pietraszek, Katarzyna; Brézillon, Stéphane; Perreau, Corinne; Malicka-Błaszkiewicz, Maria; Maquart, François‐Xavier; Wegrowski, Yanusz

doi:10.1371/journal.pone.0076232

Cited by 54 publications

(66 citation statements)

References 33 publications

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“…1B). In addition, previous study from our laboratory showed that lumican-derived peptides were able to regulate the MMP-14 expression in B16F1 cells [34]. These results suggest that lumican, but not decorin, specifically decreases the MMP-14 activity in melanoma cells by interaction with the enzyme.…”

Section: Lumican Inhibits Mmp-14 Activity In a More Efficient Way Thasupporting

confidence: 55%

Lumican: A new inhibitor of matrix metalloproteinase‐14 activity

et al. 2014

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Edited by Veli-Pekka LehtoKeywords: Lumican Decorin Small leucine-rich proteoglycan MMP-14 a b s t r a c tWe previously showed that lumican regulates MMP-14 expression. The aim of this study was to compare the effect of lumican and decorin on MMP-14 activity. In contrast to decorin, the glycosylated form of lumican was able to significantly decrease MMP-14 activity in B16F1 melanoma cells. Our results suggest that a direct interaction occurs between lumican and MMP-14. Lumican behaves as a competitive inhibitor which leads to a complete blocking of the activity of MMP-14. It binds to the catalytic domain of MMP-14 with moderate affinity (K D $ 275 nM). Lumican may protect collagen against MMP-14 proteolysis, thus influencing cell-matrix interaction in tumor progression. Structured summary of protein interactions:MMP-14 binds to Lumican by surface plasmon resonance (View interaction) MMP-14 cleaves Lumican by enzymatic study (View interaction)

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Section: Lumican Inhibits Mmp-14 Activity In a More Efficient Way Thasupporting

confidence: 55%

Lumican: A new inhibitor of matrix metalloproteinase‐14 activity

et al. 2014

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“…inhibiting the migration of melanoma cells and cell-matrix interactions required to promote tumor progression [30,67]. This inhibitory activity resides in a peptide named lumcorin located in LRR-9 of LUM [68]. MT1-MMP however cleaves LUM abrogating the suppressive activity it displays towards tumor cell colony formation [69].…”

Section: Resultsmentioning

confidence: 99%

Catabolism of Fibromodulin in Developmental Rudiment and Pathologic Articular Cartilage Demonstrate Novel Roles for MMP-13 and ADAMTS-4 in C-Terminal Processing of SLRPs

Shu¹,

Flannery²,

Little³

et al. 2018

Preprint

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Cartilage regeneration requires a balance of anabolic and catabolic processes. This study examined the susceptibility of fibromodulin (FMOD) and lumican (LUM) to degradation by MMP-13, ADAMTS-4 and ADAMTS-5, the three major degradative proteinases in articular cartilage in osteoarthritis (OA). Immunolocalisation of FMOD and LUM in foot sections of developmental cartilages demonstrated prominent localisations in metatarsal and phalangeal foetal rudiment cartilages and growth plate. An MMP-13 neoepitope antibody (TsYG11) demonstrated localisation of MMP-13 cleaved FMOD in the hypertrophic chondrocytes of the metatarsal growth plate. FMOD was more prominently localised in the superficial cartilage of normal and fibrillated zones in OA cartilage, TsYG11 positive FMOD was located deeper in the cartilage samples. Ab TsYG11 also identified FMOD fragmentation in Western blots of extracts of normal and fibrillated cartilage and total knee replacement OA cartilage.  The C-terminal anti-FMOD used in this study (PR-184) failed to identify FMOD fragmentation due to C terminal processing, an equivalent Ab to the C-terminus of LUM (pAb PR-353) identified 3 prominent LUM fragments in OA human knee cartilages. In-vitro digestion of human knee cartilage with MMP-13, ADAMTS-4 and ADAMTS-5 generated equivalently sized FMOD fragments of 54, 45 and 32kDa to those in blots of OA cartilage, LUM was not less susceptible to fragmention in in-vitro digestions however Ab PR-353 detected N-terminally processed LUM fragments of 39, 38 and 22 kDa in 65-80 year old OA knee cartilage. FMOD and LUM were differentially processed during in-vitro digestions with MMP-13, ADAMTS-4 and ADAMTS-5 with FMOD susceptible to degradation by MMP-13, ADAMTS-4 and to a lesser extent ADAMTS-5 however LUM was less susceptible to fragmentation. FMOD was processed by MMP-13 in metatarsal and phalangeal foetal rudiment developmental cartilages and growth plate indicating a role in skeletogenesis.

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“…They showed that the peptide effectively forms a complex with type I receptor for TGFb1 (ALK5) and promoted corneal wound healing in mice (Yamanaka et al, 2013). Lumican derived peptides-lumcorin, have been tested against melanoma and show therapeutic potential by inhibiting cell chemotaxis and melanoma growth through MMP-14 inhibition (Zeltz et al, 2009;Pietraszek et al, 2013). The vast array of studies showing the biological activity of lumican underscore the importance of proteogycans in homeostasis and disease and highlight the potential of targeting these ECM molecules to treat disease.…”

Section: Lumicanmentioning

confidence: 99%

“…Dermatan sulfate Macular degeneration, diabetic retinopathy, diabetic macular edema (Devore et al, 2010) Corneal wound healing (Grisanti et al, 2005;Hill et al, 2018) Anti-scarring (Stuart et al, 2011;Ahmed et al, 2014;Wang et al, 2016) Oncosupression (Yang et al, 2015;Wang et al, 2016;Liu et al, 2017;Oh et al, 2017a) Abdominal aortic aneurysm (Shen et al, 2017) Vascular neointimal hyperplasia (Paderi et al, 2011;Scott and Panitch, 2014;Scott et al, 2017) Lumican Keratan sulfate Corneal wound healing (Chakravarti, 2002;Gesteira et al, 2017) Bacterial lung infections (Shao et al, 2012;Shao et al, 2013a) Scarring (Yeh et al, 2005;Liu et al, 2013;Yamanaka et al, 2013;Zhao et al, 2016) Melanoma (Zeltz et al, 2009;Pietraszek et al, 2013)…”

Section: Decorinmentioning

confidence: 99%

Proteoglycans in Biomedicine: Resurgence of an Underexploited Class of ECM Molecules

Walimbe

Panitch

2020

Front. Pharmacol.

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Proteoglycans have emerged as biomacromolecules with important roles in matrix remodeling, homeostasis, and signaling in the past two decades. Due to their negatively charged glycosaminoglycan chains as well as distinct core protein structures, they interact with a variety of molecules, including matrix proteins, growth factors, cytokines and chemokines, pathogens, and enzymes. This led to the dawn of glycan therapies in the 20 th century, but this research was quickly overshadowed by readily available DNA and protein-based therapies. The recent development of recombinant technology and advances in our understanding of proteoglycan function have led to a resurgence of these molecules as potential therapeutics. This review focuses on the recent preclinical efforts that are bringing proteoglycan research and therapies back to the forefront. Examples of studies using proteoglycan cores and mimetics have also been included to give the readers a perspective on the wide-ranging and extensive applications of these versatile molecules. Collectively, these advances are opening new avenues for targeting diseases at a molecular level, and providing avenues for the development of new and exciting treatments in regenerative medicine.

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Lumican – Derived Peptides Inhibit Melanoma Cell Growth and Migration

Cited by 54 publications

References 33 publications

Lumican: A new inhibitor of matrix metalloproteinase‐14 activity

Lumican: A new inhibitor of matrix metalloproteinase‐14 activity

Catabolism of Fibromodulin in Developmental Rudiment and Pathologic Articular Cartilage Demonstrate Novel Roles for MMP-13 and ADAMTS-4 in C-Terminal Processing of SLRPs

Proteoglycans in Biomedicine: Resurgence of an Underexploited Class of ECM Molecules

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