Effect of elastin peptides on human monocytes: Ca2+ mobilization, stimulation of respiratory burst and enzyme secretion

Fülöp, Tamás; Jacob, Marie‐Paule; Varga, Zsolt; Fóris, Gabriella; Leövey, A; Robert, L.

doi:10.1016/s0006-291x(86)80339-4

Cited by 98 publications

(19 citation statements)

References 24 publications

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“…The binding of elastin peptides to the elastin-binding protein (EBP) 1 has been shown to be responsible for chemotaxis to the peptides (6 -12), stimulation of cell proliferation (13)(14)(15)(16), ions flux modifications (17,18), vasorelaxation (19 -22), and enzymes secretion (23,24).…”

mentioning

confidence: 99%

Conformational Dependence of Collagenase (Matrix Metalloproteinase-1) Up-regulation by Elastin Peptides in Cultured Fibroblasts

Brassart¹,

Fuchs²,

Huet³

et al. 2001

Journal of Biological Chemistry

155

147

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We have established that treatment of cultured human skin fibroblasts with tropoelastin or with heterogenic peptides, obtained after organo-alkaline or leukocyte elastase hydrolysis of insoluble elastin, induces a high expression of pro-collagenase-1 (pro-matrix metalloproteinase-1 (pro-MMP-1)). The identical effect was achieved after stimulation with a VGVAPG synthetic peptide, reflecting the elastin-derived domain known to bind to the 67-kDa elastin-binding protein. This clearly indicated involvement of this receptor in the described phenomenon. This notion was further reinforced by the fact that elastin peptides-dependent MMP-1 up-regulation has not been demonstrated in cultures preincubated with 1 mM lactose, which causes shedding of the elastin-binding protein and with pertussis toxin, which blocks the elastin-binding protein-dependent signaling pathway involving G protein, phospholipase C, and protein kinase C. Moreover, we demonstrated that diverse peptides maintaining GXXPG sequences can also induce similar cellular effects as a "principal" VGVAPG ligand of the elastin receptor. Results of our biophysical studies suggest that this peculiar consensus sequence stabilizes a type VIII ␤-turn in several similar, but not identical, peptides that maintain a sufficient conformation to be recognized by the elastin receptor. We have also established that GXXPG elastin-derived peptides, in addition to pro-MMP-1, cause up-regulation of pro-matrix metalloproteinase-3 (pro-stromelysin 1). Furthermore, we found that the presence of plasmin in the culture medium activated these MMP proenzymes, leading to a consequent degradation of collagen substrate. Our results may be, therefore, relevant to pathobiology of inflammation, in which elastin-derived peptides bearing the GXXPG conformation (created after leukocyte-dependent proteolysis) bind to the elastin receptor of local fibroblasts and trigger signals leading to expression and activation of MMP-1 and MMP-3, which in turn exacerbate local connective tissue damage.The extracellular matrix protein elastin is responsible for the elastic properties of tissues such as lung, skin, and large arteries (1-3). Due to its numerous cross-links and the extreme hydrophobicity of its tropoelastin chains, elastin is highly resistant to proteolysis. However, during inflammatory disorders, proteinases secreted from polymorphonuclear neutrophils, such as elastase, cathepsin G, and gelatinase B may cause significant elastolysis (4).It has been established that peptides derived from elastin or from the hydrophobic domains of tropoelastin interact with cells via a cell surface-resided 67-kDa elastin-binding protein identical to an enzymatically inactive, alternatively spliced form of ␤-galactosidase (5). The binding of elastin peptides to the elastin-binding protein (EBP) 1 has been shown to be responsible for chemotaxis to the peptides (6 -12), stimulation of cell proliferation (13-16), ions flux modifications (17, 18), vasorelaxation (19 -22), and enzymes secretion (23,24).Matrix metall...

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mentioning

confidence: 99%

Conformational Dependence of Collagenase (Matrix Metalloproteinase-1) Up-regulation by Elastin Peptides in Cultured Fibroblasts

Brassart¹,

Fuchs²,

Huet³

et al. 2001

Journal of Biological Chemistry

155

147

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“…These peptides act as agonists of the elastin-receptor present on the membrane of SMCs [27]. Among other reactions they trigger the release of free radicals and elastolytic endopeptidases [28]. As shown in Figure 3, GPs added to fibroblast cell cultures induce an increased production of elastase activity.…”

Section: Role Of the Maillard Reaction In Atherogenesis And Heart Faimentioning

confidence: 99%

Role of the Maillard reaction in aging and age-related diseases. Studies at the cellular-molecular level

Robert

Labat‐Robert

2014

Clinical Chemistry and Laboratory Medicine

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Increase in life expectancy concerns most populations but more importantly developed countries. This increase is accompanied by the shift of chronic diseases to the senior population, especially cardiovascular diseases and diabetes type II. Aging mechanisms, mostly post-genetic, comprise among others the Maillard reaction which strongly contributes by several harmful processes to the age-dependent decline of tissue structure and function. Several of these mechanisms were studied in our laboratory at the cellular-molecular level and will be described in this review with respect to their role in aging and age-related pathologies, especially cardiovascular diseases.

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“…The ELR was shown to be present on a variety of cell types, among others on monocytes, polynuclear cells, and lymphocytes [39,40]. In the presence of the agonist of the receptor, elastin peptides, there is an amplification of elastase production and release [39][40][41] as well as a release of superoxide radicals [39]. Superoxide is supposed to be responsible for glutamate receptor induced neurotoxicity [42].…”

Section: Production Of Free Radicalsmentioning

confidence: 99%

“…Soon after, this receptor could be demonstrated on a variety of cell types as mentioned above. It could be shown that it controls a variety of biological functions such as cell migration [52], vasorelaxation [43], increase and release of lytic enzymes and free radicals [38][39][40][41], and also modulation of some of the biosynthetic activities of the cells [11]. Among them, we could show recently [53] that the activation of the receptor decreases the rate of incorporation of 14 C-acetate in cholesterol by monocytes in culture.…”

Section: Role Of Cell Membrane Receptorsmentioning

confidence: 99%

Mechanisms of Aging of the Extracellular Matrix: Role of the Elastin-Laminin Receptor

Robert

1998

Gerontology

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Aging of connective tissues is important for the understanding of aging mechanisms of tissues rich in extracellular matrix and of age-dependent diseases often affecting such tissues. Aging mechanisms of such tissues can be divided as follows: (1) age-dependent modifications of matrix biosynthesis; (2) postsynthetic modifications of extracellular matrix, and (3) modifications of cell-matrix interactions. Examples are discussed for all three aspects of tissue aging, with special emphasis on the role of epigenetic reactions. These reactions include the Maillard reaction, uncontrolled proteolytic degradation, and free radical release. Proteolytic fragments of fibronectin and of elastic fibers were shown to produce noxious effects and to be engaged in vicious circles of autoentertained and self-amplified mechanisms. We studied in particular the role of the elastin-laminin receptor in tissue aging and in atherogenesis. The presence of saturating concentrations of elastin peptides in the circulation results in a chronic overstimulation of the receptor with sustained free radical and lytic enzyme production. Other examples of age-dependent uncoupling of receptors also illustrate the importance of altered receptor function in tissue aging and related pathologies.

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Effect of elastin peptides on human monocytes: Ca2+ mobilization, stimulation of respiratory burst and enzyme secretion

Cited by 98 publications

References 24 publications

Conformational Dependence of Collagenase (Matrix Metalloproteinase-1) Up-regulation by Elastin Peptides in Cultured Fibroblasts

Conformational Dependence of Collagenase (Matrix Metalloproteinase-1) Up-regulation by Elastin Peptides in Cultured Fibroblasts

Role of the Maillard reaction in aging and age-related diseases. Studies at the cellular-molecular level

Mechanisms of Aging of the Extracellular Matrix: Role of the Elastin-Laminin Receptor

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