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Elastin peptides
Peptide from fish skin
Supports the creation of new elastin fibers in skin and arteries. In skin it helps to fight gravity, in arteries, it keeps them flexible.
Effect of elastin peptides on vascular tone.
J Vasc Res. 1995 Mar-Apr;32(2):112-9.
Faury G, Ristori MT, Verdetti J, Jacob MP, Robert L.
Centre de Physiologie et Physiopathologie Cellulaires, Université Joseph-Fourier, Grenoble, France.
Elastin peptides are present in human blood. As elastin receptors exist on several cell types, especially endothelial cells, this investigation was carried out to study the effect of elastin peptides on vascular tone. For this purpose, rat aortic rings were mounted in an organ bath for isometric tension measurements. Elastin peptides (kappa-elastin) were added in the concentration range of 0.1 ng/ml to 1 microgram/ml, concentrations similar to those found in the circulating blood. In rat aortic rings, precontracted or not with noradrenaline (10(-6) M), elastin peptides induced an endothelium-dependent vasodilation. The pretreatment of aortic rings with N-omega-nitro-L-arginine methyl ester (10(-5) M), an inhibitor of nitric oxide (NO) production, or with indomethacin (10(-5) M), an inhibitor of cyclooxygenase, prevented elastin peptide-induced vasodilation. These findings suggest that elastin peptides act through the synthesis of prostanoids, leading to the production of NO. Moreover, this relaxant effect of elastin peptides was decreased or inhibited when aortic rings were treated with lactose (10(-5) to 10(-2) M) or laminin (10(-6) to 10(-4) mg/ml) whereas lactose or laminin was unable to inhibit acetylcholine-induced vasodilation. These findings suggest that the inhibitory effects of lactose and laminin are specific for elastin peptide receptors and are in agreement with previous studies on these receptors. As there is evidence of the degradation of elastin in several vascular diseases, the concept that elastin peptides may contribute to the control of vascular tone is discussed.
Ehrlich chromogens, probable cross-links in elastin and collagen.
Kemp PD, Scott JE. >Biochem J. 1988 Jun 1;252(2):387-93.
Chemical Morphology, Cell and Structural Biology, University of Manchester, U.K.
Proteolytic digests of tissue elastin contain material which reacts with dimethylaminobenzaldehyde in acid solution (Ehrlich's reagent) to give a cherry-pink colour. This Ehrlich chromogen(s) [EC(s)] is similar to but not identical with EC(s) previously demonstrated in tissue collagens [Scott, Hughes & Shuttleworth (1979) Biosci. Rep. 1, 611-618]. Both ECs react with diazonium salts in acid to give coloured products.
Diazobenzene linked via a phenolic ester to polyacrylamide beads (Biogel P10) has been used to absorb ECs specifically and almost quantitatively from proteolytic digests. The coupled deeply coloured azo-EC-peptides were then recovered after mild alkaline cleavage from the support and purified by gel chromatography.
Using 15N-labelled NaNO2, the collagen azo-EC-peptides were prepared, and 15N abundance measured therein. The molar absorption coefficient of the azo-EC group was calculated (18,700) based on the assumption that each azo-EC group contained one 15N atom.
Collagen azo-EC-peptides contained glucose and galactose, whereas elastin azo-EC peptides did not. The amino acid patterns of the two peptides were quite different, the former being rich in polar amino acids, the latter containing much alanine. The patterns were compatible with an origin from the cross-linking regions of collagen and elastin respectively.
Quantitative (molar) comparisons of the azo-EC group content with amino acid, amino end-group and sugar contents, and azo-EC peptide molecular mass, suggest that a structure is present in the collagen azo-EC-peptides containing two EC groups shared between four peptide chains. Three peptide chains probably meet at each (cross-linking) EC group. Based on this structure, about 15% of adult bovine skin collagen contains EC groups.
Study of the refirming effect of a plant complex.
Benaiges A, Marcet P, Armengol R, Betes C, Gironés E. Int J Cosmet Sci. 1998 Aug;20(4):223-33.
Provital S.A. Pol. Ind. Santiga, Talleres 6, Barberádel Vallés, Barcelona, Spain.
Loss of skin elasticity is one of the main problems of ageing. This is a mechanical property influenced by elastin, a protein in the dermis which, together with collagen and glycosaminoglycans, makes up the connective tissue. This tissue is affected by a large number of events (such as cutaneous ageing, pregnancy, slimming processes and cellulitis) which eventually cause it to change. At the same time, the metabolism of the proteins of the connective tissue decreases and there is an ever greater presence of enzymes, principally elastases and collagenases, which are responsible for breaking down the elastin and the collagen. One way to prevent such a loss of elasticity is to use active ingredients that are able to inhibit elastase enzymes. A plant complex was prepared using the following plants: lady's thistle (Silybum marianum GAERTN), alchemilla or yarrow (Alchemilla vulgaris L.), horsetail (Equisetum arvense L.) as well as germinated seeds (Glycine soja Siebold and Zucc., Triticum vulgare Vilars, Medicago sativa L., Raphanus sativus L.). The complex was standardized to give the corresponding active principles, silybin, tannins, silicon and peptides, respectively, and in vitro enzymatic tests were carried out to establish its ability to inhibit elastase. The study of enzymatic inhibition was carried out using two enzymes: (1) porcine pancreatic elastase (PPE), and (2) human leukocyte elastase (HLE). The results showed that the plant complex presents non-competitive inhibition in the order of 41.0% against PPE and 50.0% against HLE. An in vivo test was made alongside the in vitro test using an SEM 474 Cutometer (Courage & Khazaka) to study the elasticity of the skin, and positive effects were obtained when applying a cosmetic formulation containing 5% of the plant complex. Image analysis of duplicates of the cutaneous surface, before and after treatment began with a product containing 5% of plant complex and showed that wrinkles were decreased by 36.7%.
TGF-beta1 and Hyaluronan Oligomers Synergistically Enhance Elastin Matrix Regeneration by Vascular Smooth Muscle Cells.
Kothapalli CR, Taylor PM, Smolenski RT, Yacoub MH, Ramamurthi A.Clemson University-Medical University of South Carolina Bioengineering Program, Charleston, South Carolina. Tissue Eng Part A. 2008 Oct 10.
Elastin is a vital structural and regulatory matrix protein that plays an important role in conferring elasticity to blood vessel wall. Previous tissue engineering approaches to regenerate elastin in situ or within tissue engineering constructs are curtailed by innate poor elastin synthesis potential by adult vascular smooth muscle cells (SMCs). Currently, we seek to develop cellular cues to enhance tropoelastin synthesis and improve elastin matrix yield, stability, and ultrastructure. Our earlier studies attest to the elastogenic utility of hyaluronan (HA)-based cellular cues, though their effects are fragment size dependent and dose dependent, with HA oligomers deemed most elastogenic.
We presently show transforming growth factor beta 1 (TGF-beta1) and HA oligomers, when provided concurrently, to synergistically and dramatically improve elastin matrix regeneration by adult vascular SMCs. Together, these cues suppress SMC proliferation, enhance synthesis of tropoelastin (8-fold) and matrix elastin protein (5.5-fold), and also improve matrix elastin yield (45% of total elastin vs. 10% for nonadditive controls), possibly by more efficient recruitment of tropoelastin for crosslinking. The density of desmosine crosslinks within the elastin matrix was itself attenuated, although the cues together modestly increased production and activity of the elastin crosslinking enzyme, lysyl oxidase. TGF-beta1 and HA oligomers together induced much greater assembly of mature elastin fibers than they did separately, and did not induce matrix calcification. The present outcomes might be great utility to therapeutic regeneration of elastin matrix networks in situ within elastin-compromised vessels, and within tissue-engineered vascular graft replacements.
Collagen & Elastin