elastin and Hemolysis

Glutaraldehyde (GA) crosslinked bovine or porcine pericardium tissues exhibit high cell toxicity and calcification in the construction of bioprosthetic valves, which accelerate the failure of valve leaflets and motivate the exploration for alternatives. Polyphenols, including curcumin, procyanidin and quercetin, etc, have showed great calcification inhibition potential in crosslinking collagen and elastin scaffolds. Herein, we developed an innovative phenolic fixing technique by using curcumin as the crosslinking reagent for valvular materials. X-ray photoelectron spectroscopy and Fourier transform infrared spectrometry assessments confirmed the hydrogen bond between curcumin and acellular bovine pericardium. Importantly, the calcification inhibition capability of the curcumin-crosslinked bovine pericardium was proved by the dramatically reduced Ca

Topics: Animals; Bioprosthesis; Calcification, Physiologic; Cattle; Collagen; Cross-Linking Reagents; Curcumin; Elastin; Glutaral; Heart Valve Diseases; Heart Valve Prosthesis; Heart Valves; Hemolysis; Human Umbilical Vein Endothelial Cells; Humans; Hydrogen Bonding; In Vitro Techniques; Materials Testing; Osteogenesis; Pericardium; Phenol; Photoelectron Spectroscopy; Rats; Rats, Wistar; Spectroscopy, Fourier Transform Infrared; Stress, Mechanical; Thermodynamics

The present isolation and identification of napthoquinones from roots of Arnebia nobilis Reichb.f. can lead to the discovery of new anti-skin ageing ingredient in colour cosmetics. Four compounds have been isolated and purified by rigorous column chromatography. The compounds are identified as β, β-dimethylacryl alkannin (AN-I), acetoxyisovaleryl alkannin (AAN-II), acetyl alkannin (AN-III) and alkannin (AN-IV) by interpretation of spectroscopic data. This study is the first to report the isolation of Acetoxyisovaleryl alkannin (AAN-II) from A. nobilis. The IC50 values of the compounds, determined in human skin cells (human dermal fibroblasts and human keratinocytes) and mouse embryonic fibroblasts (NIH3T3) varied significantly among the four alkannins. Among the four compounds, β-acetoxyisovaleryl alkannin (AAN-II) significantly inhibited hydrogen peroxide (H2O2)-induced red blood corpuscle haemolysis and cellular senescence in human dermal fibroblasts. Collagen-I, elastin and involucrin syntheses in human dermal fibroblasts or keratinocytes were up regulated by AAN-II. These results support the potential utility of alkannins as novel anti-ageing ingredients.

Topics: Animals; Boraginaceae; Cellular Senescence; Collagen Type I; Cosmetics; Elastin; Fibroblasts; Hemolysis; Humans; Hydrogen Peroxide; Keratinocytes; Mice; Naphthoquinones; NIH 3T3 Cells; Plant Roots; Protein Precursors; Skin Aging; Up-Regulation

Elastin, a main component of decellularized extracellular matrices and elastin-containing materials, has been used for tissue engineering applications due to their excellent biocompatibility. However, elastin is easily calcified, leading to the decrease of life span for elastin-based substitutes. How to inhibit the calcification of elastin-based scaffolds, but maintain their good biocompatibility, still remains significantly challenging. Procyanidins (PC) are a type of natural polyphenols with crosslinking ability. To investigate whether pure elastin could be crosslinked by PC with anti-calcification effect, PC was first used to crosslink aortic elastin. Results show that PC can crosslink elastin and effectively inhibit elastin-initiated calcification. Further experiments reveal the possible mechanisms for the anti-calcification of PC crosslinking including (1) inhibiting inflammation cell attachment, and secretion of inflammatory factors such as MMPs and TNF-α, (2) preventing elastin degradation by elastase, and (3) direct inhibition of mineral nucleation in elastin. Moreover, the PC-crosslinked aortic elastin maintains natural structure with high pore volume (1111 μL/g), large pore size (10-300 μm) and high porosity (75.1%) which facilitates recellularization of scaffolds in vivo, and displays excellent hemocompatibility, anti-thrombus and anti-inflammatory potential. The advantages of PC-crosslinked porous aortic elastin suggested that it can serve as a promising scaffold for tissue engineering.

Topics: Animals; Aorta; Biflavonoids; Blood Coagulation; Calcification, Physiologic; Catechin; Cell Adhesion; Cell Line; Cross-Linking Reagents; Elastin; Glutaral; Heart Valves; Hemolysis; Humans; Macrophages; Matrix Metalloproteinase 12; Minerals; Pancreatic Elastase; Platelet Adhesiveness; Porosity; Proanthocyanidins; Proteolysis; Rats, Sprague-Dawley; Staining and Labeling; Sus scrofa; Tissue Scaffolds

Parvimonas micra are gram positive anaerobic cocci isolated from the oral cavity and frequently related to polymicrobial infections in humans. Despite reports about phenotypic differences, the genotypic variation of P. micra and its role in virulence are still not elucidated. The aim of this study was to determine the genotypic diversity of P. micra isolates obtained from the subgingival biofilm of subjects with different periodontal conditions and to correlate these findings with phenotypic traits. Three reference strains and 35 isolates of P. micra were genotyped by 16S rRNA PCR-RFLP and phenotypic traits such as collagenase production, elastolytic and hemolytic activities were evaluated. 16S rRNA PCR-RFLP showed that P. micra could be grouped into two main clusters: C1 and C2; cluster C1 harbored three genotypes (HG1259-like, HG1467-like and ICBMO583-like) while cluster C2 harbored two genotypes (ATCC33270-like and ICBMO36). A wide variability in collagenolytic activity intensities was observed among all isolates, while elastolytic activity was detected in only two isolates. There was an association between hemolytic activity in rabbit erythrocytes and cluster C2. There was an association between hemolytic activity in rabbit erythrocytes and cluster C1. Although these data suggest a possible association between P. micra genetic diversity and their pathogenic potential, further investigations are needed to confirm this hypothesis.

Topics: Animals; Biodiversity; Cluster Analysis; Collagenases; DNA Fingerprinting; DNA, Bacterial; DNA, Ribosomal; Elastin; Erythrocytes; Genotype; Gingiva; Gram-Positive Bacteria; Hemolysis; Humans; Periodontal Diseases; Polymorphism, Restriction Fragment Length; Rabbits; RNA, Ribosomal, 16S

Collagens from various vertebrate tissues were tested for their ability to consume complement (C) activity upon incubation in human serum or with isolated components of complement. 10 of 12 collagens tested had anticomplementary activity. The heat-denatured form of collagen, gelatin, was found weakly anticomplementary, but elastin was found inactive in the interaction with C. Inactivation of C is a reaction which is dependent on the time of incubation and the collagen concentration and partially dependent on the temperature of incubation. Most collagens depleted C from human serum in presence of cation chelators, EDTA and EGTA, whereas the large part of anticomplementary activity of soluble collagens obtained from rat skin was abolished in presence of EDTA. Evidence is presented that two different principles in collagens play a role in inactivation of C. A factor, contained in insoluble collagens and inhibitable by mild oxidation with periodate, inactivates C1 directly even in presence of chelating agents. Another principle, contained in soluble and insoluble collagen and resistant to periodate treatment, depletes C in serum by utilization of C via the alternate pathway (the C3 shunt).

Topics: Animals; Cattle; Chick Embryo; Collagen; Complement C1; Complement C2; Complement C3; Complement System Proteins; Edetic Acid; Egtazic Acid; Elastin; Gelatin; Hemolysis; Immune Adherence Reaction; Immunoelectrophoresis; Male; Periodic Acid; Rats; Skin; Solubility; Temperature; Tendons