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Human Neutrophil Elastase (human + neutrophil_elastase)

Distribution by Scientific Domains

Medical Sciences	50%

Selected Abstracts

Inhibition of elastase activity by essential oils in vitro

JOURNAL OF COSMETIC DERMATOLOGY, Issue 4 2002
Masahiro Mori
Summary, Background, Essential oils are widely used, for example in aromatherapy and aroma massage. In aroma massage, essential oil, diluted with vegetable oil, is rubbed onto the skin. Components of essential oil penetrate into the skin and have an influence on the dermis. Elastase is an enzyme which degenerates dermal elastin. Elastase activity is believed to contribute to cutaneous wrinkling and ageing. Aim, To investigate the inhibitory effect of essential oils on elastase activity. Methods, Inhibition of elastase activity by various essential oils was assessed using two elastase enzymes: porcine pancreatic elastase (PPE) and human neutrophil elastase (HNE). Results, Elastase activity was inhibited by various essential oils, especially by those oils derived from lemons, juniper and grapefruit. Although the specific inhibitory component was not determined, lemon oil had the greatest inhibitory effect on PPE. Some essential oils also inhibited HNE. Conclusions, These studies demonstrate a possible rationale for the use of essential oil massage as a preventive treatment for cutaneous wrinkling and ageing. [source]

A peptide from thrombospondin 1 modulates experimental erosive arthritis by regulating connective tissue growth factor

ARTHRITIS & RHEUMATISM, Issue 8 2006
Joanne M. Manns
Objective Rheumatoid arthritis (RA) is a chronic inflammatory disease associated with leukocyte adhesion to and extravasation through vascular endothelium into synovial tissue. Recent evidence indicates that the thrombospondin 1 gene is up-regulated in patients with RA. We have identified a region within the TSP-1 type 3 repeats that inhibits human neutrophil elastase (HNE) and binds to human neutrophils. The present study was undertaken to investigate the therapeutic benefit of this TSP-1,derived peptide sequence and its effect on connective tissue growth factor (CTGF), a protein involved in fibrotic disorders and in neovascularization, which is a hallmark of RA. Methods CTGF gene and protein expression, as well as protein levels of CTGF in the synovium, after treatment with the TSP-1,derived peptide were studied in the peptidoglycan,polysaccharide animal model of erosive arthritis. Results Peptide treatment prevented joint infiltration and inflammation and was associated with reduced circulating antigen levels of HNE and TSP-1. Additionally, CTGF was up-regulated in this experimental model of RA. Treatment with the TSP-1,derived peptide was associated with down-regulation of the message and protein levels of CTGF. Immunofluorescence studies showed that the mean area fraction of CTGF immunoreactivity in the peptide-treated group of animals was significantly less than that in the untreated group. Conclusion These results document a role for TSP-1 in regulating CTGF gene and protein expression in synovial tissue, suggesting a link with the disease course in this model of RA. This TSP-1,derived synthetic peptide may represent an important template for drug development in RA and other inflammatory conditions associated with neutrophil activation. [source]

Detection of human neutrophil elastase with peptide-bound cross-linked ethoxylate acrylate resin analogs

CHEMICAL BIOLOGY & DRUG DESIGN, Issue 4 2005
J.V. Edwards
Abstract:, An assessment of elastase-substrate kinetics and adsorption at the solid,liquid interface of peptide-bound resin was made in an approach to the solid-phase detection of human neutrophil elastase (HNE), which is found in high concentration in chronic wound fluid. N-succinyl-alanine-alanine-proline-valine- p -nitroanilide (suc-Ala-Ala-Pro-Val- pNA), a chromogenic HNE substrate, was attached to glycine-cross-linked ethoxylate acrylate resins (Gly-CLEAR) by a carbodiimide reaction. To assess the enzyme-substrate reaction in a two-phase system, the kinetic profile of resin-bound peptide substrate hydrolysis by HNE was obtained. A glycine and di-glycine spacer was placed between the resin polymer and substrate to assess the steric and spatial requirements of resin to substrate with enzyme hydrolysis. The enzymatic activities of suc-Ala-Ala-Pro-Val- pNA and suc-Ala-Ala-Pro-Ala- pNA on the solid-phase resin were compared with similar analogs in solution. An increase in visible wavelength absorbance was observed with increasing amounts of substrate-resin and enzyme concentration. Enzyme hydrolysis of the resin-bound substrate was also demonstrated on a polypropylene surface, which was employed for visible absorbance of released chromophore. A soluble active substrate analog was released from the resin through saponification of the ethoxylate ester linkages in the resin polymer. The resin-released conjugate of the HNE substrate demonstrated an increased dose response with increasing enzyme concentration. The synthesis and assay of elastase substrates bound to CLEAR resin gives an understanding of substrate-elastase adsorption and activity at the resin's solid,liquid interface for HNE detection with a solid-phase peptide. [source]