A unique network of attack, defence and competence on the outer membrane of the periodontitis pathogen Tannerella forsythia

Autor: Mirosław Książek, Theodoros Goulas, Danuta Mizgalska, Arturo Rodríguez-Banqueri, Ulrich Eckhard, Florian Veillard, Irena Waligórska, Małgorzata Benedyk-Machaczka, Alicja M. Sochaj-Gregorczyk, Mariusz Madej, Ida B. Thøgersen, Jan J. Enghild, Anna Cuppari, Joan L. Arolas, Iñaki de Diego, Mar López-Pelegrín, Irene Garcia-Ferrer, Tibisay Guevara, Vincent Dive, Marie-Louise Zani, Thierry Moreau, Jan Potempa, F. Xavier Gomis-Rüth

Publikováno v: Chemical Science
Chemical Science, 2023, 14 (4), pp.869-888. ⟨10.1039/d2sc04166a⟩
Książek, M, Goulas, T, Mizgalska, D, Rodríguez-Banqueri, A, Eckhard, U, Veillard, F, Waligórska, I, Benedyk-Machaczka, M, Sochaj-Gregorczyk, A M, Madej, M, Thøgersen, I B, Enghild, J J, Cuppari, A, Arolas, J L, de Diego, I, López-Pelegrín, M, Garcia-Ferrer, I, Guevara, T, Dive, V, Zani, M L, Moreau, T, Potempa, J & Gomis-Rüth, F X 2023, ' A unique network of attack, defence and competence on the outer membrane of the periodontitis pathogen Tannerella forsythia ', Chemical Science, vol. 14, no. 4, pp. 869-888 . https://doi.org/10.1039/d2sc04166a

Periodontopathogenic Tannerella forsythia uniquely secretes six peptidases of disparate catalytic classes and families that operate as virulence factors during infection of the gums, the KLIKK-peptidases. Their coding genes are immediately downstream

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7698e6876d479a7bef16c93ae86818e9
https://ruj.uj.edu.pl/xmlui/handle/item/308078

A Functional Variant of Elafin With Improved Anti-inflammatory Activity for Pulmonary Inflammation

Autor: Clifford C. Taggart, Sinéad Weldon, Thierry Moreau, Arlene Glasgow, Cecilia O'Kane, Derek J. Quinn, Paul McNally, Daniel F. McAuley, Sandrine Dallet-Choisy, Donna M. Small, Marie Louise Zani

Publikováno v: Small, D M, Zani, M L, Quinn, D J, Dallet-Choisy, S, Glasgow, A MA, O'Kane, C, Mcauley, D F, Mcnally, P, Weldon, S, Moreau, T & Taggart, C C 2015, ' A Functional Variant of Elafin With Improved Anti-inflammatory Activity for Pulmonary Inflammation ', Molecular therapy : the journal of the American Society of Gene Therapy, vol. 23, no. 1, pp. 24-31 . https://doi.org/10.1038/mt.2014.162

Elafin is a serine protease inhibitor produced by epithelial and immune cells with anti-inflammatory properties. Research has shown that dysregulated protease activity may elicit proteolytic cleavage of elafin, thereby impairing the innate immune fun

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fca2bcf636e5ba73dea7e8f8bae8ec50
https://doi.org/10.1038/mt.2014.162

Protection of lung epithelial cells from protease-mediated injury by trappin-2 A62L, an engineered inhibitor of neutrophil serine proteases

Autor: Marie-Lise Jourdan, Ahlame Saidi, Thierry Moreau, Annabelle Tanga, Marie-Louise Zani, Sandrine Dallet-Choisy

Publikováno v: Biochemical Pharmacology. 83:1663-1673

Neutrophil serine proteases (NSPs), including elastase, proteinase 3 and cathepsin G, play critical roles in the pathogenesis of chronic inflammatory lung diseases. The release of excess NSPs leads to the destruction of lung tissue and an overexubera

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1db21edf74932acb14a6762677c817f7
https://doi.org/10.1016/j.bcp.2012.03.009

Oxidized elafin and trappin poorly inhibit the elastolytic activity of neutrophil elastase and proteinase 3

Autor: Christian Boudier, Joseph G. Bieth, Shila M. Nobar, Thierry Moreau, Marie-Louise Zani

Publikováno v: FEBS Journal. 272:5883-5893

Neutrophil proteinase-mediated lung tissue destruction is prevented by inhibitors, including elafin and its precursor, trappin. We wanted to establish whether neutrophil-derived oxidants might impair the inhibitory function of these molecules. Myelop

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6d1f6d6610890e0c81b00fefa38a95be
https://doi.org/10.1111/j.1742-4658.2005.04988.x

SLPI and trappin-2 as therapeutic agents to target airway serine proteases in inflammatory lung diseases: current and future directions

Autor: Thierry Moreau, Annabelle Tanga, Marie-Louise Zani, Sandrine Dallet-Choisy, Ahlame Saidi, Kévin Baranger, Hélène Serrano

Publikováno v: Biochemical Society transactions. 39(5)

It is now clear that NSPs (neutrophil serine proteases), including elastase, Pr3 (proteinase 3) and CatG (cathepsin G) are major pathogenic determinants in chronic inflammatory disorders of the lungs. Two unglycosylated natural protease inhibitors, S

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1dcaf1cf6b330e90fc24e70b19909eda
https://pubmed.ncbi.nlm.nih.gov/21936830