Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Emeline Puissant"'
Autor:
Emeline Puissant, Florentine Gilis, Virginie Tevel, Jean-Michel Vandeweerd, Bruno Flamion, Michel Jadot, Marielle Boonen
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-13 (2022)
Abstract Mucopolysaccharidosis IX is a lysosomal storage disorder caused by a deficiency in HYAL1, an enzyme that degrades hyaluronic acid at acidic pH. This disease causes juvenile arthritis in humans and osteoarthritis in the Hyal1 knockout mouse m
Externí odkaz:
https://doaj.org/article/03c97d9d9aa14651bd6e8ca906f12b2b
Autor:
Emeline Puissant, Marielle Boonen
Publikováno v:
PLoS ONE, Vol 11, Iss 10, p e0165004 (2016)
Osteoclasts are giant bone-resorbing cells originating from monocytes/macrophages. During their differentiation, they overexpress two lysosomal enzymes, cathepsin K and TRAP, which are secreted into the resorption lacuna, an acidified sealed area in
Externí odkaz:
https://doaj.org/article/9a289fd8092b43f7923ff4bda700a37f
Autor:
Emeline Puissant, Florentine Gilis, Virginie Tevel, Jean-Michel Vandeweerd, Bruno Flamion, Michel Jadot, Marielle Boonen
Publikováno v:
Puissant, E, Gilis, F, Tevel, V, Vandeweerd, J-M, Flamion, B, Jadot, M & Boonen, M 2022, ' Hyaluronidase 1 deficiency decreases bone mineral density in mice ', Scientific Reports, vol. 12, no. 1, 10142 . https://doi.org/10.1038/s41598-022-14473-7
Mucopolysaccharidosis IX is a lysosomal storage disorder caused by a deficiency in HYAL1, an enzyme that degrades hyaluronic acid at acidic pH. This disease causes juvenile arthritis in humans and osteoarthritis in the Hyal1 knockout mouse model. Our
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::204df93bf1c7a4b2e647ee5fa4b95e3f
https://pubmed.ncbi.nlm.nih.gov/35710820
https://pubmed.ncbi.nlm.nih.gov/35710820
Autor:
Sophie Dogné, Florentine Gilis, Marielle Boonen, Bruno Flamion, Emeline Puissant, Michel Jadot
Publikováno v:
Traffic. 15:500-515
The hyaluronidase Hyal-1 is an acid hydrolase that degrades hyaluronic acid (HA), a component of the extracellular matrix. It is often designated as a lysosomal protein. Yet few data are available on its intracellular localization and trafficking. We
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bc3ddd75dfc302bc211c82a8da2df34a
https://doi.org/10.1111/tra.12162
https://doi.org/10.1111/tra.12162
Publikováno v:
Biochemical and biophysical research communications. 446(4)
It has long been known that liver lysosomes contain an endoglycosidase activity able to degrade the high molecular mass glycosaminoglycan hyaluronic acid (HA). The identification and cloning of a hyaluronidase with an acidic pH optimum, Hyal-1, sugge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44c60345fb6d0ad5dcdc753620847fc4
https://pubmed.ncbi.nlm.nih.gov/24667601
https://pubmed.ncbi.nlm.nih.gov/24667601
Autor:
Emeline, Puissant, Florentine, Gilis, Sophie, Dogné, Bruno, Flamion, Michel, Jadot, Marielle, Boonen
Publikováno v:
Traffic (Copenhagen, Denmark). 15(5)
The hyaluronidase Hyal-1 is an acid hydrolase that degrades hyaluronic acid (HA), a component of the extracellular matrix. It is often designated as a lysosomal protein. Yet few data are available on its intracellular localization and trafficking. We
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::56f92193b194c41befa618328cfc212b
https://pubmed.ncbi.nlm.nih.gov/24502338
https://pubmed.ncbi.nlm.nih.gov/24502338
Publikováno v:
International Journal of Molecular Sciences, Vol 18, Iss 1, p 47 (2016)
International Journal of Molecular Sciences
Staudt, C, Puissant, E & Boonen, M 2017, ' Subcellular trafficking of mammalian lysosomal proteins : An extended view ', International Journal of Molecular Sciences, vol. 18, no. 1, 47 . https://doi.org/10.3390/ijms18010047
International Journal of Molecular Sciences
Staudt, C, Puissant, E & Boonen, M 2017, ' Subcellular trafficking of mammalian lysosomal proteins : An extended view ', International Journal of Molecular Sciences, vol. 18, no. 1, 47 . https://doi.org/10.3390/ijms18010047
Lysosomes clear macromolecules, maintain nutrient and cholesterol homeostasis, participate in tissue repair, and in many other cellular functions. To assume these tasks, lysosomes rely on their large arsenal of acid hydrolases, transmembrane proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7796f7d5d9b3964dda9809cb374bb91
https://doi.org/10.3390/ijms18010047
https://doi.org/10.3390/ijms18010047