المؤلفون: Nathalie Scamuffa, Michiyo Okui, Maria Vazquez, Jun Kudoh, Stylianos E. Antonarakis, Kazunori Shibuya, Bernard C. Rossier, Marie Wattenhofer, Alexandre Reymond, Edith Hummler, Loretta Dougherty, Grégoire Vuagniaux, Elizabeth Guida, Colette Rossier, Manuela Hancock, Hamish S. Scott, Phillip L. Marzella, Karine Buchet, Nobuyoshi Shimizu, Michel Guipponi

المصدر: Scopus-Elsevier
Human Molecular Genetics, Vol. 11, No 23 (2002) pp. 2829-2836
Human Molecular Genetics, vol. 11, no. 23, pp. 2829-2836

مصطلحات موضوعية: Male, Epithelial sodium channel, Sodium Channels/ metabolism, Membrane Proteins/ genetics/ metabolism, DNA Mutational Analysis, RNA, Messenger/metabolism, Xenopus, Deafness, Neoplasm Proteins/ genetics/ metabolism, Endoplasmic Reticulum, Sodium Channels, Serine, Mice, Xenopus laevis, 0302 clinical medicine, Genes, Recessive/genetics, Spiral Ganglion/metabolism, Endoplasmic Reticulum/metabolism, Organ of Corti, In Situ Hybridization, Genetics (clinical), ddc:616, 0303 health sciences, Organ of Corti/metabolism, biology, Reverse Transcriptase Polymerase Chain Reaction, Serine Endopeptidases, Stria Vascularis, General Medicine, Transmembrane protein, Neoplasm Proteins, Protein Transport, medicine.anatomical_structure, DNA Primers/chemistry, Female, Rabbits, Spiral Ganglion, Proteases, Genotype, Mutation, Missense/ genetics, Blotting, Western, Mutation, Missense, Genes, Recessive, In Vitro Techniques, 03 medical and health sciences, Animals, Binding Sites, Deafness/genetics, Deafness/metabolism, Epithelial Sodium Channel, Humans, Membrane Proteins/genetics, Membrane Proteins/metabolism, Mutation, Missense/genetics, Neoplasm Proteins/genetics, Neoplasm Proteins/metabolism, Oocytes/metabolism, Rats, Serine Endopeptidases/genetics, Serine Endopeptidases/metabolism, Sodium Channels/metabolism, Stria Vascularis/metabolism, otorhinolaryngologic diseases, Genetics, medicine, RNA, Messenger, Serine Endopeptidases/ genetics/ metabolism, Epithelial Sodium Channels, Molecular Biology, DNA Primers, 030304 developmental biology, Serine protease, Endoplasmic reticulum, Membrane Proteins, biology.organism_classification, Molecular biology, Oocytes, biology.protein, Deafness/ genetics/metabolism, sense organs, 030217 neurology & neurosurgery

الوصف: TMPRSS3 encodes a transmembrane serine protease that contains both LDLRA and SRCR domains and is mutated in non-syndromic autosomal recessive deafness (DFNB8/10). To study its function, we cloned the mouse ortholog which maps to Mmu17, which is structurally similar to the human gene and encodes a polypeptide with 88% identity to the human protein. RT-PCR and RNA in situ hybridization on rat and mouse cochlea revealed that Tmprss3 is expressed in the spiral ganglion, the cells supporting the organ of Corti and the stria vascularis. RT-PCR on mouse tissues showed expression in the thymus, stomach, testis and E19 embryos. Transient expression of wild-type or tagged TMPRSS3 protein showed a primary localization in the endoplasmic reticulum. The epithelial amiloride-sensitive sodium channel (ENaC), which is expressed in many sodium-reabsorbing tissues including the inner ear and is regulated by membrane-bound channel activating serine proteases (CAPs), is a potential substrate of TMPRSS3. In the Xenopus oocyte expression system, proteolytic processing of TMPRSS3 was associated with increased ENaC mediated currents. In contrast, 6 TMPRSS3 mutants (D103G, R109W, C194F, W251C, P404L, C407R) causing deafness and a mutant in the catalytic triad of TMPRSS3 (S401A), failed to undergo proteolytic cleavage and activate ENaC. These data indicate that important signaling pathways in the inner ear are controlled by proteolytic cleavage and suggest: (i) the existence of an auto-catalytic processing by which TMPRSS3 would become active, and (ii) that ENaC could be a substrate of TMPRSS3 in the inner ear.

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::216a1dc433b46a41c8721058e7f2d04a
https://doi.org/10.1093/hmg/11.23.2829

المصدر: Developmental brain research, 126 (2

مستخلص: The immunolocalization of three members of the S100 calcium-binding protein family was investigated in the dog cochlea during normal postnatal development. Sections of decalcified and paraffin-embedded cochleae from 16 beagle puppies aged from birth to 3 months were treated with polyclonal antisera raised against the human recombinant S100A1, S100A5, and S100A6 proteins. At birth, in the dog cochlea, S100A1 was expressed in the immature Deiter's cells, and slightly in the pillar cells. From the second week, S100A1 was detected in the supporting structures of the organ of Corti, i.e. the Deiter's, the pillar, the border, and the Hensen's cells, and in the reticular membrane. From birth onwards, S100A5 remained a neuronal-specific protein, only located in a subpopulation of neurons in the spiral ganglion. S100A6 was not expressed at birth. From the second week of life, the Schwann cells and nerve sheaths in the modiolus, in the spiral ganglion, and running in the direction of the organ of Corti exhibited S100A6-labeling. From the 12th postnatal day, some scattered intermediate cells started to express S100A6 protein in the stria vascularis. The number of labeled intermediate cells increased during the third week. At adult stage, the intermediate cells were S100A6-stained with cytoplasmic labeling throughout the stria vascularis from the base to the apex of the cochlea. None of the other cochlear structures expressed the S100 proteins under study during the postnatal development of the dog cochlea. The S100A1, S100A5, S100A6 immunostaining was limited to specific cell types in dog cochlea. These S100 proteins were useful markers in the study of supporting cells, neurons, nerve fibers sheaths and stria vascularis (S100A6) during the normal postnatal development of the dog cochlea.
Journal Article
info:eu-repo/semantics/published

مصطلحات الفهرس: Sciences bio-médicales et agricoles, Animals, Animals, Newborn, Calcium-Binding Proteins -- metabolism, Cochlea -- cytology, Cochlea -- growth & development, Cochlea -- metabolism, Dogs, Female, Immunohistochemistry, Male, Organ Specificity, S100 Proteins -- metabolism, Spiral Ganglion -- cytology, Spiral Ganglion -- growth & development, Spiral Ganglion -- metabolism, Stria Vascularis -- cytology, Stria Vascularis -- metabolism, info:eu-repo/semantics/article, info:ulb-repo/semantics/articlePeerReview, info:ulb-repo/semantics/openurl/article

URL: http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/52443
http://worldcat.org/search?q=on:EQY+http://difusion-oai.ulb.ac.be/oai/request+DCG_ENTIRE_REPOSITORY+CNTCOLL

المصدر: Developmental brain research, 126 (2

مستخلص: The immunolocalization of three members of the S100 calcium-binding protein family was investigated in the dog cochlea during normal postnatal development. Sections of decalcified and paraffin-embedded cochleae from 16 beagle puppies aged from birth to 3 months were treated with polyclonal antisera raised against the human recombinant S100A1, S100A5, and S100A6 proteins. At birth, in the dog cochlea, S100A1 was expressed in the immature Deiter's cells, and slightly in the pillar cells. From the second week, S100A1 was detected in the supporting structures of the organ of Corti, i.e. the Deiter's, the pillar, the border, and the Hensen's cells, and in the reticular membrane. From birth onwards, S100A5 remained a neuronal-specific protein, only located in a subpopulation of neurons in the spiral ganglion. S100A6 was not expressed at birth. From the second week of life, the Schwann cells and nerve sheaths in the modiolus, in the spiral ganglion, and running in the direction of the organ of Corti exhibited S100A6-labeling. From the 12th postnatal day, some scattered intermediate cells started to express S100A6 protein in the stria vascularis. The number of labeled intermediate cells increased during the third week. At adult stage, the intermediate cells were S100A6-stained with cytoplasmic labeling throughout the stria vascularis from the base to the apex of the cochlea. None of the other cochlear structures expressed the S100 proteins under study during the postnatal development of the dog cochlea. The S100A1, S100A5, S100A6 immunostaining was limited to specific cell types in dog cochlea. These S100 proteins were useful markers in the study of supporting cells, neurons, nerve fibers sheaths and stria vascularis (S100A6) during the normal postnatal development of the dog cochlea.
Journal Article
info:eu-repo/semantics/published

مصطلحات الفهرس: Sciences bio-médicales et agricoles, Animals, Animals, Newborn, Calcium-Binding Proteins -- metabolism, Cochlea -- cytology, Cochlea -- growth & development, Cochlea -- metabolism, Dogs, Female, Immunohistochemistry, Male, Organ Specificity, S100 Proteins -- metabolism, Spiral Ganglion -- cytology, Spiral Ganglion -- growth & development, Spiral Ganglion -- metabolism, Stria Vascularis -- cytology, Stria Vascularis -- metabolism, info:eu-repo/semantics/article, info:ulb-repo/semantics/articlePeerReview, info:ulb-repo/semantics/openurl/article

URL: http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/52443
http://worldcat.org/search?q=on:EQY+http://difusion-oai.ulb.ac.be/oai/request+DCG_ENTIRE_REPOSITORY+CNTCOLL