Phagosome maturation during endosome interaction revealed by partial rhodopsin processing in retinal pigment epithelium

Detalhes bibliográficos
Autor(a) principal: Wavre-Shapton, Silène T
Data de Publicação: 2014
Outros Autores: Meschede, Ingrid P, Seabra, Miguel C, Futter, Clare E
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/21960
Resumo: Defects in phagocytosis and degradation of photoreceptor outer segments (POS) by the retinal pigment epithelium (RPE) are associated with aging and retinal disease. The daily burst of rod outer segment (ROS) phagocytosis by the RPE provides a unique opportunity to analyse phagosome processing in vivo. In mouse retinae, phagosomes containing stacked rhodopsin-rich discs were identified by immuno-electron microscopy. Early apical phagosomes stained with antibodies against both cytoplasmic and intradiscal domains of rhodopsin. During phagosome maturation, a remarkably synchronised loss of the cytoplasmic epitope coincided with movement to the cell body and preceded phagosome-lysosome fusion and disc degradation. Loss of the intradiscal rhodopsin epitope and disc digestion occurred upon fusion with cathepsin-D-positive lysosomes. The same sequential stages of phagosome maturation were identified in cultured RPE and macrophages challenged with isolated POS. Loss of the cytoplasmic rhodopsin epitope was insensitive to pH but sensitive to protease inhibition and coincided with the interaction of phagosomes with endosomes. Thus, during pre-lysosomal maturation of ROS-containing phagosomes, limited rhodopsin processing occurs upon interaction with endosomes. This potentially provides a sensitive readout of phagosome-endosome interactions that is applicable to multiple phagocytes.
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spelling Phagosome maturation during endosome interaction revealed by partial rhodopsin processing in retinal pigment epitheliumPHAGOCYTOSISRPEENDOCYTIC PATHWAYUSHER-SYNDROME 1BAGE-RELATED-CHANGESCELL BIOLOGYPHOSPHATIDYLINOSITOL 3-KINASERhodopsinCATHEPSIN-DROD OUTER SEGMENTSMDCK CELLSPhagosomeALPHA-V-BETA-5 INTEGRINRPEPhagosomeRhodopsinDefects in phagocytosis and degradation of photoreceptor outer segments (POS) by the retinal pigment epithelium (RPE) are associated with aging and retinal disease. The daily burst of rod outer segment (ROS) phagocytosis by the RPE provides a unique opportunity to analyse phagosome processing in vivo. In mouse retinae, phagosomes containing stacked rhodopsin-rich discs were identified by immuno-electron microscopy. Early apical phagosomes stained with antibodies against both cytoplasmic and intradiscal domains of rhodopsin. During phagosome maturation, a remarkably synchronised loss of the cytoplasmic epitope coincided with movement to the cell body and preceded phagosome-lysosome fusion and disc degradation. Loss of the intradiscal rhodopsin epitope and disc digestion occurred upon fusion with cathepsin-D-positive lysosomes. The same sequential stages of phagosome maturation were identified in cultured RPE and macrophages challenged with isolated POS. Loss of the cytoplasmic rhodopsin epitope was insensitive to pH but sensitive to protease inhibition and coincided with the interaction of phagosomes with endosomes. Thus, during pre-lysosomal maturation of ROS-containing phagosomes, limited rhodopsin processing occurs upon interaction with endosomes. This potentially provides a sensitive readout of phagosome-endosome interactions that is applicable to multiple phagocytes.Centro de Estudos de Doenças Crónicas (CEDOC)NOVA Medical School|Faculdade de Ciências Médicas (NMS|FCM)RUNWavre-Shapton, Silène TMeschede, Ingrid PSeabra, Miguel CFutter, Clare E2017-07-14T22:01:02Z2014-09-012014-09-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article10application/pdfhttp://hdl.handle.net/10362/21960eng0021-9533PURE: 398898https://doi.org/10.1242/jcs.154757info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-05-22T17:26:37Zoai:run.unl.pt:10362/21960Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-05-22T17:26:37Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Phagosome maturation during endosome interaction revealed by partial rhodopsin processing in retinal pigment epithelium
title Phagosome maturation during endosome interaction revealed by partial rhodopsin processing in retinal pigment epithelium
spellingShingle Phagosome maturation during endosome interaction revealed by partial rhodopsin processing in retinal pigment epithelium
Wavre-Shapton, Silène T
PHAGOCYTOSIS
RPE
ENDOCYTIC PATHWAY
USHER-SYNDROME 1B
AGE-RELATED-CHANGES
CELL BIOLOGY
PHOSPHATIDYLINOSITOL 3-KINASE
Rhodopsin
CATHEPSIN-D
ROD OUTER SEGMENTS
MDCK CELLS
Phagosome
ALPHA-V-BETA-5 INTEGRIN
RPE
Phagosome
Rhodopsin
title_short Phagosome maturation during endosome interaction revealed by partial rhodopsin processing in retinal pigment epithelium
title_full Phagosome maturation during endosome interaction revealed by partial rhodopsin processing in retinal pigment epithelium
title_fullStr Phagosome maturation during endosome interaction revealed by partial rhodopsin processing in retinal pigment epithelium
title_full_unstemmed Phagosome maturation during endosome interaction revealed by partial rhodopsin processing in retinal pigment epithelium
title_sort Phagosome maturation during endosome interaction revealed by partial rhodopsin processing in retinal pigment epithelium
author Wavre-Shapton, Silène T
author_facet Wavre-Shapton, Silène T
Meschede, Ingrid P
Seabra, Miguel C
Futter, Clare E
author_role author
author2 Meschede, Ingrid P
Seabra, Miguel C
Futter, Clare E
author2_role author
author
author
dc.contributor.none.fl_str_mv Centro de Estudos de Doenças Crónicas (CEDOC)
NOVA Medical School|Faculdade de Ciências Médicas (NMS|FCM)
RUN
dc.contributor.author.fl_str_mv Wavre-Shapton, Silène T
Meschede, Ingrid P
Seabra, Miguel C
Futter, Clare E
dc.subject.por.fl_str_mv PHAGOCYTOSIS
RPE
ENDOCYTIC PATHWAY
USHER-SYNDROME 1B
AGE-RELATED-CHANGES
CELL BIOLOGY
PHOSPHATIDYLINOSITOL 3-KINASE
Rhodopsin
CATHEPSIN-D
ROD OUTER SEGMENTS
MDCK CELLS
Phagosome
ALPHA-V-BETA-5 INTEGRIN
RPE
Phagosome
Rhodopsin
topic PHAGOCYTOSIS
RPE
ENDOCYTIC PATHWAY
USHER-SYNDROME 1B
AGE-RELATED-CHANGES
CELL BIOLOGY
PHOSPHATIDYLINOSITOL 3-KINASE
Rhodopsin
CATHEPSIN-D
ROD OUTER SEGMENTS
MDCK CELLS
Phagosome
ALPHA-V-BETA-5 INTEGRIN
RPE
Phagosome
Rhodopsin
description Defects in phagocytosis and degradation of photoreceptor outer segments (POS) by the retinal pigment epithelium (RPE) are associated with aging and retinal disease. The daily burst of rod outer segment (ROS) phagocytosis by the RPE provides a unique opportunity to analyse phagosome processing in vivo. In mouse retinae, phagosomes containing stacked rhodopsin-rich discs were identified by immuno-electron microscopy. Early apical phagosomes stained with antibodies against both cytoplasmic and intradiscal domains of rhodopsin. During phagosome maturation, a remarkably synchronised loss of the cytoplasmic epitope coincided with movement to the cell body and preceded phagosome-lysosome fusion and disc degradation. Loss of the intradiscal rhodopsin epitope and disc digestion occurred upon fusion with cathepsin-D-positive lysosomes. The same sequential stages of phagosome maturation were identified in cultured RPE and macrophages challenged with isolated POS. Loss of the cytoplasmic rhodopsin epitope was insensitive to pH but sensitive to protease inhibition and coincided with the interaction of phagosomes with endosomes. Thus, during pre-lysosomal maturation of ROS-containing phagosomes, limited rhodopsin processing occurs upon interaction with endosomes. This potentially provides a sensitive readout of phagosome-endosome interactions that is applicable to multiple phagocytes.
publishDate 2014
dc.date.none.fl_str_mv 2014-09-01
2014-09-01T00:00:00Z
2017-07-14T22:01:02Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10362/21960
url http://hdl.handle.net/10362/21960
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0021-9533
PURE: 398898
https://doi.org/10.1242/jcs.154757
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 10
application/pdf
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv mluisa.alvim@gmail.com
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