Distribution of peptidyl-glycine α-amidating mono-oxygenase (PAM) enzymes in normal human lung and in lung epithelial tumors
C-terminal α-amidation is a post-translational modification necessary for the biological activity of many regulatory peptides produced in the respiratory tract. This modification is a two-step process catalyzed by two separate enzyme activities, both derived from the peptidyl-glycine α- amidating mo...
| Autores: | , , , , , , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 1996 |
| País: | España |
| Institución: | Universidad de La Rioja (UR) |
| Repositorio: | RIUR. Repositorio Institucional de la Universidad de La Rioja |
| OAI Identifier: | oai:portal.dialnet.es:doc/5d31a3a02999521056385011 |
| Acceso en línea: | https://investigacion.unirioja.es/documentos/5d31a3a02999521056385011 |
| Access Level: | acceso abierto |
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Distribution of peptidyl-glycine α-amidating mono-oxygenase (PAM) enzymes in normal human lung and in lung epithelial tumorsSaldise, LauraMartínez, Alfredo [0000-0003-4882-4044]Montuenga, Luis M. [0000-0002-8739-1387]Treston, AnthonySpringall, David R.Polak, Julia M.Vázquez, Jesús J.C-terminal α-amidation is a post-translational modification necessary for the biological activity of many regulatory peptides produced in the respiratory tract. This modification is a two-step process catalyzed by two separate enzyme activities, both derived from the peptidyl-glycine α- amidating mono-oxygenase (PAM) precursor. The distribution of these two enzymes, peptidyl-glycine α-hydroxylating monooxygenase (PHM) and peptidyl- α-hydroxyglycine α-amidating lyase (PAL), was studied in the normal lung and in lung tumors using immunocytochemical methods and in situ hybridization. In normal lung the enzymes were located in some cells of the airway epithelium and glands, the endothelium of blood vessels, some chondrocytes of the bronchial cartilage, the alveolar macrophages, smooth muscle cells, neurons of the intrinsic ganglia, and in myelinated nerves. A total of 24 lung tumors of seven different histological types were studied. All cases contained PAM-immunoreactive cells with various patterns of distribution. All immunoreactive cells were positive for the PHM antiserum but only some of them for the PAL antiserum. The distribution of PAM co- localizes with some other previously described amidated peptides, suggesting that amidation is an important physiological process taking place in the normal and malignant human lung tissue.Histochemical Society Inc.1996info:eu-repo/semantics/articleSubtype: Articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://investigacion.unirioja.es/documentos/5d31a3a02999521056385011reponame:RIUR. Repositorio Institucional de la Universidad de La Riojainstname:Universidad de La Rioja (UR)Inglésinfo:eu-repo/semantics/altIdentifier/doi/10.1177/44.1.8543779info:eu-repo/semantics/altIdentifier/pmid/8543779info:eu-repo/semantics/altIdentifier/pissn/0022-1554Distribution of peptidyl-glycine α-amidating mono-oxygenase (PAM) enzymes in normal human lung and in lung epithelial tumors, 1996, vol. 44, núm. 1, pág. 3-12info:eu-repo/semantics/openAccessoai:portal.dialnet.es:doc/5d31a3a029995210563850112026-06-14T12:47:17Z |
| dc.title.none.fl_str_mv |
Distribution of peptidyl-glycine α-amidating mono-oxygenase (PAM) enzymes in normal human lung and in lung epithelial tumors |
| title |
Distribution of peptidyl-glycine α-amidating mono-oxygenase (PAM) enzymes in normal human lung and in lung epithelial tumors |
| spellingShingle |
Distribution of peptidyl-glycine α-amidating mono-oxygenase (PAM) enzymes in normal human lung and in lung epithelial tumors Saldise, Laura |
| title_short |
Distribution of peptidyl-glycine α-amidating mono-oxygenase (PAM) enzymes in normal human lung and in lung epithelial tumors |
| title_full |
Distribution of peptidyl-glycine α-amidating mono-oxygenase (PAM) enzymes in normal human lung and in lung epithelial tumors |
| title_fullStr |
Distribution of peptidyl-glycine α-amidating mono-oxygenase (PAM) enzymes in normal human lung and in lung epithelial tumors |
| title_full_unstemmed |
Distribution of peptidyl-glycine α-amidating mono-oxygenase (PAM) enzymes in normal human lung and in lung epithelial tumors |
| title_sort |
Distribution of peptidyl-glycine α-amidating mono-oxygenase (PAM) enzymes in normal human lung and in lung epithelial tumors |
| dc.creator.none.fl_str_mv |
Saldise, Laura Martínez, Alfredo [0000-0003-4882-4044] Montuenga, Luis M. [0000-0002-8739-1387] Treston, Anthony Springall, David R. Polak, Julia M. Vázquez, Jesús J. |
| author |
Saldise, Laura |
| author_facet |
Saldise, Laura Martínez, Alfredo [0000-0003-4882-4044] Montuenga, Luis M. [0000-0002-8739-1387] Treston, Anthony Springall, David R. Polak, Julia M. Vázquez, Jesús J. |
| author_role |
author |
| author2 |
Martínez, Alfredo [0000-0003-4882-4044] Montuenga, Luis M. [0000-0002-8739-1387] Treston, Anthony Springall, David R. Polak, Julia M. Vázquez, Jesús J. |
| author2_role |
author author author author author author |
| description |
C-terminal α-amidation is a post-translational modification necessary for the biological activity of many regulatory peptides produced in the respiratory tract. This modification is a two-step process catalyzed by two separate enzyme activities, both derived from the peptidyl-glycine α- amidating mono-oxygenase (PAM) precursor. The distribution of these two enzymes, peptidyl-glycine α-hydroxylating monooxygenase (PHM) and peptidyl- α-hydroxyglycine α-amidating lyase (PAL), was studied in the normal lung and in lung tumors using immunocytochemical methods and in situ hybridization. In normal lung the enzymes were located in some cells of the airway epithelium and glands, the endothelium of blood vessels, some chondrocytes of the bronchial cartilage, the alveolar macrophages, smooth muscle cells, neurons of the intrinsic ganglia, and in myelinated nerves. A total of 24 lung tumors of seven different histological types were studied. All cases contained PAM-immunoreactive cells with various patterns of distribution. All immunoreactive cells were positive for the PHM antiserum but only some of them for the PAL antiserum. The distribution of PAM co- localizes with some other previously described amidated peptides, suggesting that amidation is an important physiological process taking place in the normal and malignant human lung tissue. |
| publishDate |
1996 |
| dc.date.none.fl_str_mv |
1996 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article Subtype: Article info:eu-repo/semantics/publishedVersion |
| format |
article |
| status_str |
publishedVersion |
| dc.identifier.none.fl_str_mv |
https://investigacion.unirioja.es/documentos/5d31a3a02999521056385011 |
| url |
https://investigacion.unirioja.es/documentos/5d31a3a02999521056385011 |
| dc.language.none.fl_str_mv |
Inglés |
| language_invalid_str_mv |
Inglés |
| dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1177/44.1.8543779 info:eu-repo/semantics/altIdentifier/pmid/8543779 info:eu-repo/semantics/altIdentifier/pissn/0022-1554 Distribution of peptidyl-glycine α-amidating mono-oxygenase (PAM) enzymes in normal human lung and in lung epithelial tumors, 1996, vol. 44, núm. 1, pág. 3-12 |
| dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess |
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openAccess |
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application/pdf |
| dc.publisher.none.fl_str_mv |
Histochemical Society Inc. |
| publisher.none.fl_str_mv |
Histochemical Society Inc. |
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reponame:RIUR. Repositorio Institucional de la Universidad de La Rioja instname:Universidad de La Rioja (UR) |
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Universidad de La Rioja (UR) |
| reponame_str |
RIUR. Repositorio Institucional de la Universidad de La Rioja |
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RIUR. Repositorio Institucional de la Universidad de La Rioja |
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1869425130306797568 |
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15,300719 |