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Registro completo
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Biblioteca (s) : |
INIA La Estanzuela. |
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Fecha : |
02/03/2017 |
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Actualizado : |
26/02/2019 |
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Autor : |
GAFFNEY PM; BARR, B.; ROWE, J.D.; BETT, C.; DRYGIANNAKIS, I.; GIANNITTI, F.; TREJO, M.; GHASSEMIAN ,M.; MASLIAH, E.; SIGURDSON, C.J. |
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Afiliación : |
FEDERICO GIANNITTI, INIA (Instituto Nacional de Investigación Agropecuaria), Uruguay. |
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Título : |
Protein profiling of isolated uterine AA amyloidosis causing fetal death in goats. |
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Fecha de publicación : |
2015 |
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Fuente / Imprenta : |
The FASEB Journal, 2015, v. 29, n.3, p.911-919. |
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DOI : |
10.1096/fj.14-256081 |
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Idioma : |
Inglés |
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Contenido : |
ABSTRACT Pathologic amyloid accumulates in theCNS or in peripheral organs, yet the mechanism underlying the
targeting of systemic amyloid deposits is unclear. Serum amyloid A (SAA) 1 and 2 are produced predominantly by
the liver and form amyloid most commonly in the spleen, liver, and kidney. In contrast, SAA3 is produced primarily
extrahepatically and has no causal link to amyloid formation. Here, we identified 8 amyloidosis cases with amyloid
composed of SAA3 expanding the uterine wall of goats with near-term fetuses. Uterine amyloid accumulated in
the endometrium, only at the site of placental attachment,compromising maternal-fetal gas and nutrient exchange
and leading to fetal ischemia and death. No other organ contained amyloid. SAA3 mRNA levels in the uterine endometrium
were as high as SAA2 in the liver, yet mass spectrometry of the insoluble uterine peptides identified
SAA3 as the predominant protein, and not SAA1 or SAA2. These findings suggest that high local SAA3 production
led to deposition at this unusual site. Although amyloid A (AA) amyloid deposits typically consist of an N-terminal
fragment of SAA1 or SAA2, here, abundant C-terminal peptides indicated that the uterine amyloid was largely
composed of full-length SAA3. The exclusive deposition of SAA3 amyloid in the uterus, together with elevated
uterine SAA3 transcripts, suggests that the uterine amyloid deposits were due to locally produced SAA3. This is
the first report of SAA3 as a cause of amyloidosis and of AA amyloid deposited exclusively in the uterus. MenosABSTRACT Pathologic amyloid accumulates in theCNS or in peripheral organs, yet the mechanism underlying the
targeting of systemic amyloid deposits is unclear. Serum amyloid A (SAA) 1 and 2 are produced predominantly by
the liver and form amyloid most commonly in the spleen, liver, and kidney. In contrast, SAA3 is produced primarily
extrahepatically and has no causal link to amyloid formation. Here, we identified 8 amyloidosis cases with amyloid
composed of SAA3 expanding the uterine wall of goats with near-term fetuses. Uterine amyloid accumulated in
the endometrium, only at the site of placental attachment,compromising maternal-fetal gas and nutrient exchange
and leading to fetal ischemia and death. No other organ contained amyloid. SAA3 mRNA levels in the uterine endometrium
were as high as SAA2 in the liver, yet mass spectrometry of the insoluble uterine peptides identified
SAA3 as the predominant protein, and not SAA1 or SAA2. These findings suggest that high local SAA3 production
led to deposition at this unusual site. Although amyloid A (AA) amyloid deposits typically consist of an N-terminal
fragment of SAA1 or SAA2, here, abundant C-terminal peptides indicated that the uterine amyloid was largely
composed of full-length SAA3. The exclusive deposition of SAA3 amyloid in the uterus, together with elevated
uterine SAA3 transcripts, suggests that the uterine amyloid deposits were due to locally produced SAA3. This is
the first report of SAA3 as a cause of amyloidosis and... Presentar Todo |
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Palabras claves : |
AMILOIDE; AMYLOID; ESPECTROMETRIA DE MASAS; MAL REPLIEGUE DE PROTEÍNA; MASS SPECTROMETRY; PROTEIN MISFOLDING; SALUD ANIMAL. |
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Thesagro : |
CABRAS. |
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Asunto categoría : |
L73 Enfermedades de los animales |
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Marc : |
LEADER 02476naa a2200337 a 4500
001 1056751
005 2019-02-26
008 2015 bl uuuu u00u1 u #d
024 7 $a10.1096/fj.14-256081$2DOI
100 1 $aGAFFNEY PM
245 $aProtein profiling of isolated uterine AA amyloidosis causing fetal death in goats.$h[electronic resource]
260 $c2015
520 $aABSTRACT Pathologic amyloid accumulates in theCNS or in peripheral organs, yet the mechanism underlying the targeting of systemic amyloid deposits is unclear. Serum amyloid A (SAA) 1 and 2 are produced predominantly by the liver and form amyloid most commonly in the spleen, liver, and kidney. In contrast, SAA3 is produced primarily extrahepatically and has no causal link to amyloid formation. Here, we identified 8 amyloidosis cases with amyloid composed of SAA3 expanding the uterine wall of goats with near-term fetuses. Uterine amyloid accumulated in the endometrium, only at the site of placental attachment,compromising maternal-fetal gas and nutrient exchange and leading to fetal ischemia and death. No other organ contained amyloid. SAA3 mRNA levels in the uterine endometrium were as high as SAA2 in the liver, yet mass spectrometry of the insoluble uterine peptides identified SAA3 as the predominant protein, and not SAA1 or SAA2. These findings suggest that high local SAA3 production led to deposition at this unusual site. Although amyloid A (AA) amyloid deposits typically consist of an N-terminal fragment of SAA1 or SAA2, here, abundant C-terminal peptides indicated that the uterine amyloid was largely composed of full-length SAA3. The exclusive deposition of SAA3 amyloid in the uterus, together with elevated uterine SAA3 transcripts, suggests that the uterine amyloid deposits were due to locally produced SAA3. This is the first report of SAA3 as a cause of amyloidosis and of AA amyloid deposited exclusively in the uterus.
650 $aCABRAS
653 $aAMILOIDE
653 $aAMYLOID
653 $aESPECTROMETRIA DE MASAS
653 $aMAL REPLIEGUE DE PROTEÍNA
653 $aMASS SPECTROMETRY
653 $aPROTEIN MISFOLDING
653 $aSALUD ANIMAL
700 1 $aBARR, B.
700 1 $aROWE, J.D.
700 1 $aBETT, C.
700 1 $aDRYGIANNAKIS, I.
700 1 $aGIANNITTI, F.
700 1 $aTREJO, M.
700 1 $aGHASSEMIAN ,M.
700 1 $aMASLIAH, E.
700 1 $aSIGURDSON, C.J.
773 $tThe FASEB Journal, 2015$gv. 29, n.3, p.911-919.
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Registro original : |
INIA La Estanzuela (LE) |
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| Registros recuperados : 14 | |
| 4. |  | GALVÁN, G.; VICENTE, E.; ARIAS, M.; GONZÁLEZ RABELINO, P. Selección por resistencia a Peronospora destructor en el mejoramiento genético de cebolla (Allium cepa). MV 30 - COMUNICACIONES LIBRES - MV. MEJORAMIENTO VEGETAL In: JOURNAL OF BASIC & APPLIED GENETICS, 2016, Vol.27, Iss. 1 (Supp.). XVI LATIN AMERICAN CONGRESS OF GENETICS, IV CONGRESS OF THE URUGUAYAN SOCIETY OF GENETICS, XLIX ANNUAL MEETING OF THE GENETICS SOCIETY OF CHILE, XLV ARGENTINE CONGRESS OF GENETICS, 9-12 October 2016. PROCEEDINGS. Montevideo (Uruguay): SAG, 2016. p. 295| Tipo: Trabajos en Congresos/Conferencias |
| Biblioteca(s): INIA Las Brujas. |
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| 6. | | ARIAS, M.; FERENCZI, A.; GALIGER, S.; GONZÁLEZ, J.; MARA, V.; URRABURU, M.; SEVERINO, V. Análisis de la evolución del quemado de sol en Granny Smith. Seminario técnico. Las Brujas, Canelones (UY), 1-2 octubre 2014. In: INIA Las Brujas, Programa Nacional Producción Frutícola. Actualización técnica de frutales de pepita. Montevideo (Uruguay): INIA, 2014. p. 101-106 (Serie Actividades de Difusión ; 739)| Biblioteca(s): INIA Las Brujas. |
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| 12. | | SEVERINO, V.; FERENCZI, A.; GALIGER, S.; GONZÁLEZ, J.; MARA, V.; URRABURU, M.; ARIAS, M. Medidas de manejo para aumentar el sobrecolor de manzanas en montes instalados. Seminario técnico. Las Brujas, Canelones (UY), 1-2 octubre 2014. In: INIA Las Brujas, Programa Nacional Producción Frutícola. Actualización técnica de frutales de pepita. Montevideo (Uruguay): INIA, 2014. p. 85-91 (Serie Actividades de Difusión ; 739)| Biblioteca(s): INIA Las Brujas. |
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| 13. | | ARIAS, M.; CURBELO, N.; GONZÁLEZ, P.; VICENTE, E.; GIMÉNEZ, G.; GALVÁN, G. Inheritance of resistance against Peronospora destructor in onion cv. 'Regia'. Australian Journal of Crop Science, 2020, Volume 14, Issue 12, Pages 1999-2009. OPEN ACCESS. Doi: Article history: Published, December 2020.
The first author acknowledges the postgraduate fellowship from Sistema Nacional de Becas, Agencia Nacional de Investigación e Innovación (SNB-ANII), Uruguay.| Tipo: Artículos en Revistas Indexadas Internacionales | Circulación / Nivel : Internacional - -- |
| Biblioteca(s): INIA Las Brujas. |
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| 14. | | VICENTE, E.; RODRÍGUEZ, G.; GHELFI, B.; LADO, J.; ARRUABARRENA, A.; ARIAS, M.; GONZÁLEZ-ARCOS, M.; ZUNINI, N. ¿Cómo se obtienen las variedades de boniato?- Hortifruticultura. Revista INIA Uruguay, Diciembre 2023, no.75 p.68-70. (Revista INIA; 75).| Tipo: Artículos en Revistas Agropecuarias |
| Biblioteca(s): INIA Las Brujas. |
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| Registros recuperados : 14 | |
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