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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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Registro completo
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Biblioteca (s) : |
INIA Tacuarembó. |
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Fecha actual : |
21/02/2014 |
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Actualizado : |
22/02/2014 |
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Autor : |
Gimeno, D.; Coronel, F. |
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Título : |
De las planillas de Flock Testing a las DEPs |
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Fecha de publicación : |
2007 |
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Fuente / Imprenta : |
Ovinos Notas Prácticas, Hoja coleccionable no. 1, 2007 |
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Idioma : |
Español |
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Thesagro : |
MEJORA GENETICA; OVINOS. |
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Asunto categoría : |
-- |
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Marc : |
LEADER 00386naa a2200145 a 4500
001 1029001
005 2014-02-22
008 2007 bl uuuu u00u1 u #d
100 1 $aGIMENO, D.
245 $aDe las planillas de Flock Testing a las DEPs
260 $c2007
650 $aMEJORA GENETICA
650 $aOVINOS
700 1 $aCORONEL, F.
773 $tOvinos Notas Prácticas, Hoja coleccionable no. 1, 2007
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Registro original : |
INIA Tacuarembó (TBO) |
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