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1.
J Reprod Dev ; 61(6): 565-9, 2015.
Artigo em Inglês | MEDLINE | ID: mdl-26400127

RESUMO

The objective of this study was to examine the effects of metritis and subclinical hypocalcemia on reduction of uterine size in dairy cows using ultrasonography and sonomicrometry. Four piezoelectric crystals were implanted via laparotomy into the myometrium of the pregnant uterine horn of 12 pluriparous Holstein Friesian cows 3 weeks before the calculated calving date. Sonometric measurements were conducted daily from 2 days before parturition (= Day 0) until Day 14 after calving and then every other day until Day 28. Distances between adjacent crystals were expressed in relation to reference values obtained before calving. The diameter of the formerly pregnant uterine horn was measured using transrectal B-Mode sonography starting on Day 10. Cows were retrospectively divided into the following groups: cows without metritis (M-; n = 7), cows with metritis (M+; n = 5), cows with normocalcemia (SH-; Ca > 2.0 mmol/l on Days 1 to 3; n = 5) and cows with subclinical hypocalcemia (SH+; Ca < 2.0 mmol/l in at least one sample between Days 1 and 3; n = 7). Metritis did not affect (P > 0.05) sonometric measurements, but the diameter of the formerly pregnant horn was larger (P ≤ 0.05) between Days 15 and 21 in M+ cows than in M‒ cows. Reduction in uterine length in hypocalcemic cows was delayed (P ≤ 0.05) between Days 8 and 21 compared with normocalcemic cows, but the uterine horn diameter was not related to calcium status. In conclusion, both diseases affected reduction of uterine size until Day 28. Cows with metritis had a larger uterine diameter, possibly attributable to accumulation of lochia, and cows with subclinical hypocalcemia had delayed reduction of uterine length, presumably related to reduction of myometrial contractility.


Assuntos
Doenças dos Bovinos/patologia , Endometrite/veterinária , Hipocalcemia/veterinária , Complicações na Gravidez/veterinária , Útero/patologia , Animais , Bovinos , Doenças dos Bovinos/diagnóstico por imagem , Endometrite/diagnóstico por imagem , Endometrite/patologia , Feminino , Hipocalcemia/diagnóstico por imagem , Hipocalcemia/patologia , Gravidez , Complicações na Gravidez/diagnóstico por imagem , Complicações na Gravidez/patologia , Ultrassonografia , Útero/diagnóstico por imagem
2.
J Biol Chem ; 283(11): 6656-67, 2008 Mar 14.
Artigo em Inglês | MEDLINE | ID: mdl-18180301

RESUMO

The preprotein translocon at the inner envelope of chloroplasts (Tic complex) facilitates the import of nuclear-encoded preproteins into the organelle. Seven distinct subunits have been identified so far. For each of those, specific functions have been proposed based on structural prediction or experimental evidence. Three of those subunits possess modules that could act as redox-active regulatory components in the import process. To date, however, the mode of redox regulation of the import process remains enigmatic. To investigate how the chloroplast redox state influences translocon behavior and composition, we studied the Tic component and the putative redox sensor Tic62 in more detail. The experimental results provide evidence that Tic62 can act as a bona fide dehydrogenase in vitro, and that it changes its localization in the chloroplast dependent on the NADP+/NADPH ratio in the stroma. Moreover, the redox state influences the interactions of Tic62 with the translocon and the flavoenzyme ferredoxin-NADP+ oxidoreductase. Additionally, we give initial experimental insights into the Tic62 structure using circular dichroism measurements and demonstrate that the protein consists of two structurally different domains. Our results indicate that Tic62 possesses redox-dependent properties that would allow it to fulfill a role as redox sensor protein in the chloroplast.


Assuntos
Regulação da Expressão Gênica de Plantas , NADPH Desidrogenase/metabolismo , NADP/química , Pisum sativum/metabolismo , Sequência de Aminoácidos , Cloroplastos/metabolismo , Dicroísmo Circular , Ferredoxinas/química , Modelos Biológicos , Dados de Sequência Molecular , NADPH Desidrogenase/fisiologia , Oxirredução , Oxirredutases/metabolismo , Oxigênio/metabolismo , Estrutura Terciária de Proteína , Transporte Proteico , Homologia de Sequência de Aminoácidos
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