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      Revisión: Función y regresión del cuerpo lúteo durante el ciclo estral de la vaca Translated title: Review: Function and regression of the corpus luteum during the estrous cycle

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          Abstract

          RESUMEN El cuerpo lúteo (CL) es una estructura ovárica que produce progesterona para mantener la gestación, inicia su crecimiento a partir del tercer día de iniciado el estro creciendo hasta el décimo octavo día. Sí, el CL es fertilizado la formación del embrión producirá el interferón τ (IFN-τ) sustancia responsable del reconocimiento materno de la gestación (RMG) en los bovinos durante toda su gestación. Al no ser fertilizado el CL el endometrio uterino secreta prostaglandinas F2α (PGF2α) causando la lisis del cuerpo lúteo. Los niveles séricos de la progesterona disminuyen generando desbloqueo del hipotálamo y secreción de la hormona liberadora de gonadotropinas (GnRH) para activar el eje hipotalámico-hipofisiario-gonadal que desarrolla folículos nuevos de 48 a 72 h posteriores e inicia un nuevo estro. La presente revisión bibliográfica detalla los mecanismos fisiológicos involucrados en la formación del cuerpo lúteo durante el ciclo estral de los bovinos.

          Translated abstract

          ABSTRACT The corpus luteum (CL) is an ovarian structure that produces progesterone to maintain pregnancy, begins its growth from the third day of the beginning of estrus growing until the eighteenth day. If the CL is fertilized, the formation of the embryo will produce the interferon τ (IFN-τ) substance responsible for maternal recognition of pregnancy (RMG) in cattle during their entire pregnancy. When CL is not fertilized, the uterine endometrium secretes prostaglandins F2α (PGF2α) causing lysis of the corpus luteum. The serum levels of progesterone decrease generating hypothalamus unlocking and gonadotropin-releasing hormone (GnRH) secretion to activate the hypothalamic-pituitary-gonadal axis that develops new follicles 48 to 72 h later and initiates a new estrus. This bibliographic review details the physiological mechanisms involved in the formation of the corpus luteum during the estrous cycle of cattle in the function and regression of the corpus luteum during the estrous cycle of cows.

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          Caspases: the executioners of apoptosis.

          Apoptosis is a major form of cell death, characterized initially by a series of stereotypic morphological changes. In the nematode Caenorhabditis elegans, the gene ced-3 encodes a protein required for developmental cell death. Since the recognition that CED-3 has sequence identity with the mammalian cysteine protease interleukin-1 beta-converting enzyme (ICE), a family of at least 10 related cysteine proteases has been identified. These proteins are characterized by almost absolute specificity for aspartic acid in the P1 position. All the caspases (ICE-like proteases) contain a conserved QACXG (where X is R, Q or G) pentapeptide active-site motif. Capases are synthesized as inactive proenzymes comprising an N-terminal peptide (prodomain) together with one large and one small subunit. The crystal structures of both caspase-1 and caspase-3 show that the active enzyme is a heterotetramer, containing two small and two large subunits. Activation of caspases during apoptosis results in the cleavage of critical cellular substrates, including poly(ADP-ribose) polymerase and lamins, so precipitating the dramatic morphological changes of apoptosis. Apoptosis induced by CD95 (Fas/APO-1) and tumour necrosis factor activates caspase-8 (MACH/FLICE/Mch5), which contains an N-terminus with FADD (Fas-associating protein with death domain)-like death effector domains, so providing a direct link between cell death receptors and the caspases. The importance of caspase prodomains in the regulation of apoptosis is further highlighted by the recognition of adapter molecules, such as RAIDD [receptor-interacting protein (RIP)-associated ICH-1/CED-3-homologous protein with a death domain]/CRADD (caspase and RIP adapter with death domain), which binds to the prodomain of caspase-2 and recruits it to the signalling complex. Cells undergoing apoptosis following triggering of death receptors execute the death programme by activating a hierarchy of caspases, with caspase-8 and possibly caspase-10 being at or near the apex of this apoptotic cascade.
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            The biology of vascular endothelial growth factor.

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              Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation.

              Programmed necrosis is a form of caspase-independent cell death whose molecular regulation is poorly understood. The kinase RIP1 is crucial for programmed necrosis, but also mediates activation of the prosurvival transcription factor NF-kappaB. We postulated that additional molecules are required to specifically activate programmed necrosis. Using a RNA interference screen, we identified the kinase RIP3 as a crucial activator for programmed necrosis induced by TNF and during virus infection. RIP3 regulates necrosis-specific RIP1 phosphorylation. The phosphorylation of RIP1 and RIP3 stabilizes their association within the pronecrotic complex, activates the pronecrotic kinase activity, and triggers downstream reactive oxygen species production. The pronecrotic RIP1-RIP3 complex is induced during vaccinia virus infection. Consequently, RIP3(-/-) mice exhibited severely impaired virus-induced tissue necrosis, inflammation, and control of viral replication. Our findings suggest that RIP3 controls programmed necrosis by initiating the pronecrotic kinase cascade, and that this is necessary for the inflammatory response against virus infections.
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                Author and article information

                Journal
                av
                Abanico veterinario
                Abanico vet
                Sergio Martínez González (Tepic, Nayarit, Mexico )
                2007-428X
                2448-6132
                2019
                : 9
                : e924
                Affiliations
                [1] Zacatecas orgnameUniversidad Autónoma de Zacatecas orgdiv1Unidad Académica de Medicina Veterinaria y Zootecnia Mexico arechiga.uaz@ 123456gmail.com
                Article
                S2448-61322019000100224 S2448-6132(19)00900000224
                10.21929/abavet2019.924
                fc21ada0-f16d-493c-9b81-ac87e51c06c6

                This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.

                History
                : 28 October 2019
                : 06 February 2019
                Page count
                Figures: 0, Tables: 0, Equations: 0, References: 150, Pages: 0
                Product

                SciELO Mexico

                Categories
                Artículos de revisión

                progesterona,bovinos,cuerpo lúteo,prostaglandinas,luteolisis,bovine,corpus luteum,progesterone,prostaglandins,luteolysis

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