Annexin V and Phospholipid Metabolism

Russo‐Marie, Françoise

doi:10.1515/cclm.1999.050

Cited by 30 publications

(17 citation statements)

References 38 publications

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“…The interaction between these proteins and Ca 2ϩ is also known from other studies reviewed by Gerke et al (23). Furthermore, ANXA1 and ANXA5 can inhibit phospholipase A2 (32,53). Since cPLA2 is a key enzyme responsible for signal transduction in inflammation, and the annexins have been …”

Section: Discussionmentioning

confidence: 80%

Identification of differentially expressed proteins in ruminal epithelium in response to a concentrate-supplemented diet

Bondzio¹,

Gabler²,

Badewien-Rentzsch³

et al. 2011

American Journal of Physiology-Gastrointestinal and Liver Physi

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minal epithelium adapts to dietary change with well-coordinated alterations in metabolism, proliferation, and permeability. To further understand the molecular events controlling diet effects, the aim of this study was to evaluate protein expression patterns of ruminal epithelium in response to various feeding regimes. Sheep were fed with a concentrate-supplemented diet for up to 6 wk. The control group received hay only. Proteome analysis with differential in gel electrophoresis technology revealed that, after 2 days, 60 proteins were significantly modulated in ruminal epithelium in a comparison between hay-fed and concentrate-fed sheep (P Ͻ 0.05). Forty proteins were upregulated and 20 proteins were downregulated in response to concentrate diet. After 6 wk of this diet, only 14 proteins were differentially expressed. Among these, 11 proteins were upregulated and 3 downregulated. To identify proteins that were modulated by dietary change, two-dimensional electrophoresis was coupled with liquid chromatography electrospray ionization mass spectrometry. The differential expression of selected proteins, such as esterase D, annexin 5, peroxiredoxin 6, carbonic anhydrase I, and actin-related protein 3, was verified by immunoblotting and/or mRNA analysis. The identified proteins were mainly associated with functions related to cellular stress, metabolism, and differentiation. These results suggest new candidate proteins that may contribute to a better understanding of the signaling pathways and mechanisms that mediate rumen epithelial adaptation to high-concentrate diet.proteomics; mRNA expression; protein markers; sheep RUMINANTS ARE OF MAJOR WORLDWIDE interest and economic importance because of increasing meat and milk production. A substantial improvement in the productivity and performance of ruminants can only be achieved with adequate dietary supplementation. When high-yielding cattle, milk sheep, or goats merely consume forage, the intake of energy and protein is too low for the desired rates of animal performance. Hence, supplementation of forage-fed ruminants with sufficient amounts of energy and protein is necessary and significantly improves milk production or daily weight gain (41), but, particularly, a surplus of easily fermented carbohydrates or low-fiber intake will place the animals at risk. Such a change in the diet is a challenge for rumen microbes (31) and especially for the ruminal epithelium with respect to adaptation to the new fermentation pattern (47,55). Insufficient adaptation to diet may result in disintegration of the epithelium (22), translocation of lipopolysaccharides (30), and disturbed transport mechanisms (22) and can further cause subacute ruminal acidosis (14, 49). This disease not only can lead to depressed feed intake and milk production, but can also be associated with laminitis, inflammation, and liver abscesses (14,42,49).Hence, one objective of attaining an adequate diet composition for ruminants is to maintain the physiological functions of the forestomach, such as optimal fe...

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Section: Discussionmentioning

confidence: 80%

Identification of differentially expressed proteins in ruminal epithelium in response to a concentrate-supplemented diet

Bondzio¹,

Gabler²,

Badewien-Rentzsch³

et al. 2011

American Journal of Physiology-Gastrointestinal and Liver Physi

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“…Annexins participate in a variety of intracellular processes, ranging from the regulation of membrane dynamics to cell migration, proliferation and apoptosis (Monastyrskaya et al, 2009). Annexin A5, one of the most abundant annexins in mammalian cells, has a hitherto unknown function within the intracellular environment, although it has been found to modulate the activities of protein kinase C as well as phospholipase A by interfering with their binding to negatively charged phospholipids and Ca 2+ (Russo-Marie, 1999). Furthermore, an anti-thrombotic property has been proposed for annexin A5 by shielding phospholipids, especially phosphatidylserine, and thereby blocking their availability for coagulation reactions (Cederholm and Frostegard, 2007).…”

Section: Discussionmentioning

confidence: 99%

Annexin A5 stimulates autophagy and inhibits endocytosis

Ghislat

Aguado

Knecht

2012

Journal of Cell Science

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SummaryMacroautophagy is a major lysosomal catabolic process activated particularly under starvation in eukaryotic cells. A new organelle, the autophagosome, engulfs cytoplasmic substrates, which are degraded after fusion with endosomes and/or lysosomes. During a shotgun proteome analysis of purified lysosomal membranes from mouse fibroblasts, a Ca 2+ -dependent phospholipid-binding protein, annexin A5, was found to increase on lysosomal membranes under starvation. This suggests a role for this protein, an abundant annexin with a still unknown intracellular function, in starvation-induced lysosomal degradation. Transient overexpression and silencing experiments showed that annexin A5 increased lysosomal protein degradation, and colocalisation experiments, based on GFP sensitivity to lysosomal acidic pH, indicated that this was mainly the result of inducing autophagosome-lysosome fusion. Annexin A5 also inhibited the endocytosis of a fluid-phase marker and cholera toxin, but not receptor-mediated endocytosis. Therefore, we propose a double and opposite role of annexin A5 in regulating the endocytic and autophagic pathways and the fusion of autophagosomes with lysosomes and endosomes.

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“…In fact Dubois and collaborators (34 -36) showed association between annexin 6 and a 56-kDa protein kinase in T cells. Other proteins that affect the annexin binding to the membrane are the phospholipases (37,38). In smooth muscle cell membranes, the organization of raft or non-raft microdomains is regulated by annexin 6, and this association is mediated by interaction with the cytoskeleton (13, 39 -41).…”

Section: Discussionmentioning

confidence: 99%

Annexin 6 Modulates the Maxi-chloride Channel of the Apical Membrane of Syncytiotrophoblast Isolated from Human Placenta

Riquelme

Llanos

Tischner

et al. 2004

Journal of Biological Chemistry

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The syncytiotrophoblast separates the maternal and fetal blood and constitutes the primary barrier for maternal-fetal transport. The Maxi-chloride channel from the apical membrane of the syncytiotrophoblast plays a role in the chloride conductance. Annexins can play an important role in the regulation of membrane events. In this study we evaluate the role of annexin 6 in the Maxichloride channel properties. The results showed that annexin 6 is bound in the apical placenta membranes in a calcium-dependent phospholipid-binding manner but also in a calcium-independent fashion. The neutralization of annexin 6 decreased the total current by 39 ؎ 1.9% in the range of ؎80 mV, and the currents decrease with the time. The single-channel slope conductance was decreased from 253 ؎ 7.4 pS (control) to 105 ؎ 13 pS, and the amplitude decreased by 50%. The open probability was also affected when higher voltage steps were used, changes in either the positive or negative direction induced the channel to close, and the open probability (P o ) did not decrease. In channels with neutralized annexin 6, it was maintained at 1 at ؎40 mV and at ؎80 mV. These results suggest that endogenous annexin 6 could regulate the Maxi-chloride channel. The results obtained with normal placentae, in which annexin 6 was neutralized, are similar to those described for the Maxichloride channel isolated from pre-eclamptic placenta. Together these data suggest that annexin 6 could play an important role in ion transport of the placenta.

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Annexin V and Phospholipid Metabolism

Cited by 30 publications

References 38 publications

Identification of differentially expressed proteins in ruminal epithelium in response to a concentrate-supplemented diet

Identification of differentially expressed proteins in ruminal epithelium in response to a concentrate-supplemented diet

Annexin A5 stimulates autophagy and inhibits endocytosis

Annexin 6 Modulates the Maxi-chloride Channel of the Apical Membrane of Syncytiotrophoblast Isolated from Human Placenta

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