Differential effects of annexins I, II, III, and V on cytosolic phospholipase A2 activity: specific interaction model

Kim, Seung Wook; Ko, Jesang; Kim, Jae Hong; Choi, Eung‐Chil; Na, Doe Sun

doi:10.1016/s0014-5793(00)02326-7

Cited by 49 publications

(42 citation statements)

References 28 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: 79%

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: 79%

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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“…Similarly, reduction of ANXA2 expression in HeLa, 293 and 293T cells results in significant reduction of DNA synthesis and cell proliferation, 26 and overexpression of ANXA2 induced a higher cell proliferation rate in LLC-PK1 cells. 27 In contrast, ANXA2 is highly upregulated in PC12 cells undergoing neuronal differentiation during which proliferation ceases, 28 and exogenous expression of ANXA2 did not affect proliferation of DU145 cells 8 whereas a nuclear-localized ANXA2 variant suppressed proliferation of LNCaP cells. 9 Thus, the consensus in the literature for numerous cancer cell types is that ANXA2 expression is positively associated with proliferation-with the exception of prostate cells.…”

Section: Discussionmentioning

confidence: 97%

“…For example, A2t and S100A10 are each able to inhibit phospholipase A2 activity whereas monomeric ANXA2 cannot. 27 Similarly, the activation of plasminogen, which can contribute to the invasive phenotypes of highly aggressive cancers, 28 is stimulated by S100A10 or A2t, whereas the ANXA2 monomer has only limited ability to do so. 23 The more prominent cytoplasmic localization of ANXA2 in high-grade prostate cancer may be a result of lower levels of S100A10; immunohistochemical analyses of prostate cancer specimens will help to determine this possibility.…”

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confidence: 99%

Annexin A2 positively contributes to the malignant phenotype and secretion of IL‐6 in DU145 prostate cancer cells

Inokuchi

Narula

Yee

et al. 2008

Intl Journal of Cancer

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Several groups, including ours, have reported that annexin A2 (ANXA2) expression is reduced in most prostate cancer (CaP). More recently, however, we reported that ANXA2 is expressed in some high-grade tumors, but the biologic consequence of this is currently unknown. To elucidate the function of ANXA2 in CaP, we reduced its expression in DU145 cells using shRNA and tested the impact on characteristics of malignancy. Reduction of ANXA2 suppressed anchorage-dependent and -independent cell growth without affecting invasiveness. Interestingly, interleukin-6 (IL-6) secretion was reduced concomitantly with the reduction of ANXA2 but independently of S100A10. IL-6 expression was restored when wild type but not mutant ANXA2 was reexpressed in these cells. In a retrospective study of radical prostatectomy specimens from patients with nonmetastatic CaP, 100% of patients with ANXA2-positive tumors (n 5 4) had a biochemical relapse while only 50% of patients with ANXA2 negative tumors (n 5 20) relapsed, suggesting that ANXA2 expression in prostate tumors may be predictive of biochemical relapse. Significant cytoplasmic staining of ANXA2 was detected in 3 of 4 ANXA2-positive tumors, whereas ANXA2 is localized to the plasma membrane in benign prostatic glands. These finding, taken together, suggests a possible mechanism whereby ANXA2 expression positively contributes to an aggressive phenotype in a subset of CaP and suggest that ANXA2 has markedly different functions depending on its cellular context. Finally, this is the first description of a role for ANXA2 in IL-6 expression, and ANXA2 represents a new therapeutic target for reducing IL-6 in high-grade prostate cancer.

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“…74) Fourth, some annexins can function as negative regulators of cPLA 2 a in cellular signal transduction. The Cterminal region of annexin I binds to the C2 domain of cPLA 2 a and inhibits PLA 2 activity by specific interaction, 75) whereas annexin V inhibits cPLA 2 a activity mainly by substrate depletion. 76) Annexins II and III do not have any inhibitory effects.…”

Section: -5 Regulation By Protein Interaction and Cleavagementioning

confidence: 99%

Regulatory Mechanism and Physiological Role of Cytosolic Phospholipase A2

Hirabayashi

Murayama

Shimizu

2004

Biological & Pharmaceutical Bulletin

216

184

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Cytosolic phospholipase A 2 a a (cPLA 2 a a) preferentially hydrolyzes phospholipids containing arachidonic acid and plays a key role in the biosynthesis of eicosanoids. This review discusses the essential features of cPLA 2 a a regulation and addresses new insights into the functional properties of this enzyme. Full activation of the enzyme requires Ca 2؉ binding to an N-terminal C2 domain and phosphorylation on serine residues. Ca 2؉ binding induces translocation of cPLA 2 a a from the cytosol to the perinuclear membranes. Serine phosphorylation is mediated by mitogen-activated protein kinases (MAPKs), Ca 2؉ /calmodulin-dependent protein kinase II, and MAPK-interacting kinase Mnk1. Interaction with proteins and lipids, which include vimentin, annexins, NADPH oxidase, phosphatidylcholine, phosphatidylinositol 4,5-bisphosphate (PIP 2 ), and ceramide-1-phosphate, can also modulate the activity of cPLA 2 a a. Recent evidence has established the physiological and pathological roles of cPLA 2 a a using cPLA 2 a a knockout mice. This enzyme has been implicated in fertility, striated muscle growth, renal concentration, postischemic brain injury, arthritis, inflammatory bone resorption, intestinal polyposis, pulmonary fibrosis, acute respiratory distress syndrome, and autoimmune encephalomyelitis. Now novel three paralogs, cPLA 2 b b, cPLA 2 g g, and cPLA 2 d d, have been identified in humans. cPLA 2 g g is distinct from others in that it is farnesylated and lacks the C2 domain. Biological roles for these new enzymes have not yet been defined.

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Differential effects of annexins I, II, III, and V on cytosolic phospholipase A2 activity: specific interaction model

Cited by 49 publications

References 28 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 A2 positively contributes to the malignant phenotype and secretion of IL‐6 in DU145 prostate cancer cells

Regulatory Mechanism and Physiological Role of Cytosolic Phospholipase A2

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