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Journal articles on the topic 'Annexin A5'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Brachvogel, Bent, Jörg Dikschas, Helga Moch, Heike Welzel, Klaus von der Mark, Clementine Hofmann, and Ernst Pöschl. "Annexin A5 Is Not Essential for Skeletal Development." Molecular and Cellular Biology 23, no. 8 (April 15, 2003): 2907–13. http://dx.doi.org/10.1128/mcb.23.8.2907-2913.2003.

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ABSTRACT Annexins are highly conserved proteins that are characterized by their ability to interact with phospholipids in a calcium-dependent manner. Although diverse functions have been ascribed to annexins based on in vitro analyses, their in vivo functions still remain unclear. The intensively studied annexin A5 has been identified by its effects on blood coagulation, and subsequently, its function as a calcium-specific ion channel was described. In vitro experiments and expression studies suggested a potential role of annexin A5 during calcification processes in vivo, especially in endochondral ossification. To gain insights into the relevance of annexin A5 in this process, we generated an annexin A5-deficient mouse mutant. Mice lacking annexin A5 are viable, are fertile, and reveal no significant alterations in the biochemical parameters characteristic for metabolic or functional defects. Neither the development of skeletal elements nor the in vitro calcification properties of isolated chondrocytes is significantly impaired by the absence of annexin A5. Therefore, annexin A5 is dispensable for the formation and maintenance of skeletal elements in the mouse and may possibly be pointing to a compensatory effect of other members from the annexin family due to their high functional and structural similarity.

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2

BROOKS, Nicole D., Jean E. GRUNDY, Nadine LAVIGNE, Mélanie C. DERRY, Christina M. RESTALL, ROGER C. MacKENZIE, David M. WAISMAN, and Edward L. G. PRYZDIAL. "Ca2+-dependent and phospholipid-independent binding of annexin 2 and annexin 5." Biochemical Journal 367, no. 3 (November 1, 2002): 895–900. http://dx.doi.org/10.1042/bj20020997.

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Annexins are a family of homologous proteins that associate with anionic phospholipid (aPL) in the presence of Ca2+. Evidence that the function of one annexin type may be regulated by another was recently reported in studies investigating cytomegalovirus—aPL interactions, where the fusogenic function of annexin 2 (A2) was attenuated by annexin 5 (A5). This observation suggested that A2 may bind directly to A5. In the present study, we demonstrated this interaction. The A2—A5 complex was first detected utilizing (covalently linked) fluorescein-labelled A5 (F-A5) as a reporter group. The interaction required concentrations of Ca2+ in the millimolar range, had an apparent dissociation constant [Kd(app)] of 1nM at 2mM Ca2+ and was independent of aPL. A2 bound comparably with F-A5 pre-equilibrated with an amount of aPL that could bind just the F-A5 or to an excess amount of aPL providing sufficient binding sites for all of F-A5 and A2. A2—A5 complex formation was corroborated in an experiment, where [125I]A2 associated in a Ca2+-dependent manner with A5 coated on to polystyrene. Surface plasmon resonance was used as a third independent method to demonstrate the binding of A2 and A5 and, furthermore, supported the conclusion that the monomeric and tetrameric forms of A2 bind equivalently to A5. Together these results demonstrate an A2—A5 interaction and provide an explanation as to how A5 inhibits the previously reported A2-dependent enhancement of virus—aPL fusion.

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3

Bećarević, Mirjana, Svetlana Ignjatović, and Nada Majkić-Singh. "Apoptosis, Annexin A5 and Anti-Annexin A5 Antibodies in The Antiphospholipid Syndrome." Journal of Medical Biochemistry 32, no. 2 (April 1, 2013): 89–95. http://dx.doi.org/10.2478/jomb-2013-0014.

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Summary It has been proposed that apoptosis is one of the mechanisms involved in the generation of antiphospholipid antibodies. The presence of antiphospholipid antibodies is the main laboratory criterion for a definite diagnosis of the antiphospholipid syndrome. Annexinopathies are disorders characterized by deregulation of annexins expression levels and function. Annexin A5 has been used as an agent for molecular imaging techniques (visualization of phosphatidylserineexpressing apoptotic cells) in vitro and in vivo in animal models and in patients (injection of human recombinant anxA5 into the patient‘s circulation). Although the determination of titers of anti-annexin A5 antibodies is not mandatory for the diagnosis of the antiphospholipid syndrome, it was reported that patients with primary antiphospholipid syndrome with a history of recurrent abortions had elevated titers of antiannexin A5 antibodies, while the presence of thromboses was not associated with elevated levels of these antibodies

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4

Hu, Guochang. "Recombinant Human Annexin A5." Critical Care Medicine 42, no. 1 (January 2014): 219–20. http://dx.doi.org/10.1097/01.ccm.0000435680.21801.0f.

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5

Derry, Mélanie C., Michael R. Sutherland, Christina M. Restall, David M. Waisman, and Edward L. G. Pryzdial. "Annexin 2-mediated enhancement of cytomegalovirus infection opposes inhibition by annexin 1 or annexin 5." Journal of General Virology 88, no. 1 (January 1, 2007): 19–27. http://dx.doi.org/10.1099/vir.0.82294-0.

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Biochemical studies have suggested that annexin 2 (A2) may participate in cytomegalovirus (CMV) infection. In the current work, effects of A2 monomer (p36) and heterotetramer (A2t; p362p112) were investigated. Demonstrating a role for endogenous A2, the four stages of infection that were followed were each inhibited by anti-p36 or anti-p11 at 37 °C. Immuno-inhibition was attenuated when the virus and cells were pre-incubated at 4 °C to coordinate virus entry initiated afterwards at 37 °C, reconciling controversy in the literature. As an explanation, CMV-induced phosphorylation of p36 was prevented by the 4 °C treatment. Supporting these immuno-inhibition data, purified A2t or p11 increased CMV infectious-progeny generation and CMV gene expression. A specific role for A2t was indicated by purified p36 having no effect. Unlike other steps, primary plaque formation was not enhanced by purified A2t or p11, possibly because of undetectable phosphorylation. As annexins 1 (A1) and 5 (A5) interact with A2, their effect on CMV was also tested. Both purified proteins inhibited CMV infection. In each experiment, the concentration of A1 required for half-maximal inhibition was five- to 10-fold lower than that of A5. Addition of A2 opposed A1- or A5-mediated inhibition of CMV, as did certain A2-specific antibodies that had no effect in the absence of added A1 or A5. Transfection of the p36-deficient cell line HepG2 increased CMV infection and was required for inhibition by the other annexins. These data suggest that CMV exploits A2t at physiological temperature to oppose the protection of cells conferred by A1 or A5.

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6

Monastyrskaya, Katia, Fabian Tschumi, Eduard B. Babiychuk, Deborah Stroka, and Annette Draeger. "Annexins sense changes in intracellular pH during hypoxia." Biochemical Journal 409, no. 1 (December 11, 2007): 65–75. http://dx.doi.org/10.1042/bj20071116.

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The pHi (intracellular pH) is an important physiological parameter which is altered during hypoxia and ischaemia, pathological conditions accompanied by a dramatic decrease in pHi. Sensors of pHi include ion transport systems which control intracellular Ca2+ gradients and link changes in pHi to functions as diverse as proliferation and apoptosis. The annexins are a protein family characterized by Ca2+-dependent interactions with cellular membranes. Additionally, in vitro evidence points to the existence of pH-dependent, Ca2+-independent membrane association of several annexins. We show that hypoxia promotes the interaction of the recombinant annexin A2–S100A10 (p11) and annexin A6 with the plasma membrane. We have investigated in vivo the influence of the pHi on the membrane association of human annexins A1, A2, A4, A5 and A6 tagged with fluorescent proteins, and characterized this interaction for endogenous annexins present in smooth muscle and HEK (human embryonic kidney)-293 cells biochemically and by immunofluorescence microscopy. Our results show that annexin A6 and the heterotetramer A2–S100A10 (but not annexins A1, A4 and A5) interact independently of Ca2+ with the plasma membrane at pH 6.2 and 6.6. The dimerization of annexin A2 within the annexin A2–S100A10 complex is essential for the pH-dependent membrane interaction at this pH range. The pH-induced membrane binding of annexins A6 and A2–S100A10 might have consequences for their functions as membrane organizers and channel modulators.

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7

Bahmani, Peyman, Eyk Schellenberger, Jan Klohs, Jens Steinbrink, Ryan Cordell, Marietta Zille, Jochen Müller, et al. "Visualization of Cell Death in MICE with Focal Cerebral Ischemia using Fluorescent Annexin A5, Propidium Iodide, and Tunel Staining." Journal of Cerebral Blood Flow & Metabolism 31, no. 5 (January 19, 2011): 1311–20. http://dx.doi.org/10.1038/jcbfm.2010.233.

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To monitor stroke-induced brain damage and assess neuroprotective therapies, specific imaging of cell death after cerebral ischemia in a noninvasive manner is highly desirable. Annexin A5 has been suggested as a marker for imaging cell death under various disease conditions including stroke. In this study, C57BL6/N mice received middle cerebral artery occlusion (MCAO) and were injected intravenously with either active or inactive Cy5.5-annexin A5 48 hours after reperfusion. Some mice also received propidium iodide (PI), a cell integrity marker. Only in mice receiving active Cy5.5-annexin A5 were fluorescence intensities significantly higher over the hemisphere ipsilateral to MCAO than on the contralateral side. This was detected noninvasively and ex vivo 4 and 8 hours after injection. The majority of cells positive for fluorescent annexin A5 were also positive for PI and fragmented DNA as detected by terminal deoxynucleotidyl transferase-mediated 2'-deoxyuridine 5'-triphosphate-biotin nick end labeling (TUNEL) staining. This study demonstrates the high specificity of annexin A5 for visualization of cell death in a mouse model of stroke. To our knowledge, this is the first study to compare the distribution of injected active and inactive annexin A5, PI, and TUNEL staining. It provides important information on the experimental and potential clinical applications of annexin A5-based imaging agents in stroke.

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8

Hiddink, Larissa, Marieke C. H. de Visser, and Waander L. van Heerde. "Polymorphisms in the Annexin A5 gene influence circulating Annexin A5 levels in healthy controls." Thrombosis Research 129, no. 6 (June 2012): 815–17. http://dx.doi.org/10.1016/j.thromres.2012.03.022.

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9

Baleva, Marta, Maria Hristova, and Krasimir Nikolov. "Diagnostic significance of anti-annexin-A5 antibody determination." Open Medicine 5, no. 1 (February 1, 2010): 6–11. http://dx.doi.org/10.2478/s11536-009-0132-4.

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AbstractAnti-annexin A5 antibodies are directed against annexin A5 — a phospholipid-binding protein that belongs to the ubiquitous annexin family. These antibodies were first discovered in 1994 by Matsuda et al. in women with recurrent fetal loss or preeclampsia and in patients with systemic lupus erythematosus and positive lupus anticoagulant and/or anticardiolipin antibodies. Since then anti-annexin A5 antibodies have been the focus of research. In addition to their well known prothrombotic and procoagulant activities the authors discuss the involvement of these antibodies in the pathogenesis of antiphospholipid syndrome, recurrent pregnancy loss, systemic lupus erythematosus and other immune and non-immune disorders. Controversial reports are presented and a possible interpretation of the results is given. The authors suggest the significance of anti-annexin A5 antibodies as an additional diagnostic marker and discuss the necessity of more extensive research on their clinical significance.

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10

Monceau, Virginie, Yulia Belikova, Gueorgui Kratassiouk, Estelle Robidel, Françoise Russo-Marie, and Daniele Charlemagne. "Myocyte apoptosis during acute myocardial infarction in rats is related to early sarcolemmal translocation of annexin A5 in border zone." American Journal of Physiology-Heart and Circulatory Physiology 291, no. 2 (August 2006): H965—H971. http://dx.doi.org/10.1152/ajpheart.01053.2005.

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Annexin A5 is a Ca2+-dependent phospholipid binding protein well known for its high phosphatidylserine affinity. In vitro, translocation to sarcolemma and externalization of endogenous annexin A5 in the cardiomyocyte has recently been demonstrated to exert a proapoptotic effect. To determine whether these in vitro findings occurred in vivo, we performed myocardial infarction (MI) and studied the time course of apoptosis and annexin A5 localization (0.5 to 8 h) in the border zone around the infarcted area. This zone that was defined as Evans blue unstained and triphenyltetrazolium chloride (TTC) stained, represented 42.3 ± 5.5% of the area at risk and showed apoptotic characteristics (significant increases in caspase 3 activity 2.3-fold at 0.5 h; P < 0.05), transferase-mediated dUTP nick-end labeling-positive cardiomyocytes (15.8 ± 0.8% at 8 h), and DNA ladder. When compared with sham-operated rats, we found that in this area, annexin A5 was translocated to the sarcolemma as early as 0.5 h after MI and that translocation increased with time. Moreover, the amount of annexin A5 was unchanged in the border zone and decreased in the infarcted area after 1 h (77.1 ± 4.8%; P < 0.01 vs. perfused area), suggesting a release in the latter but not in the former. In conclusion, we demonstrated that annexin A5 translocation is an early and rapid event of the whole border zone, likely due to Ca2+ increase. Part of this translocation occurred in areas where apoptosis was later detected and suggests that in vivo as in vitro annexin A5 might be involved in the regulation of early apoptotic events during cardiac pathological situations.

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11

WAHEZI, DAWN M., NORMAN T. ILOWITE, SWAPNIL RAJPATHAK, and JACOB H. RAND. "Prevalence of Annexin A5 Resistance in Children and Adolescents with Rheumatic Diseases." Journal of Rheumatology 39, no. 2 (December 15, 2011): 382–88. http://dx.doi.org/10.3899/jrheum.110768.

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Objective.The underlying mechanism(s) by which antiphospholipid antibodies (aPL) result in thrombosis remains poorly understood. A significant body of evidence has evolved to support the hypothesis that antibody-mediated disruption of an annexin A5 anticoagulant shield may play a role in the pathogenesis; this proposed mechanism has not been previously studied in children.Methods.We investigated the association between aPL and resistance to annexin A5 anticoagulant activity in 90 children with a variety of rheumatic diseases using a novel mechanistic assay, the annexin A5 resistance assay (A5R).Results.Patients with a diagnosis of primary aPL syndrome, systemic lupus erythematosus, and mixed connective tissue disease demonstrated lower mean A5R levels (p = 0.030), higher prevalence of positive aPL (p < 0.001), and more thrombotic events (p = 0.014) compared to those with other diagnoses. Patients with persistently positive aPL had significantly lower mean A5R compared to patients with no aPL (mean A5R = 203% ± 44% vs 247% ± 35%; p < 0.001), whereas patients with transient aPL did not. Patients with thrombosis had lower A5R levels compared to those without thrombosis (mean A5R = 207% ± 36% vs 237% ± 46%; p = 0.048).Conclusion.Children and adolescents with rheumatic diseases and persistent aPL have reduced annexin A5 anticoagulant activity, whereas transient, nonpathogenic aPL have less effect on annexin A5 activity.

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12

McQuade, Paul, Marie-Jose Belanger, Xiangjun Meng, Ilonka Guenther, Stephen Krause, Dinko Gonzalez Trotter, Chris Reutelingsperger, et al. "Comparison of the In Vivo Distribution of Four Different Annexin A5 Adducts in Rhesus Monkeys." International Journal of Molecular Imaging 2011 (May 4, 2011): 1–9. http://dx.doi.org/10.1155/2011/405840.

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Annexin A5 has been used for the detection of apoptotic cells, due to its ability to bind to phosphatidylserine (PS). Four different labeled Annexin A5 adducts were evaluated in rhesus monkey, with radiolabeling achieved via 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid (DOTA). Of these adducts differing conjugation methods were employed which resulted in nonspecific radiolabeling (AxA5-I), or site-specific radiolabeling (AxA5-II). A nonbinding variant of Annexin A5 was also evaluated (AxA5-IINBV ), conjugation here was site specific. The fourth adduct examined had both specific and nonspecific conjugation techniques employed (AxA5-IImDOTA ). Blood clearance for each adduct was comparable, while appreciable uptake was observed in kidney, liver, and spleen. Significant differences in uptake of AxA5-I and AxA5-II were observed, as well as between AxA5-II and AxA5-IINBV . No difference between AxA5-II and AxA5-IImDOTA was observed, suggesting that conjugating DOTA nonspecifically did not affect the in vivo biodistribution of Annexin A5.

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13

Morrone, Kerry A., Xue Xiaonan, Suzette O. Oyeku, Jane A. Little, Catherine Driscoll, Jacob Rand, and Deepa Manwani. "Association of Annexin A5 Resistance with Silent Infarct in Sickle Cell Disease." Blood 124, no. 21 (December 6, 2014): 1394. http://dx.doi.org/10.1182/blood.v124.21.1394.1394.

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Abstract Background: In sickle cell disease (SCD) abnormally shaped RBCs interact with white blood cells and the endothelium, leading to a vasculopathy and thrombotic/ prothrombotic complications such as stroke and pulmonary hypertension. About 10 % of patients with a thrombotic event in the general population will have the presence of an antiphospholipid (aPL) antibody (Andreoli et al. 2013). One proposed mechanism for the thrombophilic nature of aPL antibodies is the disruption of annexin A5. Annexin A5 is a potent anticoagulant protein that has an affinity to phospholipids. In the presence of aPL antibodies, annexin A5 is unable to form its crystallized anticoagulant shield (annexin A5 resistance). There is a paucity of data which assesses the association of aPL antibodies with vasculopathic complications of SCD, and there have been no studies investigating the annexin A5 resistance assay (A5R). We designed a pilot study assessing aPL antibody levels and A5R in a pediatric sickle cell population. Methods: Patients with a history of stroke, abnormal transcranial doppler (TCD) and elevated TR gradient by echocardiography (>25mm of Hg) were eligible. A5R, lupus anticoagulant- DRRVT, anti β2GP1, anti phosphatidylserine and anti cardiolipin antibody (IgG, IgA, IgM) assays were performed on samples obtained prospectively when patients were at a steady state (at least 4 weeks after an acute event). A5R measures coagulation times in the presence and absence of annexin A5. Resistance to the anticoagulant effects of annexin is expressed as a reduction in this ratio (Rand et al. 2004). Statistical analysis assessed multiple variables including age, gender, hemoglobin, reticulocyte count, LDH, hydroxyurea therapy, transfusion therapy, elevated TR gradient, stroke and silent stroke. Univariate analysis and multivariate logistic regression was performed with abnormal annexin A5 as the outcome variable. Results:There were a total of 39 patients: 12 patients with a history of stroke, 6 with an elevated TCD velocity and 15 patients with an elevated TR gradient. Of the 27 patients that did not have a stroke, 25 had a screening MRI in the prior year, and 9 of these patients had silent infarcts. Only 1 of 39 patients had elevated anticardiolipin IgG antibodies and 1 had an abnormal lupus coagulant (DRVVT). In contrast, 5/39 patients (12.8%) had low or abnormal annexin A5 resistance, 7/39 (18%) were in the borderline range and 27/39 (69%) were normal. This frequency of abnormality was unexpected in the antiphospolipid antibody and lupus anticoagulant negative population. None of the patients, except the one with the positive lupus anticoagulant, developed any thrombotic events in 3.5 years of follow up. None of the patients with overt stroke or abnormal TCDs had an abnormal A5R. Multivariate logistic regression analyses showed statistically significant association of hemoglobin (p= 0.037, OR 0.25, CI 0.07-0.92)), age (p =0.047, OR 1.43, CI 1.01-2.04) and silent infarct (p =0.015, OR 28.5, CI 1.9-420.5) with abnormal annexin A5 resistance. A multivariate analysis using linear regression with annexin A5 resistance as a continuous outcome variable (Table 1), showed persistence of the significant association of silent infarcts (p =0.037). Conclusion: We report an association between annexin A5 resistance and low hemoglobin, older age and presence of silent infarct in a subgroup of SCD patients. Prevalence of abnormal aPL antibody assays and lupus anticoagulant was strikingly low in this cohort. A potential role for perturbed annexin A5 resistance in the pathophysiology of silent infarction in SCD will need to be evaluated further in carefully designed prospective studies and may be a novel therapeutic target. Table 1. Hemoglobin, Age and Silent Stroke are Associated with Abnormal Annexin A5 Resistance Characteristic Odds Ratio Odds Ratio Confidence Interval p-value Hemoglobin* 0.25 0.07-0.92 0.037 Reticulocyte count 0.77 0.54-1.08 0.13 LDH 1.00 0.99-1.00 0.51 Age* 1.43 1.01-2.04 0.047 Monocyte count 1.00 1.00-1.00 0.34 Silent infarct* 28.5 1.9-420.5 0.015 Stroke 0.47 0.05-4.88 0.53 Elevated TR gradient 0.34 0.03-3.49 0.36 Gender 0.47 0.05-4.88 0.53 Allosensitization 0.56 0.05-5.86 0.63 HU vs no treatment 0.46 0.03-6.93 0.58 Transfusion vs no treatment 0.18 0.01-4.26 0.29 Disclosures No relevant conflicts of interest to declare.

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14

SEOK, HOSIK, HAE JEONG PARK, BYOUNG WOOK LEE, JONG WOO KIM, MIN JUNG, SEO RA LEE, KI HO PARK, YOUNG GUK PARK, HYUNG HWAN BAIK, and JOO-HO CHUNG. "Association of annexin A5 polymorphisms with obesity." Biomedical Reports 1, no. 4 (May 29, 2013): 654–58. http://dx.doi.org/10.3892/br.2013.118.

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15

Hiddink, Larissa, Bas de Laat, Ronald H. W. M. Derksen, Philip G. de Groot, and Waander L. van Heerde. "Annexin A5 haplotypes in the antiphospholipid syndrome." Thrombosis Research 135, no. 2 (February 2015): 417–19. http://dx.doi.org/10.1016/j.thromres.2014.12.004.

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16

Bouter, A., R. Carmeille, C. Gounou, F. Bouvet, S. A. Degrelle, D. Evain-Brion, and A. R. Brisson. "Review: Annexin-A5 and cell membrane repair." Placenta 36 (April 2015): S43—S49. http://dx.doi.org/10.1016/j.placenta.2015.01.193.

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17

Ghislat, G., C. Aguado, and E. Knecht. "Annexin A5 stimulates autophagy and inhibits endocytosis." Journal of Cell Science 125, no. 1 (January 1, 2012): 92–107. http://dx.doi.org/10.1242/jcs.086728.

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18

de Laat, B., R. H. W. M. Derksen, I. J. Mackie, M. Roest, S. Schoormans, B. J. Woodhams, P. G. de Groot, and W. L. van Heerde. "Annexin A5 polymorphism (-1C->T) and the presence of anti-annexin A5 antibodies in the antiphospholipid syndrome." Annals of the Rheumatic Diseases 65, no. 11 (November 1, 2006): 1468–72. http://dx.doi.org/10.1136/ard.2005.045237.

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19

Benali, Khadija, Liliane Louedec, Rana Ben Azzouna, Olivier Merceron, Pierre Nassar, Faisal Al Shoukr, Anne Petiet, et al. "Preclinical Validation of99mTc–Annexin A5–128 in Experimental Autoimmune Myocarditis and Infective Endocarditis: Comparison with99mTc–HYNIC–Annexin A5." Molecular Imaging 14, no. 1 (January 2015): 7290.2014.00049. http://dx.doi.org/10.2310/7290.2014.00049.

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20

Kenis, Heidi, Hugo van Genderen, Abdel Bennaghmouch, Hilde A. Rinia, Peter Frederik, Jagat Narula, Leo Hofstra, and Chris P. M. Reutelingsperger. "Cell Surface-expressed Phosphatidylserine and Annexin A5 Open a Novel Portal of Cell Entry." Journal of Biological Chemistry 279, no. 50 (September 20, 2004): 52623–29. http://dx.doi.org/10.1074/jbc.m409009200.

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Expression of phosphatidylserine (PtdSer) at the cell surface is part of the membrane dynamics of apoptosis. Expressed phosphatidylserine functions as an “eat me” flag toward phagocytes. Here, we report that the expressed phosphatidylserine forms part of a hitherto undescribed pinocytic pathway. Annexin A5, a phosphatidylserine-binding protein, binds to and polymerizes through protein-protein interactions on membrane patches expressing phosphatidylserine. The two-dimensional protein network of annexin A5 at the surface prevents apoptotic body formation without interfering with the progression of apoptosis as demonstrated by activation of caspase-3, PtdSer exposure, and DNA fragmentation. The annexin A5 protein network bends the membrane patch nanomechanically into the cell and elicits budding, endocytic vesicle formation, and cytoskeleton-dependent trafficking of the endocytic vesicle. Annexin A1, which binds to PtdSer without forming a two-dimensional protein network, does not induce the formation of endocytic vesicles. This novel pinocytic pathway differs from macropinocytosis, which is preceded by membrane ruffling and actin polymerization. We clearly showed that actin polymerization is not involved in budding and endocytic vesicle formation but is required for intracellular trafficking. The phosphatidylserine-annexin A5-mediated pinocytic pathway is not restricted to cells in apoptosis. We demonstrated that living tumor cells can take up substances through this novel portal of cell entry. This opens new avenues for targeted drug delivery and cell entry.

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Grewal, Thomas, Sundeep J. Wason, Carlos Enrich, and Carles Rentero. "Annexins – insights from knockout mice." Biological Chemistry 397, no. 10 (October 1, 2016): 1031–53. http://dx.doi.org/10.1515/hsz-2016-0168.

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AbstractAnnexins are a highly conserved protein family that bind to phospholipids in a calcium (Ca2+) – dependent manner. Studies with purified annexins, as well as overexpression and knockdown approaches identified multiple functions predominantly linked to their dynamic and reversible membrane binding behavior. However, most annexins are found at multiple locations and interact with numerous proteins. Furthermore, similar membrane binding characteristics, overlapping localizations and shared interaction partners have complicated identification of their precise functions. To gain insight into annexin functionin vivo, mouse models deficient of annexin A1 (AnxA1), A2, A4, A5, A6 and A7 have been generated. Interestingly, with the exception of one study, all mice strains lacking one or even two annexins are viable and develop normally. This suggested redundancy within annexins, but examining these knockout (KO) strains under stress conditions revealed striking phenotypes, identifying underlying mechanisms specific for individual annexins, often supporting Ca2+homeostasis and membrane transport as central for annexin biology. Conversely, mice lacking AnxA1 or A2 show extracellular functions relevant in health and disease that appear independent of membrane trafficking or Ca2+signaling. This review will summarize the mechanistic insights gained from studies utilizing mouse models lacking members of the annexin family.

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Montgomery, Samuel T., Stephen M. Stick, and Anthony Kicic. "An adapted novel flow cytometry methodology to delineate types of cell death in airway epithelial cells." Journal of Biological Methods 7, no. 4 (November 11, 2020): e139. http://dx.doi.org/10.14440/jbm.2020.336.

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Current methodologies to measure apoptotic and necrotic cell death using flow cytometry do not adequately differentiate between the two. Here, we describe a flow cytometry methodology adapted to airway epithelial cells (AEC) to sufficiently differentiate apoptotic and necrotic AEC. Specifically, cell lines and primary AEC (n = 12) were permeabilized or infected with rhinovirus 1b (RV1b) over 48 h. Cell death was then measured via annexin V/propidium iodide (A5/PI) or annexin V/TO-PRO-3 (A5/TP3) staining using a novel flow cytometry and gating methodology adapted to AEC. We show that A5/PI staining could not sufficiently differentiate between types of cell death following RV1b infection of primary AEC. However, A5/TP3 staining was able to distinguish six cell death populations (viable, necrotic, debris, A5+ apoptotic, A5− apoptotic, apoptotic bodies) after permeabilization or infection with RV1b, with phenotypic differences were observed in apoptotic populations. Collectively, using a staining and gating strategy never adapted to AEC, A5/TP3 could accurately differentiate and quantify viable, necrotic, and apoptotic AEC following RV1b infection.

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Kulkarni, Suhasini, Kevin J. Woollard, Stephen Thomas, David Oxley, and Shaun P. Jackson. "Conversion of platelets from a proaggregatory to a proinflammatory adhesive phenotype: role of PAF in spatially regulating neutrophil adhesion and spreading." Blood 110, no. 6 (September 15, 2007): 1879–86. http://dx.doi.org/10.1182/blood-2006-08-040980.

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Abstract The ability of platelets to provide a highly reactive surface for the recruitment of other platelets and leukocytes to sites of vascular injury is critical for hemostasis, atherothrombosis, and a variety of inflammatory diseases. The mechanisms coordinating platelet-platelet and platelet-leukocyte interactions have been well defined and, in general, it is assumed that increased platelet activation correlates with enhanced reactivity toward other platelets and neutrophils. In the current study, we demonstrate a differential role for platelets in supporting platelet and neutrophil adhesive interactions under flow. We demonstrate that the conversion of spread platelets to microvesiculated procoagulant (annexin A5–positive [annexin A5+ve]) forms reduces platelet-platelet adhesion and leads to a paradoxical increase in neutrophil-platelet interaction. This enhancement in neutrophil adhesion and spreading is partially mediated by the proinflammatory lipid, platelet-activating factor (PAF). PAF production, unlike other neutrophil chemokines (IL-8, GRO-α, NAP-2, IL-1β) is specifically and markedly up-regulated in annexin A5+ve cells. Physiologically, this spatially controlled production of PAF plays an important role in localizing neutrophils on the surface of thrombi. These studies define for the first time a specific proinflammatory function for annexin A5+ve platelets. Moreover, they demonstrate an important role for platelet-derived PAF in spatially regulating neutrophil adhesion under flow.

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Senzel, Lisa, Xiao-Xuan Wu, and Jacob Rand. "A Novel Flow Cytometric Annexin A5 Competition Assay for the Diagnosis of Antiphospholipid Syndrome." Blood 104, no. 11 (November 16, 2004): 4042. http://dx.doi.org/10.1182/blood.v104.11.4042.4042.

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Abstract Annexin A5 (A5) is a potent anticoagulant protein that crystallizes over phospholipid surfaces, shielding them from availability for coagulation enzyme reactions. The antiphospholipid antibody (aPL) syndrome (APS) is an autoimmune thrombophilia that is marked by the presence of antibodies against phospholipid-binding proteins and the paradoxical lupus anticoagulant phenomenon. aPL antibodies can promote coagulation by interfering with the crystallization of A5, thereby increasing the exposure of blood to thrombogenic anionic phospholipids. Since a flow cytometric assay for aPL measuring A5 binding to frozen thawed platelets was previously reported, we investigated whether phosphatidylserine-bound polystyrene beads could provide a robust platform for the assay. Beads were incubated with sera from patients with the aPL syndrome and from non-aPL controls. Fluorescence-tagged A5 was added and samples were analyzed by flow cytometry. Similarly treated beads were also used in coagulation assays to determine whether A5 anticoagulant function was also inhibited. Control sera permitted fluorescent labeling of nearly all beads. In contrast, sera from aPL syndrome patients produced a major population of unlabeled beads, sometimes accompanied by a minor population of labeled beads. 7 of 13 confirmed aPL syndrome patients, and 7 of 12 anticardiolipin antibody positive patients, demonstrated reduced A5 binding in this assay, while 10 of 10 healthy blood donor controls did not. Dilution of the aPL sera resulted in progressive increase of A5 binding. Reduction of A5 binding appeared to correlate with reduced A5 anticoagulant activity (r=0.42, n=33, p=.01). This assay shows promise for investigating the effects of aPL antibodies on A5 binding and for the clinical diagnosis of the aPL syndrome. Figure Figure Figure Figure

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EL-Gharib, M. N., T. M. Elhawary, S. H. Elshourbagy, and M. A. Morad. "Anti-annexin V Antibodies in Women with Recurrent Miscarriage." Clinical Medicine Insights: Reproductive Health 4 (January 2010): CMRH.S5835. http://dx.doi.org/10.4137/cmrh.s5835.

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Objective To determine the role of anti-annexin V antibodies (a-A5) as an etiologic factor in recurrent pregnancy failure. Study design Prospective observational study. Material and methods The study included ninety first trimester pregnant women who had a history of unexplained recurrent miscarriage (group I) with ninety well-matched pregnant women with a history of normal reproductive outcome allocated as control group (GII) and another ninety nonpregnant women (GIII). Sera from all women controls were analyzed for anti-annexin antibody measured by Elisa. Results The mean value of a-A5 was 11.37 ± 6.78, 7.7 ± 1.40 and 6.20 ± 0.95 ng/ml in groups I, II and III respectively. There was a significant increase in the mean value a-A5 among women with a history of recurrent miscarriage, compared with controls. The mean value was 13.92 ± 2.42 ng/ml among patients with unfavourable outcome, compared with a corresponding value of 6.95 V 0.58 ng/ml among women with favourable outcome. The receiver operator characteristic curve revealed that the cutoff value of a-A5 was 8.61 ng/ml. Conclusion This study emphasizes the relationship between anti-annexin V antibodies and recurrent miscarriage.

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Hrycek, Antoni, and Paweł Cieślik. "Annexin A5 and anti-annexin antibodies in patients with systemic lupus erythematosus." Rheumatology International 32, no. 5 (February 5, 2011): 1335–42. http://dx.doi.org/10.1007/s00296-011-1793-2.

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Саркисов, Артем, Artem Sarkisov, Владимир Зеленский, Vladimir Zelenskiy, Екатерина Полунина, Ekaterina Polunina, Карен Саркисов, and Karen Sarkisov. "ASSESSMENT OF THE LEVEL OF APOPTOSIS MARKER ANNEXIN A5 AND THE VALUE OF DENTAL INDICES IN OF VARYING SEVERITY WITHOUT GENERAL SOMATIC PATHOLOGY AND WITH BRONCHIECTATIC DISEASE." Actual problems in dentistry 15, no. 3 (October 25, 2019): 56–61. http://dx.doi.org/10.18481/2077-7566-2019-15-3-56-61.

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Background. The study of the features of the course and the general links of pathogenesis in patients with chronic generalized periodontitis (CGP) with comorbid pathology is one of the priorities of modern medicine. Objectives ― to assess and analyze the level of apoptosis marker annexin A5 and the value of dental indices in patients with CGP of varying severity without General somatic pathology and against the background of bronchiectatic disease Methods. The study involved 90 patients with present study included varying degrees (light, medium, heavy), which were divided into two groups: patients with no somatic pathology (n=40) and patients with comorbid pathology in the form of bronchoectatic disease (n=50). Somatically healthy individuals with intact periodontal disease (n=40) were examined as a control group. The values of dental indices – PMA, PI, Muhlemann and OHI-s. The level of annexin A5 was determined in the oral fluid by enzyme immunoassay. Results. In patients with CGP revealed a statistically significant higher value of the level of annexin A5 compared with somatically healthy individuals with intact periodontal and statistically significantly higher in patients with more severe periodontitis. At the same time, in patients with comorbid pathology, the level of annexin A5 in patients with CGP with bronchoectatic disease with mild, average and heavy degree of periodontitis is statistically significantly higher than in patients with CGP without somatic pathology. The revealed relationships between the value of dental indices and the level of annexin A5 indicate the influence of the studied marker of apoptosis on the state of periodontal tissues. Moreover, the patients with comorbidity the power value of the identified links more than the present study included patients with no somatic pathology. Conclusion. The obtained data show the influence on the currents present study included the presence of comorbid pathology in the form of bronchoectatic disease and presence of common mutually aggravating link of pathogenesis of apoptosis and the opportunity to use annexin A5 as predictive marker of progression, as the present study included patients with no somatic pathology and in the background bronchoectatic disease.

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Vasina, L. V. "Cellular and humoral apoptosis markers in acute coronary syndrome combined with essential hypertension." "Arterial’naya Gipertenziya" ("Arterial Hypertension") 14, no. 4 (August 28, 2008): 332–35. http://dx.doi.org/10.18705/1607-419x-2008-14-4-332-335.

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The aim of this work was to examine the contents of annexin A5, sApo-1/Fas and sBcl-2 and the number of circulating mononuclear cells in apoptosis in order to clarify their role in the pathogenesis of acute coronary syndrome (ACS) combined with arterial hypertension (AH). We examined 83 patients with ACS (47 patients with unstable angina and 36 with myocardial infarction) and 14 healthy individuals. AH has been identified in 15 patients with unstable angina and in 17 with myocardial infarction. The number of viable mononuclear cells was significantly decreased and the number of mononuclear cells at the early stages of apoptosis (annexin A5-positive) was significantly increased as compared to control group in patients with the ACS, especially if combined with AH. At the same time there was a significant increase of sBcl-2 and sApo-1/Fas and annexin A5 in blood of the patients with myocardial infarction compared to patients with unstable angina, especially if combined with AH. The association between the level of sAro-1/Fas, annexin A5 and the number of circulating mononuclear cells at the early stages of apoptosis was shown in the study. Thus, in ACS, especially if combined with AH, enhanced cell apoptosis resulting from hemodynamic abnormal changes leads to activation of antiapoptotic mechanisms aimed at the decrease of the thrombophilia severity by reducing thrombogenic features of endotheliocytes subjected to apoptosis.

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Mittag, Jens, Wiebke Oehr, Heike Heuer, Tuula Hämäläinen, Bent Brachvogel, Ernst Pöschl, and Karl Bauer. "Expression and thyroid hormone regulation of annexins in the anterior pituitary." Journal of Endocrinology 195, no. 3 (September 13, 2007): 385–92. http://dx.doi.org/10.1677/joe-07-0042.

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Due to their property to bind to phospholipids in a Ca2+-dependent manner, proteins of the annexin superfamily are involved in many membrane-related events and thus in various forms of physiological and pathological processes. We were therefore interested in analyzing the mRNA expression of the annexins in the severely disorganized pituitaries of the athyroid Pax8−/− mice in comparison with that of control animals. In neither condition was mRNA expression of the annexins A3, A7, A8, A9, A11, and A13 detectable. The annexins A2, A4, and A6 were equally expressed in wild-type and Pax8−/− mice. Transcript levels of A1 and A10 were highly increased and those of A5 were significantly decreased in the athyroid mutants compared with controls. Treatment of Pax8−/− mice with physiological doses of thyroxine for 3 days normalized the mRNA expression of A1, A5, and A10 indicating that the expression of these annexins is directly regulated by thyroid hormone (TH). Since A5 exhibits by far the highest transcript levels of all annexins in the pituitary and its regulation by TH could be also confirmed at the protein level, we analyzed the mRNA expression of pituitary hormones in A5−/− mice. In these mutants, only the β-FSH mRNA expression was found to be significantly reduced, while the mRNA expression levels of the other pituitary hormones were not altered. These results support the concept that annexins might serve important albeit redundant functions as modulators of pituitary hormone secretion.

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Ornaghi, S., P. Vergani, G. Urban, V. Giardini, F. Moltrasio, and B. E. Leone. "Immunohistochemical expression of Annexin A5 in preeclamptic placentas☆." Placenta 32, no. 3 (March 2011): 264–68. http://dx.doi.org/10.1016/j.placenta.2010.12.015.

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Brisson, Alain, Anthony Bouter, Romain Carmeille, Sisareuth Tan, Celine Gounou, Severine Degrelle, Guillaume Pidoux, and Daniele Evain-Brion. "Annexin-A5 and membrane repair in the placenta." Placenta 35, no. 9 (September 2014): A5. http://dx.doi.org/10.1016/j.placenta.2014.06.017.

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Cederholm, A., and J. Frostegard. "Annexin A5 multitasking: A potentially novel antiatherothrombotic agent?" Drug News & Perspectives 20, no. 5 (2007): 321. http://dx.doi.org/10.1358/dnp.2007.20.5.1120220.

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Carmeille, Romain, Séverine A. Degrelle, Laurent Plawinski, Flora Bouvet, Céline Gounou, Danièle Evain-Brion, Alain R. Brisson, and Anthony Bouter. "Annexin-A5 promotes membrane resealing in human trophoblasts." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1853, no. 9 (September 2015): 2033–44. http://dx.doi.org/10.1016/j.bbamcr.2014.12.038.

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Laufer, Edward M., Chris P. M. Reutelingsperger, Jagat Narula, and Leonard Hofstra. "Annexin A5: an imaging biomarker of cardiovascular risk." Basic Research in Cardiology 103, no. 2 (March 2008): 95–104. http://dx.doi.org/10.1007/s00395-008-0701-8.

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Simon, Anne, Céline Gounou, Sisareuth Tan, Louis Tiefenauer, Marco Di Berardino, and Alain R. Brisson. "Free-standing lipid films stabilized by Annexin-A5." Biochimica et Biophysica Acta (BBA) - Biomembranes 1828, no. 11 (November 2013): 2739–44. http://dx.doi.org/10.1016/j.bbamem.2013.07.028.

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Rice, Anne M., Samantha Jaworski, Michael E. Fealey, Anika Rannikko, and Anne Hinderliter. "Membrane Regulation and Signal Transduction by Annexin A5." Biophysical Journal 106, no. 2 (January 2014): 97a. http://dx.doi.org/10.1016/j.bpj.2013.11.608.

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Peng, Boya, Chunmei Guo, Hongwei Guan, Shuqing Liu, and Ming-Zhong Sun. "Annexin A5 as a potential marker in tumors." Clinica Chimica Acta 427 (January 2014): 42–48. http://dx.doi.org/10.1016/j.cca.2013.09.048.

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38

van Tits, Berry, Waander van Heerde, Precious Landburg, Frits Muskiet, Ashley Duits, and John-John Schnog. "The Plasma Concentration of the Antithrombotic Protein Annexin A5 Is Elevated in Sickle Cell Disease and Rises Further during Painful Crisis." Blood 112, no. 11 (November 16, 2008): 4820. http://dx.doi.org/10.1182/blood.v112.11.4820.4820.

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Abstract Expression of phosphatidylserine (PS) on the membrane surface of red blood cells and circulating microparticles plays an important role in the etiology of the hypercoagulable state of sickle cell disease (SCD), as well as in the reduced red cell life span and adhesive interactions between red cells and endothelium. Annexin A5, an intracellular protein abundantly present in endothelial cells, exhibits high affinity for PS and has been shown to inhibit microparticle-induced PS-mediated thrombin generation. We determined plasma annexin A5 levels and microparticles in 17 sickle cell patients (12 HbSS and 5 HbSC) in steady state and at presentation with a painful crisis. Twenty five HbAA blood donors served as controls. Both annexin A5 levels and microparticle numbers were highest in HbSS patients (5.7 ng/mL IQR 3.7–7.6 and 37.9 nM, IQR 31.9–69.8) as compared to HbSC patients (1.8 ng/mL, IQR 1.7–7.6 and 20.9 nM IQR10.9–29.6) and healthy controls (2.5 ng/mL, IQR 1.4–4.4 and 13.1 nM, IQR 9.5–18.5) (p=0.01 and p<0.001, respectively). At presentation with a painful crisis, annexin V levels and microparticle numbers increased significantly in 16 of 17 patients (p=0.001) and 16 of 17 patients (p<0.001), respectively. Annexin V/microparticle ratio’s were lower at presentation with a painful crisis in 9 patients. In conclusion, sickle cell patients have elevated plasma concentrations of annexin V. The potential role of annexin V in modulating PS related pathophysiological processes in SCD is subject of further investigation.

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Rand, Jacob H., Alan A. Arslan, Xiao-Xuan Wu, Rosemary Wein, Jeanine Mulholland, Manish Shah, Waander L. van Heerde, Chris P. Reutelingsperger, Charles J. Lockwood, and Edward Kuczynski. "Reduction of circulating annexin A5 levels and resistance to annexin A5 anticoagulant activity in women with recurrent spontaneous pregnancy losses." American Journal of Obstetrics and Gynecology 194, no. 1 (January 2006): 182–88. http://dx.doi.org/10.1016/j.ajog.2005.05.034.

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Gaspersic, N., A. Ambrozic, B. Bozic, J. Majhenc, S. Svetina, and B. Rozman. "Annexin A5 binding to giant phospholipid vesicles is differentially affected by anti- 2-glycoprotein I and anti-annexin A5 antibodies." Rheumatology 46, no. 1 (January 1, 2007): 81–86. http://dx.doi.org/10.1093/rheumatology/kel200.

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Tiscia, Giovanni Luca, Elisabeth Dørum, Christiane Filion Myklebust, Elvira Grandone, Per Morten Sandset, and Grethe Skretting. "Functional characterization of annexin A5 gene promoter allelic variants." Thrombosis Research 144 (August 2016): 93–99. http://dx.doi.org/10.1016/j.thromres.2016.06.009.

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Garnier, Boris, Anthony Bouter, Céline Gounou, Klaus G. Petry, and Alain R. Brisson. "Annexin A5-Functionalized Liposomes for Targeting Phosphatidylserine-Exposing Membranes." Bioconjugate Chemistry 20, no. 11 (November 18, 2009): 2114–22. http://dx.doi.org/10.1021/bc9002579.

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43

Stöcker, Michael, Alessa Pardo, Christian Hetzel, Chris Reutelingsperger, Rainer Fischer, and Stefan Barth. "Eukaryotic expression and secretion of EGFP-labeled annexin A5." Protein Expression and Purification 58, no. 2 (April 2008): 325–31. http://dx.doi.org/10.1016/j.pep.2007.12.009.

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Degrelle, Severine, Pascale Gerbaud, Anthony Bouter, Jean Guibourdenche, Alain Brisson, Daniele Evain-Brion, and Guillaume Pidoux. "Annexin A5 as a biomarker of placenta membrane integrity?" Placenta 35, no. 9 (September 2014): A107—A108. http://dx.doi.org/10.1016/j.placenta.2014.06.351.

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Sohma, Hitoshi, Mami Yamaguchi, Shin-ichi Imai, Kumiko Utsumi, Kyoichi Matsumoto, Hirohito Honda, Yuka Mizue, Masako Momma, Yoichi Ito, and Yasuo Kokai. "Annexin A5 is a potential biomarker for Alzheimer disease." Neuroscience Research 68 (January 2010): e66-e67. http://dx.doi.org/10.1016/j.neures.2010.07.060.

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Schmidt, Vanessa, Cristiano Giacomelli, François Lecolley, Joséphine Lai-Kee-Him, Alain R. Brisson, and Redouane Borsali. "Diblock Copolymer Micellar Nanoparticles Decorated with Annexin-A5 Proteins." Journal of the American Chemical Society 128, no. 28 (July 2006): 9010–11. http://dx.doi.org/10.1021/ja062408n.

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Stöhr, Robert, Leon Schurgers, Rick van Gorp, Armand Jaminon, Nikolaus Marx, and Chris Reutelingsperger. "Annexin A5 reduces early plaque formation in ApoE -/- mice." PLOS ONE 12, no. 12 (December 21, 2017): e0190229. http://dx.doi.org/10.1371/journal.pone.0190229.

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Božič, Borut, Špela Irman, Nataša Gašperšič, Tanja Kveder, and Blaž Rozman. "Antibodies against annexin A5: Detection pitfalls and clinical associations." Autoimmunity 38, no. 6 (January 2005): 425–30. http://dx.doi.org/10.1080/08916930500288356.

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HENDRIKUS, H., H. BOERSMA, S. WOLTERS, A. PETROV, M. SARAI, J. NARULA, G. HEIDENDAL, L. HOFSTRA, and C. REUTELINGSPERGER. "10.4Minimisation of infarct size with minocycline:imaging with annexin-A5." Journal of Nuclear Cardiology 14, no. 2 (March 2007): S77. http://dx.doi.org/10.1016/j.nuclcard.2006.12.306.

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Ravassa, Susana, Abdelkader Bennaghmouch, Heidi Kenis, Theo Lindhout, Tilman Hackeng, Jagat Narula, Leo Hofstra, and Chris Reutelingsperger. "Annexin A5 Down-regulates Surface Expression of Tissue Factor." Journal of Biological Chemistry 280, no. 7 (December 2, 2004): 6028–35. http://dx.doi.org/10.1074/jbc.m411710200.

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