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A7 is thought to have a role in vesicle fusion and in regulating and stabilizing membrane domains [1]. The protein has been localized to the plasma membrane including raft subdomains, furthermore it is present in the cytosol where it is found on subcellular vesicle-like structures. This distribution appears to be independent of the tissue or cell type analysed. In specialized or terminally differentiated cells, expression levels increase and frequently the larger of the two isoforms is being expressed [6,34,35].\nRed blood cells, which were thought to be devoid of annexin A7, were recently shown to harbor the 47 kDa isoform together with its binding partner sorcin [7]. We showed the presence of the 51 kDa isoform as well, adding red blood cells to the list of cells that harbor this isoform. Salzer et al. [7] not only demonstrated the presence of annexin A7 in red blood cells, they also showed that annexin A7 and sorcin were enriched in membrane raft domains of nanovesicles formed from red blood cells in vitro. Raft domains in general are considered key players in membrane organization and in mediating the vesiculation process. They result from the clustering of sphingolipids and cholesterol in the outer leaflet of the membrane connected to phospholipids and cholesterol in the inner leaflet and are enriched in special proteins. Biochemically rafts are defined as membranes that are resistant to extraction by cold Triton X-100 and can be floated to low densities in sucrose gradient centrifugation [36].\nThe findings of Caohuy et al. [37] that annexin A7 mediates membrane aggregation also suggested that annexin A7 is an essential component during vesiculation. In addition they reported a further activation of the vesiculation process by GTP and proposed that annexin A7 acts as a GTPase. Similarly, the presence of GTP enhanced the secretion of surfactant by annexin A7. These results were thought to support a direct role for annexin A7 in surfactant secretion, but in these studies annexin A7 mediated membrane fusion was separated from a second GTP-dependent mechanism [38].\nHaving an annexin A7 knockout mouse we tested the involvement of annexin A7 in budding of red blood cell vesicles. Our data suggest that the efficiency of micro- and nanovesicle formation is not significantly different in wild type and mutant red blood cells. Likewise, Dictyostelium discoideum cells, in which the single annexin gene was inactivated, were not impaired in processes requiring membrane fusion [[39]; and data unpublished]. It might well be that the observed fusion of phospholipid layers by annexin A7 in the presence of high Ca2+ concentrations may turn out to be an in vitro effect. Similarly, the high abundance of annexin A7 in micro- and nanovesicles might be fortuitous as a significant percentage of the red blood cell membrane, with which annexin A7 associates when the Ca2+ levels rise, appears to be involved in the formation of exovesicles. Furthermore, the distribution of both annexin A7 isoforms in gradients of red blood cells indicates a function which differs from organizing subcellular membranes or membrane pathways. Whereas annexin A2 is tightly associated with endosomes and may have functions in membrane fusion and the endosomal pathway, annexin A7 distributes with plasma membrane raft domains of different types and densities. Interestingly, in vesicles of red blood cells lacking annexin A7 the amount of sorcin is lowered, indicating that its localisation is affected by the loss of annexin A7 or its expression during red blood cell development was reduced.\nHaving excluded a direct role in vesicle formation and membrane fusion, annexin A7 might act by its property as Ca2+-binding protein [17]. Previous results in which annexin A7 was shown to play a role in membrane aggregation might be explained by a supportive function of annexin A7 in that it interferes with the local Ca2+ homeostasis thus influencing membrane organization. As the annexins belong to a wide spread and evolutionarily conserved protein family, redundant, but not identical functions are expected. However, so far no other members of the annexin family, which may substitute for annexin A7, have been described in red blood cells.\nThe structural basis for the elasticy of red blood cells in circulation are long range molecular functions of the plasma membrane and the membrane associated part of the cytoskeleton [40-43]. Major constituents of the membrane skeleton are spectrin tetramers linked together by short actin filaments and several other proteins covering the entire cytoplasmic surface of the red blood cell membrane [44]. Membrane cholesterol diminishes red blood cell haemolysis by the complement complex, whereas depletion of raft cholesterol abrogates association of all raft proteins with no significant effect on areas in the rest of the cell membrane and deformability [45,46].\nAnnexin A7 knock out mouse red blood cells show a more flat shape and have a higher osmotic resistance. The presence of annexin A7 may alter the membrane flexibility in that it supports the typical biconcave membrane shape and leads to a lower minimal osmotic resistance. Annexin A7 does not appear to have an influence on plasma membrane integrity itself as the maximal osmotic resistance value stays constant. Ca2+ and membrane skeletal proteins are known to play key roles on the red blood cell membrane shape and stability [47]. Annexins have been reported to bind directly to F-actin, we could however exclude such an activity for annexin A7. Nevertheless it might interact with other components and have a role in organizing the membrane cytoskeleton, controlling raft protein associations or influencing the ionic strength of red blood cells on its own or by interfering with other signaling pathways.\nAs discussed above annexin A7 could be involved in the cytoplasmic Ca2+ homeostasis. It has been demonstrated that micromolar changes of the intracellular Ca2+ concentration exert a profound effect on the membrane properties that regulate red blood cell deformability [48,49]. Furthermore, the intracellular Ca2+ was shown to regulate the membrane stability through modulation of cytoskeletal protein interactions [50]. Ca2+ also induces a transbilayer phospholipid redistribution inducing a shape change of red blood cells [51]. In addition, Ca2+ ions can drive spiculation of the membrane bilayer without involving the cytoskeleton [52].\nWe have also observed a defect in platelet function in the annexin A7 mutant. In the platelet aggregation experiments the initial aggregation velocity was slightly, but significantly lower in platelets lacking annexin A7. These data are not reflected by a change in the in vivo bleeding time. However the reaction speed of murine platelets is much higher than those of human and due to the technical setup we might have missed larger changes in the mouse samples. The immediate reaction of mouse platelets and the absence of a lag phase after triggering may be caused by an immediately initiated thrombin generation [22]. As known from the frequent human vWF-syndrome or other haemostatic diseases, small defects often are clinically silent and do not result in physiological changes under normal conditions. Only in situations with severe physical injury, distinct environmental influences or additional platelet attributes like the platelet antigen polymorphism [53] differences might become apparent."}

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A7 is thought to have a role in vesicle fusion and in regulating and stabilizing membrane domains [1]. The protein has been localized to the plasma membrane including raft subdomains, furthermore it is present in the cytosol where it is found on subcellular vesicle-like structures. This distribution appears to be independent of the tissue or cell type analysed. In specialized or terminally differentiated cells, expression levels increase and frequently the larger of the two isoforms is being expressed [6,34,35].\nRed blood cells, which were thought to be devoid of annexin A7, were recently shown to harbor the 47 kDa isoform together with its binding partner sorcin [7]. We showed the presence of the 51 kDa isoform as well, adding red blood cells to the list of cells that harbor this isoform. Salzer et al. [7] not only demonstrated the presence of annexin A7 in red blood cells, they also showed that annexin A7 and sorcin were enriched in membrane raft domains of nanovesicles formed from red blood cells in vitro. Raft domains in general are considered key players in membrane organization and in mediating the vesiculation process. They result from the clustering of sphingolipids and cholesterol in the outer leaflet of the membrane connected to phospholipids and cholesterol in the inner leaflet and are enriched in special proteins. Biochemically rafts are defined as membranes that are resistant to extraction by cold Triton X-100 and can be floated to low densities in sucrose gradient centrifugation [36].\nThe findings of Caohuy et al. [37] that annexin A7 mediates membrane aggregation also suggested that annexin A7 is an essential component during vesiculation. In addition they reported a further activation of the vesiculation process by GTP and proposed that annexin A7 acts as a GTPase. Similarly, the presence of GTP enhanced the secretion of surfactant by annexin A7. These results were thought to support a direct role for annexin A7 in surfactant secretion, but in these studies annexin A7 mediated membrane fusion was separated from a second GTP-dependent mechanism [38].\nHaving an annexin A7 knockout mouse we tested the involvement of annexin A7 in budding of red blood cell vesicles. Our data suggest that the efficiency of micro- and nanovesicle formation is not significantly different in wild type and mutant red blood cells. Likewise, Dictyostelium discoideum cells, in which the single annexin gene was inactivated, were not impaired in processes requiring membrane fusion [[39]; and data unpublished]. It might well be that the observed fusion of phospholipid layers by annexin A7 in the presence of high Ca2+ concentrations may turn out to be an in vitro effect. Similarly, the high abundance of annexin A7 in micro- and nanovesicles might be fortuitous as a significant percentage of the red blood cell membrane, with which annexin A7 associates when the Ca2+ levels rise, appears to be involved in the formation of exovesicles. Furthermore, the distribution of both annexin A7 isoforms in gradients of red blood cells indicates a function which differs from organizing subcellular membranes or membrane pathways. Whereas annexin A2 is tightly associated with endosomes and may have functions in membrane fusion and the endosomal pathway, annexin A7 distributes with plasma membrane raft domains of different types and densities. Interestingly, in vesicles of red blood cells lacking annexin A7 the amount of sorcin is lowered, indicating that its localisation is affected by the loss of annexin A7 or its expression during red blood cell development was reduced.\nHaving excluded a direct role in vesicle formation and membrane fusion, annexin A7 might act by its property as Ca2+-binding protein [17]. Previous results in which annexin A7 was shown to play a role in membrane aggregation might be explained by a supportive function of annexin A7 in that it interferes with the local Ca2+ homeostasis thus influencing membrane organization. As the annexins belong to a wide spread and evolutionarily conserved protein family, redundant, but not identical functions are expected. However, so far no other members of the annexin family, which may substitute for annexin A7, have been described in red blood cells.\nThe structural basis for the elasticy of red blood cells in circulation are long range molecular functions of the plasma membrane and the membrane associated part of the cytoskeleton [40-43]. Major constituents of the membrane skeleton are spectrin tetramers linked together by short actin filaments and several other proteins covering the entire cytoplasmic surface of the red blood cell membrane [44]. Membrane cholesterol diminishes red blood cell haemolysis by the complement complex, whereas depletion of raft cholesterol abrogates association of all raft proteins with no significant effect on areas in the rest of the cell membrane and deformability [45,46].\nAnnexin A7 knock out mouse red blood cells show a more flat shape and have a higher osmotic resistance. The presence of annexin A7 may alter the membrane flexibility in that it supports the typical biconcave membrane shape and leads to a lower minimal osmotic resistance. Annexin A7 does not appear to have an influence on plasma membrane integrity itself as the maximal osmotic resistance value stays constant. Ca2+ and membrane skeletal proteins are known to play key roles on the red blood cell membrane shape and stability [47]. Annexins have been reported to bind directly to F-actin, we could however exclude such an activity for annexin A7. Nevertheless it might interact with other components and have a role in organizing the membrane cytoskeleton, controlling raft protein associations or influencing the ionic strength of red blood cells on its own or by interfering with other signaling pathways.\nAs discussed above annexin A7 could be involved in the cytoplasmic Ca2+ homeostasis. It has been demonstrated that micromolar changes of the intracellular Ca2+ concentration exert a profound effect on the membrane properties that regulate red blood cell deformability [48,49]. Furthermore, the intracellular Ca2+ was shown to regulate the membrane stability through modulation of cytoskeletal protein interactions [50]. Ca2+ also induces a transbilayer phospholipid redistribution inducing a shape change of red blood cells [51]. In addition, Ca2+ ions can drive spiculation of the membrane bilayer without involving the cytoskeleton [52].\nWe have also observed a defect in platelet function in the annexin A7 mutant. In the platelet aggregation experiments the initial aggregation velocity was slightly, but significantly lower in platelets lacking annexin A7. These data are not reflected by a change in the in vivo bleeding time. However the reaction speed of murine platelets is much higher than those of human and due to the technical setup we might have missed larger changes in the mouse samples. The immediate reaction of mouse platelets and the absence of a lag phase after triggering may be caused by an immediately initiated thrombin generation [22]. As known from the frequent human vWF-syndrome or other haemostatic diseases, small defects often are clinically silent and do not result in physiological changes under normal conditions. Only in situations with severe physical injury, distinct environmental influences or additional platelet attributes like the platelet antigen polymorphism [53] differences might become apparent."}

{"project":"2_test","denotations":[{"id":"12925238-632306-8102400","span":{"begin":118,"end":119},"obj":"632306"},{"id":"12925238-11338180-8102401","span":{"begin":527,"end":528},"obj":"11338180"},{"id":"12925238-1825209-8102402","span":{"begin":529,"end":531},"obj":"1825209"},{"id":"12925238-10672515-8102403","span":{"begin":532,"end":534},"obj":"10672515"},{"id":"12925238-11895795-8102404","span":{"begin":692,"end":693},"obj":"11895795"},{"id":"12925238-11895795-8102405","span":{"begin":835,"end":836},"obj":"11895795"},{"id":"12925238-12208858-8102406","span":{"begin":1538,"end":1540},"obj":"12208858"},{"id":"12925238-8855260-8102407","span":{"begin":1574,"end":1576},"obj":"8855260"},{"id":"12925238-11290524-8102408","span":{"begin":2116,"end":2118},"obj":"11290524"},{"id":"12925238-7657724-8102409","span":{"begin":2532,"end":2534},"obj":"7657724"},{"id":"12925238-11390641-8102410","span":{"begin":3758,"end":3760},"obj":"11390641"},{"id":"12925238-3862123-8102411","span":{"begin":4456,"end":4458},"obj":"3862123"},{"id":"12925238-1540701-8102411","span":{"begin":4456,"end":4458},"obj":"1540701"},{"id":"12925238-8211222-8102411","span":{"begin":4456,"end":4458},"obj":"8211222"},{"id":"12925238-8434261-8102412","span":{"begin":4671,"end":4673},"obj":"8434261"},{"id":"12925238-9761744-8102413","span":{"begin":4930,"end":4932},"obj":"9761744"},{"id":"12925238-11352913-8102414","span":{"begin":4933,"end":4935},"obj":"11352913"},{"id":"12925238-1398703-8102415","span":{"begin":5466,"end":5468},"obj":"1398703"},{"id":"12925238-154737-8102416","span":{"begin":6116,"end":6118},"obj":"154737"},{"id":"12925238-9435486-8102417","span":{"begin":6119,"end":6121},"obj":"9435486"},{"id":"12925238-3403710-8102418","span":{"begin":6262,"end":6264},"obj":"3403710"},{"id":"12925238-8003498-8102419","span":{"begin":6372,"end":6374},"obj":"8003498"},{"id":"12925238-7131536-8102420","span":{"begin":6482,"end":6484},"obj":"7131536"},{"id":"12925238-11713907-8102421","span":{"begin":7104,"end":7106},"obj":"11713907"}],"text":"Discussion\nAnnexin A7 is thought to have a role in vesicle fusion and in regulating and stabilizing membrane domains [1]. The protein has been localized to the plasma membrane including raft subdomains, furthermore it is present in the cytosol where it is found on subcellular vesicle-like structures. This distribution appears to be independent of the tissue or cell type analysed. In specialized or terminally differentiated cells, expression levels increase and frequently the larger of the two isoforms is being expressed [6,34,35].\nRed blood cells, which were thought to be devoid of annexin A7, were recently shown to harbor the 47 kDa isoform together with its binding partner sorcin [7]. We showed the presence of the 51 kDa isoform as well, adding red blood cells to the list of cells that harbor this isoform. Salzer et al. [7] not only demonstrated the presence of annexin A7 in red blood cells, they also showed that annexin A7 and sorcin were enriched in membrane raft domains of nanovesicles formed from red blood cells in vitro. Raft domains in general are considered key players in membrane organization and in mediating the vesiculation process. They result from the clustering of sphingolipids and cholesterol in the outer leaflet of the membrane connected to phospholipids and cholesterol in the inner leaflet and are enriched in special proteins. Biochemically rafts are defined as membranes that are resistant to extraction by cold Triton X-100 and can be floated to low densities in sucrose gradient centrifugation [36].\nThe findings of Caohuy et al. [37] that annexin A7 mediates membrane aggregation also suggested that annexin A7 is an essential component during vesiculation. In addition they reported a further activation of the vesiculation process by GTP and proposed that annexin A7 acts as a GTPase. Similarly, the presence of GTP enhanced the secretion of surfactant by annexin A7. These results were thought to support a direct role for annexin A7 in surfactant secretion, but in these studies annexin A7 mediated membrane fusion was separated from a second GTP-dependent mechanism [38].\nHaving an annexin A7 knockout mouse we tested the involvement of annexin A7 in budding of red blood cell vesicles. Our data suggest that the efficiency of micro- and nanovesicle formation is not significantly different in wild type and mutant red blood cells. Likewise, Dictyostelium discoideum cells, in which the single annexin gene was inactivated, were not impaired in processes requiring membrane fusion [[39]; and data unpublished]. It might well be that the observed fusion of phospholipid layers by annexin A7 in the presence of high Ca2+ concentrations may turn out to be an in vitro effect. Similarly, the high abundance of annexin A7 in micro- and nanovesicles might be fortuitous as a significant percentage of the red blood cell membrane, with which annexin A7 associates when the Ca2+ levels rise, appears to be involved in the formation of exovesicles. Furthermore, the distribution of both annexin A7 isoforms in gradients of red blood cells indicates a function which differs from organizing subcellular membranes or membrane pathways. Whereas annexin A2 is tightly associated with endosomes and may have functions in membrane fusion and the endosomal pathway, annexin A7 distributes with plasma membrane raft domains of different types and densities. Interestingly, in vesicles of red blood cells lacking annexin A7 the amount of sorcin is lowered, indicating that its localisation is affected by the loss of annexin A7 or its expression during red blood cell development was reduced.\nHaving excluded a direct role in vesicle formation and membrane fusion, annexin A7 might act by its property as Ca2+-binding protein [17]. Previous results in which annexin A7 was shown to play a role in membrane aggregation might be explained by a supportive function of annexin A7 in that it interferes with the local Ca2+ homeostasis thus influencing membrane organization. As the annexins belong to a wide spread and evolutionarily conserved protein family, redundant, but not identical functions are expected. However, so far no other members of the annexin family, which may substitute for annexin A7, have been described in red blood cells.\nThe structural basis for the elasticy of red blood cells in circulation are long range molecular functions of the plasma membrane and the membrane associated part of the cytoskeleton [40-43]. Major constituents of the membrane skeleton are spectrin tetramers linked together by short actin filaments and several other proteins covering the entire cytoplasmic surface of the red blood cell membrane [44]. Membrane cholesterol diminishes red blood cell haemolysis by the complement complex, whereas depletion of raft cholesterol abrogates association of all raft proteins with no significant effect on areas in the rest of the cell membrane and deformability [45,46].\nAnnexin A7 knock out mouse red blood cells show a more flat shape and have a higher osmotic resistance. The presence of annexin A7 may alter the membrane flexibility in that it supports the typical biconcave membrane shape and leads to a lower minimal osmotic resistance. Annexin A7 does not appear to have an influence on plasma membrane integrity itself as the maximal osmotic resistance value stays constant. Ca2+ and membrane skeletal proteins are known to play key roles on the red blood cell membrane shape and stability [47]. Annexins have been reported to bind directly to F-actin, we could however exclude such an activity for annexin A7. Nevertheless it might interact with other components and have a role in organizing the membrane cytoskeleton, controlling raft protein associations or influencing the ionic strength of red blood cells on its own or by interfering with other signaling pathways.\nAs discussed above annexin A7 could be involved in the cytoplasmic Ca2+ homeostasis. It has been demonstrated that micromolar changes of the intracellular Ca2+ concentration exert a profound effect on the membrane properties that regulate red blood cell deformability [48,49]. Furthermore, the intracellular Ca2+ was shown to regulate the membrane stability through modulation of cytoskeletal protein interactions [50]. Ca2+ also induces a transbilayer phospholipid redistribution inducing a shape change of red blood cells [51]. In addition, Ca2+ ions can drive spiculation of the membrane bilayer without involving the cytoskeleton [52].\nWe have also observed a defect in platelet function in the annexin A7 mutant. In the platelet aggregation experiments the initial aggregation velocity was slightly, but significantly lower in platelets lacking annexin A7. These data are not reflected by a change in the in vivo bleeding time. However the reaction speed of murine platelets is much higher than those of human and due to the technical setup we might have missed larger changes in the mouse samples. The immediate reaction of mouse platelets and the absence of a lag phase after triggering may be caused by an immediately initiated thrombin generation [22]. As known from the frequent human vWF-syndrome or other haemostatic diseases, small defects often are clinically silent and do not result in physiological changes under normal conditions. Only in situations with severe physical injury, distinct environmental influences or additional platelet attributes like the platelet antigen polymorphism [53] differences might become apparent."}

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A7 is thought to have a role in vesicle fusion and in regulating and stabilizing membrane domains [1]. The protein has been localized to the plasma membrane including raft subdomains, furthermore it is present in the cytosol where it is found on subcellular vesicle-like structures. This distribution appears to be independent of the tissue or cell type analysed. In specialized or terminally differentiated cells, expression levels increase and frequently the larger of the two isoforms is being expressed [6,34,35].\nRed blood cells, which were thought to be devoid of annexin A7, were recently shown to harbor the 47 kDa isoform together with its binding partner sorcin [7]. We showed the presence of the 51 kDa isoform as well, adding red blood cells to the list of cells that harbor this isoform. Salzer et al. [7] not only demonstrated the presence of annexin A7 in red blood cells, they also showed that annexin A7 and sorcin were enriched in membrane raft domains of nanovesicles formed from red blood cells in vitro. Raft domains in general are considered key players in membrane organization and in mediating the vesiculation process. They result from the clustering of sphingolipids and cholesterol in the outer leaflet of the membrane connected to phospholipids and cholesterol in the inner leaflet and are enriched in special proteins. Biochemically rafts are defined as membranes that are resistant to extraction by cold Triton X-100 and can be floated to low densities in sucrose gradient centrifugation [36].\nThe findings of Caohuy et al. [37] that annexin A7 mediates membrane aggregation also suggested that annexin A7 is an essential component during vesiculation. In addition they reported a further activation of the vesiculation process by GTP and proposed that annexin A7 acts as a GTPase. Similarly, the presence of GTP enhanced the secretion of surfactant by annexin A7. These results were thought to support a direct role for annexin A7 in surfactant secretion, but in these studies annexin A7 mediated membrane fusion was separated from a second GTP-dependent mechanism [38].\nHaving an annexin A7 knockout mouse we tested the involvement of annexin A7 in budding of red blood cell vesicles. Our data suggest that the efficiency of micro- and nanovesicle formation is not significantly different in wild type and mutant red blood cells. Likewise, Dictyostelium discoideum cells, in which the single annexin gene was inactivated, were not impaired in processes requiring membrane fusion [[39]; and data unpublished]. It might well be that the observed fusion of phospholipid layers by annexin A7 in the presence of high Ca2+ concentrations may turn out to be an in vitro effect. Similarly, the high abundance of annexin A7 in micro- and nanovesicles might be fortuitous as a significant percentage of the red blood cell membrane, with which annexin A7 associates when the Ca2+ levels rise, appears to be involved in the formation of exovesicles. Furthermore, the distribution of both annexin A7 isoforms in gradients of red blood cells indicates a function which differs from organizing subcellular membranes or membrane pathways. Whereas annexin A2 is tightly associated with endosomes and may have functions in membrane fusion and the endosomal pathway, annexin A7 distributes with plasma membrane raft domains of different types and densities. Interestingly, in vesicles of red blood cells lacking annexin A7 the amount of sorcin is lowered, indicating that its localisation is affected by the loss of annexin A7 or its expression during red blood cell development was reduced.\nHaving excluded a direct role in vesicle formation and membrane fusion, annexin A7 might act by its property as Ca2+-binding protein [17]. Previous results in which annexin A7 was shown to play a role in membrane aggregation might be explained by a supportive function of annexin A7 in that it interferes with the local Ca2+ homeostasis thus influencing membrane organization. As the annexins belong to a wide spread and evolutionarily conserved protein family, redundant, but not identical functions are expected. However, so far no other members of the annexin family, which may substitute for annexin A7, have been described in red blood cells.\nThe structural basis for the elasticy of red blood cells in circulation are long range molecular functions of the plasma membrane and the membrane associated part of the cytoskeleton [40-43]. Major constituents of the membrane skeleton are spectrin tetramers linked together by short actin filaments and several other proteins covering the entire cytoplasmic surface of the red blood cell membrane [44]. Membrane cholesterol diminishes red blood cell haemolysis by the complement complex, whereas depletion of raft cholesterol abrogates association of all raft proteins with no significant effect on areas in the rest of the cell membrane and deformability [45,46].\nAnnexin A7 knock out mouse red blood cells show a more flat shape and have a higher osmotic resistance. The presence of annexin A7 may alter the membrane flexibility in that it supports the typical biconcave membrane shape and leads to a lower minimal osmotic resistance. Annexin A7 does not appear to have an influence on plasma membrane integrity itself as the maximal osmotic resistance value stays constant. Ca2+ and membrane skeletal proteins are known to play key roles on the red blood cell membrane shape and stability [47]. Annexins have been reported to bind directly to F-actin, we could however exclude such an activity for annexin A7. Nevertheless it might interact with other components and have a role in organizing the membrane cytoskeleton, controlling raft protein associations or influencing the ionic strength of red blood cells on its own or by interfering with other signaling pathways.\nAs discussed above annexin A7 could be involved in the cytoplasmic Ca2+ homeostasis. It has been demonstrated that micromolar changes of the intracellular Ca2+ concentration exert a profound effect on the membrane properties that regulate red blood cell deformability [48,49]. Furthermore, the intracellular Ca2+ was shown to regulate the membrane stability through modulation of cytoskeletal protein interactions [50]. Ca2+ also induces a transbilayer phospholipid redistribution inducing a shape change of red blood cells [51]. In addition, Ca2+ ions can drive spiculation of the membrane bilayer without involving the cytoskeleton [52].\nWe have also observed a defect in platelet function in the annexin A7 mutant. In the platelet aggregation experiments the initial aggregation velocity was slightly, but significantly lower in platelets lacking annexin A7. These data are not reflected by a change in the in vivo bleeding time. However the reaction speed of murine platelets is much higher than those of human and due to the technical setup we might have missed larger changes in the mouse samples. The immediate reaction of mouse platelets and the absence of a lag phase after triggering may be caused by an immediately initiated thrombin generation [22]. As known from the frequent human vWF-syndrome or other haemostatic diseases, small defects often are clinically silent and do not result in physiological changes under normal conditions. Only in situations with severe physical injury, distinct environmental influences or additional platelet attributes like the platelet antigen polymorphism [53] differences might become apparent."}