Annexin VI Participates in the Formation of a Reversible, Membrane-Cytoskeleton Complex in Smooth Muscle Cells

Babiychuk, Eduard B.; Palstra, Robert-Jan; Schaller, Johann; Kämpfer, Urs; Draeger, Annette

doi:10.1074/jbc.274.49.35191

Cited by 92 publications

(102 citation statements)

References 45 publications

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“…In addition to modulating endocytosis at the plasma membrane, annexin VI was shown to be present in a late endocytic compartment of epithelial cells (30 -34), where it is thought to direct the delivery of endosomal vesicles to lysosomes (16,17). Interestingly, in smooth muscle, annexin VI plays a dynamic role in regulating reversible interactions between actin-cytoskeletal components and the caveolar fraction of the sarcolemma during muscle contraction (35,36). Collectively, these studies suggest that annexin VI plays a generalized role in Ca 2ϩ -dependent cellular processes involving transient interactions between membrane and cytoskeletal proteins.…”

Section: Discussionmentioning

confidence: 99%

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Identification of Annexin VI as a Ca2+-sensitive CRHSP-28-binding Protein in Pancreatic Acinar Cells

Thomas

Kaspar

Taft

et al. 2002

Journal of Biological Chemistry

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, indicating these molecules likely interact under physiological conditions. Immunofluorescence microscopy confirmed a dual localization of CRHSP-28 and annexin VI, which appeared in a punctate pattern in the supranuclear and apical cytoplasm of acini. Stimulation of cells for 5 min with the secretagogue cholecystokinin enhanced the colocalization of CRHSP-28 and annexin VI within regions of acini immediately below the apical plasma membrane. Tissue fractionation revealed that CRHSP-28 is a peripheral membrane protein that is highly enriched in smooth microsomal fractions of pancreas. Further, the content of CRHSP-28 in microsomes was significantly reduced in pancreatic tissue obtained from rats that had been infused with a secretory dose of cholecystokinin for 40 min, demonstrating that secretagogue stimulation transiently alters the association of CRHSP-28 with membranes in cells. Collectively, the Ca 2؉ -dependent binding of CRHSP-28 and annexin VI, together with their colocalization in the apical cytoplasm, is consistent with a role for these molecules in acinar cell membrane trafficking events that are essential for digestive enzyme secretion.

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Section: Discussionmentioning

confidence: 99%

“…microdomains (35,36). Thus, similar to its role in smooth muscle contraction, annexin VI may regulate interactions between zymogen granules and actin-cytoskeletal components of the subapical web in acini.…”

Section: Figmentioning

confidence: 99%

Identification of Annexin VI as a Ca2+-sensitive CRHSP-28-binding Protein in Pancreatic Acinar Cells

Thomas

Kaspar

Taft

et al. 2002

Journal of Biological Chemistry

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“…Annexin family proteins have been studied in different cell types, such as epithelial (Yao et al 1999, Akiba et al 2000, endothelial (Hajjar & Acharya 2000, Deora et al 2004, and skeletal and smooth muscle cells (Babiychuk et al 1999, Draeger et al 2005. Even though the cell biology of annexin 2 and p11 has been extensively studied at the molecular and cellular levels in various Figure 4 Western blot analysis of cytosolic annexin 2 (A2) protein (A) in pregnant sheep myometrium collected from controls treated with vehicle (Cont, lanes 1-6), progesterone (P, lanes 7-11), estradiol and progesterone (EP, lanes 12-16), and estradiol (E, lanes 17-22) at 121 dGA.…”

Section: Discussionmentioning

confidence: 99%

Separate and synergistic effect of progesterone and estradiol on induction of annexin 2 and its interaction protein p11 in pregnant sheep myometrium

Zhang

Wen

2007

Journal of Molecular Endocrinology

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To search for myometrial candidate genes regulated by progesterone, we isolated annexin 2 cDNA by subtractive hybridization and cloning. We also examined the effect of estradiol and/or progesterone, individually or combined, on expressions of annexin 2 and its ligand protein, p11 in pregnant sheep intrauterine tissues. Annexin 2 is a Ca 2C -dependent phospholipid-binding protein which interacts with p11 to form a bivalent heterotetramer. The heterotetramer was indicated in the production of prostaglandins through the regulation of cytosolic phospholipase A2 (cPLA2) and arachidonic acid release. Thus, annexin 2 and p11 could be the important players in Ca 2C signaling and prostaglandin production in uterine smooth muscles. Twenty-two ewes were treated with vehicle (nZ6), or 5 mg estradiol administered intramuscularly twice a day for 2 days (nZ6), or 100 mg progesterone administered intramuscularly twice a day for 14 days (nZ5), or estradiol plus progesterone with 100 mg progesterone administered intramuscularly twice a day for 10 days (nZ5) and then with vehicle for 2 days followed by estradiol for 2 days (5 mg administered intramuscularly twice a day). At 121 days of gestation age (dGA), endometrium, myometrium, placenta, and cervix were obtained under halothane anesthesia. Subtractive hybridization was used to isolate differentially expressed mRNAs from myometrial tissues treated with progesterone, which was confirmed by western blot at protein level. Annexin 2 and p11 interaction was validated by immunoprecipitation and their expressions in intrauterine tissues were determined by western blot analysis. Data were analyzed by ANOVA. A cDNA clone from myometrial-subtracted library representing differentially expressed mRNA in the pregnant sheep myometrium with progesterone treatment was identified as annexin 2 by sequence analysis and BLASTN search. Annexin 2 was present in both cytosolic and membrane-associated fractions of intrauterine tissues. In contrast, p11 was detectable only in myometrial cytosolic fraction. Both annexin 2 and p11 significantly increased in myometrial cytosolic fraction after progesterone or progesterone plus estradiol treatment. Furthermore, estradiol and progesterone combined had a more profound effect on induction of annexin 2 than progesterone alone. Annexin 2 was immunoprecipitated specifically by p11 antibody from the myometrium. This study indicates that progesterone may play an important role in the control of myometrial contractility by modifying protein expression associated with Ca 2C and prostaglandin signaling systems during pregnancy. Enhanced expression of myometrial annexin 2 in progesterone plus estradiol group supports our hypothesis that estrogen's stimulation is optimized by progesterone's priming in the pregnant sheep uterus.

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“…Decreased Fluid-phase Uptake Is Reversed by the Inhibition of GSL Synthesis in NPC Cell Culture Models-Annexins are of particular interest because they are thought to be important in endocytic trafficking and are associated with membrane microdomains (16,21,55,56). NPC cell culture models show altered annexin 2 localization and a decrease in the intracellular accumulation of the fluid phase marker HRP (15).…”

Section: Altered Endocytic Trafficking In An Npc Cell Culture Model Imentioning

confidence: 99%

Accumulation of Glycosphingolipids in Niemann-Pick C Disease Disrupts Endosomal Transport

Vruchte

Lloyd-Evans

Veldman

et al. 2004

Journal of Biological Chemistry

172

138

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Glycosphingolipids are endocytosed and targeted to the Golgi apparatus but are mistargeted to lysosomes in sphingolipid storage disorders. Substrate reduction therapy utilizes imino sugars to inhibit glucosylceramide synthase and potentially abrogate the effects of storage. Niemann-Pick type C (NPC) disease is a disorder of intracellular transport where glycosphingolipids (GSLs) and cholesterol accumulate in endosomal compartments. The mechanisms of altered intracellular trafficking are not known but may involve the mistargeting and disrupted function of proteins associated with GSL membrane microdomains. Membrane microdomains were isolated by Triton X-100 and sucrose density gradient ultracentrifugation. High pressure liquid chromatography and mass spectrometric analysis of NPC1 ؊/؊ mouse brain revealed large increases in GSL. Sphingosine was also found to be a component of membrane microdomains, and in NPC liver and spleen, large increases in cholesterol and sphingosine were found. GSL and cholesterol levels were increased in mutant NPC1-null Chinese hamster ovary cells as well as U18666A and progesterone induced NPC cell culture models. However, inhibition of GSL synthesis in NPC cells with N-butyldeoxygalactonojirimycin led to marked decreases in GSL but only small decreases in cholesterol levels. Both annexin 2 and 6, membrane-associated proteins that are important in endocytic trafficking, show distorted distributions in NPC cells. Altered BODIPY lactosylceramide targeting, decreased endocytic uptake of a fluid phase marker, and mistargeting of annexin 2 (phenotypes associated with NPC) are reversed by inhibition of GSL synthesis. It is suggested that accumulating GSL is part of a mislocalized membrane microdomain and is responsible for the deficit in endocytic trafficking found in NPC disease.Increasing evidence suggests that the membranes of eukaryotic cells are not homogeneously fluid. They contain membrane microdomains, often referred to as lipid rafts and/or caveolae, enriched in glycosphingolipids (GSLs), 1 specific proteins, and cholesterol (1-3). Being operationally defined, i.e. by detergent insolubility and low buoyant density, the natural (in situ) existence of such membrane microdomains has been and continues to be controversial (4). However, they have recently been visualized by using electron microscopy as small structures covering as much as 35% of the cell surface (5). Although membrane microdomains on the cell surface tend to be transient (6), relatively stable microdomains have been visualized in the endocytic pathway (7) where they are proposed to play a role in protein and lipid sorting (8). Many GSL storage diseases, including Niemann-Pick type C (NPC), are often characterized by enlarged liver and spleen as well as severe neurodegeneration. In these diseases, cholesterol and GSLs accumulate in the endocytic pathway because of reduced breakdown. Hence, they may be a useful tool for determining the relative importance of GSLs in endocytic transport. Fibroblasts from patients suffering f...

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Annexin VI Participates in the Formation of a Reversible, Membrane-Cytoskeleton Complex in Smooth Muscle Cells

Cited by 92 publications

References 45 publications

Identification of Annexin VI as a Ca2+-sensitive CRHSP-28-binding Protein in Pancreatic Acinar Cells

Identification of Annexin VI as a Ca2+-sensitive CRHSP-28-binding Protein in Pancreatic Acinar Cells

Separate and synergistic effect of progesterone and estradiol on induction of annexin 2 and its interaction protein p11 in pregnant sheep myometrium

Accumulation of Glycosphingolipids in Niemann-Pick C Disease Disrupts Endosomal Transport

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