Annexin-chromaffin granule membrane interactions: a comparative study of synexin, p32 and p67

Zaks, William J.; Creutz, Carl E.

doi:10.1016/0005-2736(90)90448-w

Cited by 46 publications

(33 citation statements)

References 54 publications

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“…At high Ca 2+ -concentration ($2 mM), AnxA6 is able to bind two membranes simultaneously. These results are in agreement with the observation by Zaks and Creutz that Anx6 binds membranes at low levels of calcium and aggregates membranes at higher levels of calcium (Zaks and Creutz, 1990). The data presented here support the hypothesis that the two modes of membrane association of AnxA6 correspond to the structural models presented in Fig.…”

Section: Discussionsupporting

confidence: 93%

Annexin-A6 presents two modes of association with phospholipid membranes. A combined QCM-D, AFM and cryo-TEM study

Buzhynskyy

Golczak

Lai-Kee-Him

et al. 2009

Journal of Structural Biology

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Section: Discussionsupporting

confidence: 93%

Annexin-A6 presents two modes of association with phospholipid membranes. A combined QCM-D, AFM and cryo-TEM study

Buzhynskyy

Golczak

Lai-Kee-Him

et al. 2009

Journal of Structural Biology

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“…Its role in secretion has not been extensively investigated, but the available evidence suggests that annexin VI inhibits rather than potentiates the secretory process. While exploring the ability of purified annexins to fuse chromaffin vesicles, Zaks and Creutz showed that annexin VI inhibits vesicle aggregation and fusion mediated by annexins II and VII [28]. The exact mechanism of this inhibition is unclear.…”

Section: Annexin VImentioning

confidence: 99%

Annexins in the secretory pathway

Donnelly¹,

Moss²

1997

Cellular and Molecular Life Sciences (CMLS)

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Among the multiplicity of roles suggested for proteins of the annexin family, those implicating these proteins in regulated exocytosis remain among the most convincing. Studies in this area of annexin biology have focused on annexin II, which because of its unusually low Ca(2+)-requirement for phospholipid-binding has many of the requisite properties of a membrane fusogenic Ca2+ sensor. Other annexins are also good candidates for exocytotic mediators, especially annexins I and VII, which have strong vesicle-aggregating activities. In contrast, annexin VI appears to block vesicle aggregation, perhaps acting as a negative regulator of exocytosis. In this review, we consider the evidence for and against annexins having functions in the secretory pathway.

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“…These high calcium concentrations were included in this study due to the marked biphasic response reported in a study of the binding of annexins to chromaffin granules. 46 Using specific antisera, the identities of the two major proteins were determined. Both proteins displayed calcium-binding and calcium-dependent, lipid-binding properties (Figures 2 and 4) compatible with being annexins.…”

Section: 1-mentioning

confidence: 99%

Annexins V and VI: major calcium-dependent atrial secretory granule-binding proteins.

1991

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Atrial natriuretic peptide is stored by atrial myocytes in secretory granules, known as atrial specific granules, and is released from these granules by exocytosis. We have isolated a group of atrial proteins by affinity chromatography that bind to atrial specific granules in a calcium-dependent manner. The two major proteins isolated (32.5 kd and 67 kd) are calcium-binding proteins and have been identified as annexins V and VI by immunoblotting with specific antisera. The calcium dependence of their binding to atrial specific granules has been characterized in vitro and indicates that this interaction takes place at micromolar levels of calcium. In addition, the group of proteins isolated includes another calciumbinding protein of 20 kd, as well as GTP-binding proteins of 22 to 26 kd. Membrane interactions during exocytosis are presumably mediated by the interaction of specific proteins with the granule membrane. The properties of the proteins described here, and their ability to bind to atrial specific granules in a calcium-dependent manner, make them likely candidates in the search for regulatory proteins mediating atrial natriuretic peptide secretion. (Hypertension 1991;18:648-656) A trial natriuretic peptide (ANP), a potent natri-/ \ uretic, diuretic, and vasorelaxant factor, is A. A . secreted from the mammalian heart. 1 Electron-dense granules present in atrial myocytes, 2 known as atrial specific granules (ASG), are now recognized as the intracellular storage sites for ANP. 3 These secretory granules therefore form part of the regulated secretory pathway for ANP.In other endocrine organs, such as the adrenal medulla, calcium plays an important role in the control of the secretory pathway. 4 -5 Various studies have indicated that calcium is also involved in the regulation of ANP secretion from the heart. 6 -10 The regulatory role of calcium during hormone secretion in many noncardiac endocrine organs is mediated by calcium-binding proteins. 11 Calmodulin, the ubiquitous calcium-binding protein, has been extensively studied in this regard. 12 Although ANP is present in In this study, calcium-dependent affinity chromatography with immobilized ASG was used to isolate atrial cytosolic proteins that may interact with atrial secretory granules during the regulated secretion of ANP. Proteins isolated include annexins V and VI, and their calcium-dependent binding to ASG has been characterized. Methods Granule IsolationAtria were obtained from female Sprague-Dawley rats (weight 250-275 g) after decapitation. Granules were isolated essentially as reported earlier. 3 Batches of 30 atria (from 15 rats) were processed and pooled. They were rinsed, minced, and homogenized in 0.25 M sucrose, 10 mM tris (hydroxymethyl) aminomethane

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Annexin-chromaffin granule membrane interactions: a comparative study of synexin, p32 and p67

Cited by 46 publications

References 54 publications

Annexin-A6 presents two modes of association with phospholipid membranes. A combined QCM-D, AFM and cryo-TEM study

Annexin-A6 presents two modes of association with phospholipid membranes. A combined QCM-D, AFM and cryo-TEM study

Annexins in the secretory pathway

Annexins V and VI: major calcium-dependent atrial secretory granule-binding proteins.

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