Differential recognition of secretory vesicles by annexins

https://doi.org/10.1016/0006-291X(92)91199-ZGet rights and content

Abstract

The interactions of synexin, calpactin, and p68 (annexins VII, II, and VI) with zymogen granules and adrenal medullary chromaffin granules were compared. Synexin promoted the aggregation and fusion of both types of organelles. Calpactin inhibited the action of synexin on zymogen granules but would aggregate only chromaffin granules. p68 inhibited aggregation of chromaffin granules by calpactin and fusion of zymogen granules by synexin. The results demonstrate that these annexins, all of which bind acidic phospholipids, interact differently with different biological membranes and therefore may play specific and non-overlapping roles in cells where they are coexpressed.

References (9)

  • CreutzC.E. et al.

    J. Biol. Chem.

    (1978)
  • ZaksW.J. et al.

    Biochim. Biophys. Act.

    (1990)
  • GeisowM.J. et al.

    Trends Biochem. Sci.

    (1986)
  • DrustD.S. et al.

    Nature

    (1988)
There are more references available in the full text version of this article.

Cited by (16)

  • Cytosolic dynamics of annexin a6 trigger feedback regulation of hypertrophy via atrial natriuretic peptide in cardiomyocytes

    2014, Journal of Biological Chemistry
    Citation Excerpt :

    Because basal pro-ANP levels were unaltered in H9c2Anxa6shR cells, it is possible that Anxa6 participates in the regulated rather than constitutive exocytosis of pro-ANP and participates in the formation of an ANP secretagogue under hypertrophic challenge. In this regard, earlier studies that described Anxa6 to be an inhibitor of secretion rather than a modulator, as described herein, relied on characterization of purified proteins and vesicles in competitive binding or analyzed tissue-specific distribution of the protein (9, 59). Such studies did not take into account the dynamic changes that may occur in protein function under stress at the cellular level (60).

  • Annexins and membrane dynamics

    1997, Biochimica et Biophysica Acta - Molecular Cell Research
  • Modulation of Protein Function by Lipids

    1994, Current Topics in Membranes
View all citing articles on Scopus
2

Permanent address: University of Cambridge, Department of Pharmacology, Tennis Court Road, Cambridge CB21QJ, U.K.

3

Students participating in these experiments were: Giampietro Schiavo, Istituto di Patologia Generale, Padova, Italy; Leena Nevalainen, Institute of Biotechnology, Helsinki, Finland, Ludolf von Ruden, Max Planck Institut fur biophysikalische Chemie, Gottingen, Germany; Lynda Fletcher, Department of Physiological Sciences, Manchester University, U.K.; Frank Bartels, Medizinische Hochschule Hannover, Germany; Ingo Waschulewski, Department of Anatomy and Cell Biology, University of Marburg, Germany; Roberto Buccione, Consorzio Mario Negri Sud, Centro di Ricerche Farmacologiche e Biomediche, Italy; Jef Pinxteren, Department Neurofarmacologie, UIA, Belgium; Christopher Magnus, Department of Pharmacology, School of Pharmacy, London, U.K.2222.

View full text