The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Peter James

Peter James

Professor

Peter James

Binding of calcium ions and SNAP-25 to the hexa EF-hand protein secretagogin

Author

  • Annika Rogstam
  • Sara Linse
  • Anders Lindqvist
  • Peter James
  • Ludwig Wagner
  • Tord Berggård

Summary, in English

Secretagogin is a hexa EF-hand protein, which has been identified as a novel potential tumour marker. In the present study, we show that secretagogin binds four Ca2+ ions (log K-1 = 7.1 +/- 0.4, log K-2 = 4.7 +/- 0.6, log K-3 = 3.6 +/- 0.7 and log K-4 = 4.6 +/- 0.6 in physiological salt buffers) with a [Ca2+](0.5) of approx. 25 mu M. The tertiary structure of secretagogin changes significantly upon Ca2+ binding, but not upon Mg2+ binding, and the amount of exposed hydrophobic surface in secretagogin increases upon Ca2+ binding, but not upon Mg2+ binding. These properties suggest that secretagogin belongs to the 'sensor' family of Ca2+-binding proteins. However, in contrast with the prototypical Ca2+ sensor calmodulin, which interacts with a very large number of proteins, secretagogin is significantly less promiscuous. Only one secretagogin-interacting protein was reproducibly identified from insulinoma cell lysates and from bovine and mouse brain homogenates. This protein was identified as SNAP-25 (25 kDa synaptosome-associated protein), a protein involved in Ca2+-induced exocytosis in neurons and in neuroendocrine cells. K-d was determined to be 1.2 x 10(-7) M in the presence of Ca2+ and 1.5 x 10(-6) M in the absence of Ca2+. The comparatively low Ca2+ affinity for secretagogin and the fact that it undergoes Ca2+-induced conformational changes and interacts with SNAP-25 raise the possibility that secretagogin may link Ca2+ signalling to exocytotic processes.

Department/s

  • Department of Biology
  • Biophysical Chemistry
  • Islet cell physiology
  • Department of Immunotechnology

Publishing year

2007

Language

English

Pages

353-363

Publication/Series

Biochemical Journal

Volume

401

Issue

Pt 1

Document type

Journal article

Publisher

Portland Press

Topic

  • Biochemistry and Molecular Biology

Keywords

  • secretagogin
  • conformational change
  • 25 kDa
  • sensor
  • calcium binding
  • synaptosome-associated protein (SNAP-25)
  • EF-hand

Status

Published

Research group

  • Islet cell physiology

ISBN/ISSN/Other

  • ISSN: 0264-6021