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Plasminogen structural domains exhibit different functions when associated with cell surface GRP78 or the voltage-dependent anion channel.

Publication ,  Journal Article
Gonzalez-Gronow, M; Kaczowka, SJ; Payne, S; Wang, F; Gawdi, G; Pizzo, SV
Published in: J Biol Chem
November 9, 2007

Both the voltage-dependent anion channel and the glucose-regulated protein 78 have been identified as plasminogen kringle 5 receptors on endothelial cells. In this study, we demonstrate that kringle 5 binds to a region localized in the N-terminal domain of the glucose-regulated protein 78, whereas microplasminogen does so through the C-terminal domain of the glucose-regulated protein 78. Both plasminogen fragments induce Ca(2+) signaling cascades; however, kringle 5 acts through voltage-dependent anion channel and microplasminogen does so via the glucose-regulated protein 78. Because trafficking of voltage-dependent anion channel to the cell surface is associated with heat shock proteins, we investigated a possible association between voltage-dependent anion channel and glucose-regulated protein 78 on the surface of 1-LN human prostate tumor cells. We demonstrate that these proteins co-localize, and changes in the expression of the glucoseregulated protein 78 affect the expression of voltage-dependent anion channel. To differentiate the functions of these receptor proteins, either when acting singly or as a complex, we employed human hexokinase I as a specific ligand for voltage-dependent anion channel, in addition to kringle 5. We show that kringle 5 inhibits 1-LN cell proliferation and promotes caspase-7 activity by a mechanism that requires binding to cell surface voltage-dependent anion channel and is inhibited by human hexokinase I.

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Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

November 9, 2007

Volume

282

Issue

45

Start / End Page

32811 / 32820

Location

United States

Related Subject Headings

  • Voltage-Dependent Anion Channels
  • Voltage-Dependent Anion Channel 1
  • RNA, Small Interfering
  • Protein Precursors
  • Protein Binding
  • Prostatic Neoplasms
  • Plasminogen
  • Peptide Fragments
  • Oxygen
  • Molecular Chaperones
 

Citation

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ICMJE
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Gonzalez-Gronow, M., Kaczowka, S. J., Payne, S., Wang, F., Gawdi, G., & Pizzo, S. V. (2007). Plasminogen structural domains exhibit different functions when associated with cell surface GRP78 or the voltage-dependent anion channel. J Biol Chem, 282(45), 32811–32820. https://doi.org/10.1074/jbc.M703342200
Gonzalez-Gronow, Mario, Steven J. Kaczowka, Sturgis Payne, Fang Wang, Govind Gawdi, and Salvatore V. Pizzo. “Plasminogen structural domains exhibit different functions when associated with cell surface GRP78 or the voltage-dependent anion channel.J Biol Chem 282, no. 45 (November 9, 2007): 32811–20. https://doi.org/10.1074/jbc.M703342200.
Gonzalez-Gronow M, Kaczowka SJ, Payne S, Wang F, Gawdi G, Pizzo SV. Plasminogen structural domains exhibit different functions when associated with cell surface GRP78 or the voltage-dependent anion channel. J Biol Chem. 2007 Nov 9;282(45):32811–20.
Gonzalez-Gronow, Mario, et al. “Plasminogen structural domains exhibit different functions when associated with cell surface GRP78 or the voltage-dependent anion channel.J Biol Chem, vol. 282, no. 45, Nov. 2007, pp. 32811–20. Pubmed, doi:10.1074/jbc.M703342200.
Gonzalez-Gronow M, Kaczowka SJ, Payne S, Wang F, Gawdi G, Pizzo SV. Plasminogen structural domains exhibit different functions when associated with cell surface GRP78 or the voltage-dependent anion channel. J Biol Chem. 2007 Nov 9;282(45):32811–32820.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

November 9, 2007

Volume

282

Issue

45

Start / End Page

32811 / 32820

Location

United States

Related Subject Headings

  • Voltage-Dependent Anion Channels
  • Voltage-Dependent Anion Channel 1
  • RNA, Small Interfering
  • Protein Precursors
  • Protein Binding
  • Prostatic Neoplasms
  • Plasminogen
  • Peptide Fragments
  • Oxygen
  • Molecular Chaperones