Fibulin-1C, C1 Esterase Inhibitor and Glucose Regulated Protein 75 Interact with the CREC Proteins, Calumenin and Reticulocalbin

G. A. W. Hansen, M. Ludvigsen, C. Jacobsen, C. Cangemi, L. M. Rasmussen, H. Vorum, B. Honore

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Affinity purification, immunoprecipitation, gel electrophoresis and mass spectrometry were used to identify fibulin-1C, C1 esterase inhibitor and glucose regulated protein 75, grp75, as binding partners of the CREC proteins, calumenin and reticulocalbin. Surface plasmon resonance was used to verify the interaction of all three proteins with each of the CREC proteins. Fibulin-1C interacts with calumenin and reticulocalbin with an estimated dissociation constant around 50-60 nM. The interaction, at least for reticulocalbin, was not dependent upon the presence of Ca 2+. C1 esterase inhibitor interacted with both proteins with an estimated dissociation constant at 1 μM for reticulocalbin and 150 nM for calumenin. The interaction, at least for calumenin, was dependent upon the presence of Ca 2+ with strong interaction at 3.5 mM while no detectable interaction could be found at 0.1 mM. Grp75 binds with an affinity of approximately 3-7 nM with reticulocalbin as well as with calumenin. These interactions suggest functional participation of the CREC proteins in chaperone activity, cell proliferation and transformation, cellular aging, haemostasis and thrombosis as well as modulation of the complement system in fighting bacterial infection.

Original languageEnglish
Article number e0132283
JournalP L o S One
Volume10
Issue number7
ISSN1932-6203
DOIs
Publication statusPublished - 10. Jul 2015

Keywords

  • Amino Acid Sequence
  • Arteries/metabolism
  • Calcium-Binding Proteins/metabolism
  • Cell Line
  • Chromatography, Affinity
  • Complement C1 Inhibitor Protein/metabolism
  • Female
  • HSP70 Heat-Shock Proteins/metabolism
  • Humans
  • Immune Sera/metabolism
  • Immunohistochemistry
  • Immunoprecipitation
  • Mass Spectrometry
  • Membrane Proteins/metabolism
  • Microscopy, Confocal
  • Molecular Sequence Data
  • Peptides/chemistry
  • Placenta/metabolism
  • Pregnancy
  • Protein Binding
  • Reproducibility of Results
  • Surface Plasmon Resonance

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