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SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin.

Publication ,  Journal Article
Berwin, B; Delneste, Y; Lovingood, RV; Post, SR; Pizzo, SV
Published in: J Biol Chem
December 3, 2004

Calreticulin and gp96 (GRP94) traffic associated peptides into the major histocompatibility complex class-I cross-presentation pathway of antigen-presenting cells (APCs). Efficient accession of the cross-presentation pathway requires APC receptor-mediated endocytosis of the chaperone/peptide complexes. Previously, scavenger receptor class-A (SRA) was shown to play a substantial role in trafficking gp96 and calreticulin into macrophages, accounting for half of total receptor-mediated uptake. However, the scavenger receptor ligand fucoidin competed the chaperone uptake beyond that accounted for by SRA, indicating that another scavenger receptor(s) may also contribute. Consistent with this hypothesis, we showed that the residual calreticulin uptake into SRA(-/-) macrophages is competed by the scavenger receptor ligand acetylated low density lipoprotein (LDL). We now report that an additional scavenger receptor, SREC-I (scavenger receptor expressed by endothelial cell-I), mediates the endocytosis of calreticulin and gp96. Ectopic expression of SREC-I in Chinese hamster ovary cells yielded chaperone recognition and uptake, and these processes were competed by the inhibitory ligands fucoidin and acetylated (Ac)LDL. Although AcLDL competes for the chaperone interactions with SRA and SREC, we showed that not all of the scavenger receptors, which bind AcLDL, bind calreticulin or gp96. The overexpression of SREC-I in macrophages increased chaperone endocytosis, indicating that SREC-I functions in APCs and that the cytosolic components necessary for the endocytosis of SREC-I and its cargo are present and not limiting in APCs. These data identify a novel class of ligands for SREC-I and provide insight into the mechanisms by which APCs and potentially endothelial cells traffic chaperone/antigen complexes.

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Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

December 3, 2004

Volume

279

Issue

49

Start / End Page

51250 / 51257

Location

United States

Related Subject Headings

  • Transfection
  • Scavenger Receptors, Class F
  • Scavenger Receptors, Class A
  • Receptors, Scavenger
  • Receptors, LDL
  • Protein Structure, Tertiary
  • Protein Isoforms
  • Protein Binding
  • Polysaccharides
  • Peptides
 

Citation

APA
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ICMJE
MLA
NLM
Berwin, B., Delneste, Y., Lovingood, R. V., Post, S. R., & Pizzo, S. V. (2004). SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin. J Biol Chem, 279(49), 51250–51257. https://doi.org/10.1074/jbc.M406202200
Berwin, Brent, Yves Delneste, Rachel V. Lovingood, Steven R. Post, and Salvatore V. Pizzo. “SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin.J Biol Chem 279, no. 49 (December 3, 2004): 51250–57. https://doi.org/10.1074/jbc.M406202200.
Berwin B, Delneste Y, Lovingood RV, Post SR, Pizzo SV. SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin. J Biol Chem. 2004 Dec 3;279(49):51250–7.
Berwin, Brent, et al. “SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin.J Biol Chem, vol. 279, no. 49, Dec. 2004, pp. 51250–57. Pubmed, doi:10.1074/jbc.M406202200.
Berwin B, Delneste Y, Lovingood RV, Post SR, Pizzo SV. SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin. J Biol Chem. 2004 Dec 3;279(49):51250–51257.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

December 3, 2004

Volume

279

Issue

49

Start / End Page

51250 / 51257

Location

United States

Related Subject Headings

  • Transfection
  • Scavenger Receptors, Class F
  • Scavenger Receptors, Class A
  • Receptors, Scavenger
  • Receptors, LDL
  • Protein Structure, Tertiary
  • Protein Isoforms
  • Protein Binding
  • Polysaccharides
  • Peptides