Subcellular targeting of multiligand-binding protein gC1qR
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Subcellular targeting of multiligand-binding protein gC1qR. / Dedio, J; Renné, T; Weisser, M; Müller-Esterl, W.
In: IMMUNOPHARMACOLOGY, Vol. 45, No. 1-3, 01.12.1999, p. 1-5.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Subcellular targeting of multiligand-binding protein gC1qR
AU - Dedio, J
AU - Renné, T
AU - Weisser, M
AU - Müller-Esterl, W
PY - 1999/12/1
Y1 - 1999/12/1
N2 - gC1q receptor, a protein originally described as the cell surface receptor for the globular heads of complement factor C1q, has been found to bind human H-kininogen with high affinity and specificity. Therefore, gC1qR has been considered candidate kininogen docking site on the surfaces of platelets, neutrophils and endothelial cells. Recent work demonstrating that gC1qR is an intracellular protein that is tightly associated with mitochondria rather than targeted to the cell surface has challenged this view. To further probe cellular trafficking routes of gC1qR, we overexpressed human gC1qR in a mammalian cell and monitored cell surface exposure of recombinant gC1qR by virtue of its capacity to bind labeled H-kininogen. Transient transfection of COS1 cells with the full-length cDNA of human gC1qR resulted in a high level of recombinant protein that matched the pool of endogenous gC1qR present in these tells. Overexpression of gC1qR did not significantly increase the number of H-kininogen binding sites exposed by the transfected cells thus denying the possibility that alternative routing of gC1qR to the surface of COS1 cells occurs at significant levels. Hence gC1qR has the capacity to tightly bind H-kininogen, but because gC1qR is routed to mitochondria it cannot fulfill the postulated functions as a cell docking site for kininogens and complement factors.
AB - gC1q receptor, a protein originally described as the cell surface receptor for the globular heads of complement factor C1q, has been found to bind human H-kininogen with high affinity and specificity. Therefore, gC1qR has been considered candidate kininogen docking site on the surfaces of platelets, neutrophils and endothelial cells. Recent work demonstrating that gC1qR is an intracellular protein that is tightly associated with mitochondria rather than targeted to the cell surface has challenged this view. To further probe cellular trafficking routes of gC1qR, we overexpressed human gC1qR in a mammalian cell and monitored cell surface exposure of recombinant gC1qR by virtue of its capacity to bind labeled H-kininogen. Transient transfection of COS1 cells with the full-length cDNA of human gC1qR resulted in a high level of recombinant protein that matched the pool of endogenous gC1qR present in these tells. Overexpression of gC1qR did not significantly increase the number of H-kininogen binding sites exposed by the transfected cells thus denying the possibility that alternative routing of gC1qR to the surface of COS1 cells occurs at significant levels. Hence gC1qR has the capacity to tightly bind H-kininogen, but because gC1qR is routed to mitochondria it cannot fulfill the postulated functions as a cell docking site for kininogens and complement factors.
KW - Animals
KW - Antigens, CD44
KW - Binding Sites
KW - Biological Transport
KW - COS Cells
KW - Carrier Proteins
KW - Complement C1q
KW - Humans
KW - Ligands
KW - Membrane Glycoproteins
KW - Mitochondrial Proteins
KW - Protein Processing, Post-Translational
KW - Receptors, Complement
KW - Subcellular Fractions
M3 - SCORING: Journal article
C2 - 10614982
VL - 45
SP - 1
EP - 5
JO - IMMUNOPHARMACOLOGY
JF - IMMUNOPHARMACOLOGY
SN - 0162-3109
IS - 1-3
ER -