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Soluble form of complement C3b/C4b receptor (CR1) results from a proteolytic cleavage in the C-terminal region of CR1 transmembrane domain

Hamer, I.
Maeder, C.
Carpentier, J. L.
Published in Biochemical Journal. 1998, vol. 329 ( Pt 1), p. 183-190
Abstract The complement C3b/C4b receptor (CR1) is an integral protein, anchored in the plasma membrane through a hydrophobic domain of 25 amino acids, but is also found in the plasma in soluble form (sCR1). A recombinant, soluble form of CR1 has been demonstrated to reduce complement-dependent tissue injury in animal models of ischaemia/reperfusion. In view of the important pathophysiological relevance of sCR1, we have investigated the mechanisms governing CR1 release by using various mutated and chimaeric receptors transiently expressed in COS cells. Pulse-chase experiments revealed that (1) sCR1 is produced by a proteolytic process, (2) the cleavage site lies within the C-terminus of CR1 transmembrane domain, (3) the proteolytic process involves a fully glycosylated CR1 form and (4) this process takes place in late secretory vesicles or at the plasma membrane.
Keywords Amino Acid SequenceAnimalsBrefeldin ACOS CellsCell Membrane/metabolismCyclopentanes/pharmacologyElectrophoresis, Polyacrylamide GelEndopeptidases/ metabolismEndoplasmic Reticulum/metabolismGlycosylationHumansLysosomes/metabolismMolecular Sequence DataMutagenesisPrecipitin TestsProtein Processing, Post-TranslationalReceptors, Complement 3b/blood/ chemistry/genetics/ metabolismRecombinant Fusion Proteins/chemistry/metabolismSolubilityUrokinase-Type Plasminogen Activator/genetics
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PMID: 9405292
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