Interaction of C1q and the collectins with the potential receptors calreticulin (cC1qR/collectin receptor) and megalin

Immunobiology. 1998 Aug;199(2):208-24. doi: 10.1016/s0171-2985(98)80028-4.

Abstract

Several proteins have been identified as candidate cell-surface receptors for the complement protein C1q. Some of these also interact with the structurally-related collectin proteins. Previous descriptions of C1q-binding properties of cells, and information on the cellular distribution of candidate receptors suggest that there is more than one physiologically relevant receptor for C1q. Two such candidate receptors, cell-surface calreticulin (also referred to as cC1qR or collectin receptor) and megalin are discussed in this review.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcium-Binding Proteins / isolation & purification
  • Calcium-Binding Proteins / metabolism*
  • Calreticulin
  • Carrier Proteins / isolation & purification
  • Carrier Proteins / metabolism*
  • Cattle
  • Collectins
  • Complement C1q / metabolism*
  • Dimerization
  • Endocytosis
  • Heymann Nephritis Antigenic Complex
  • Humans
  • Hyaluronan Receptors*
  • Membrane Glycoproteins / metabolism*
  • Mitochondrial Proteins
  • Molecular Sequence Data
  • Receptors, Complement / isolation & purification
  • Receptors, Complement / metabolism*
  • Ribonucleoproteins / isolation & purification
  • Ribonucleoproteins / metabolism*

Substances

  • C1QBP protein, human
  • Calcium-Binding Proteins
  • Calreticulin
  • Carrier Proteins
  • Collectins
  • Heymann Nephritis Antigenic Complex
  • Hyaluronan Receptors
  • Membrane Glycoproteins
  • Mitochondrial Proteins
  • Receptors, Complement
  • Ribonucleoproteins
  • complement 1q receptor
  • Complement C1q