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Soluble complement receptor type 1 (CD35) is released from leukocytes by surface cleavage

C Danielsson1, M Pascual, L French

  • 1Laboratory of Immunonephrology, Medizinische Klinik B, Department Innere Medizin, Kantonsspital Basel, Switzerland.

European Journal of Immunology
|November 1, 1994
PubMed
Summary
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Soluble complement receptor type 1 (sCR1) in plasma is shed from cell surfaces, primarily polymorphonuclear leukocytes (PMN). This study developed an assay to show sCR1 is an extracellular fragment, not recognized by membrane-bound CR1 assays.

Area of Science:

  • Immunology
  • Complement System Biology

Background:

  • Soluble complement receptor type 1 (sCR1) in human plasma is thought to originate from cell surface receptor shedding.
  • Understanding the source and nature of sCR1 is crucial for its role in complement regulation.

Purpose of the Study:

  • To develop a specific assay for membrane-bound CR1 (mCR1) to differentiate it from soluble CR1 (sCR1).
  • To investigate the cellular origin and release mechanism of sCR1 in human plasma.

Main Methods:

  • Developed a novel enzyme-linked immunosorbent assay (ELISA) targeting the intracellular domain of CR1 (mCR1-ELISA).
  • Tested mCR1-ELISA's specificity using various cell types (erythrocytes, PMN, lymphocytes) and recombinant proteins.
  • Induced sCR1 release from PMN in vitro using inflammatory stimuli.

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Main Results:

  • The mCR1-ELISA specifically detected membrane-bound CR1 but not plasma sCR1 or recombinant soluble CR1, confirming sCR1 is an extracellular fragment.
  • Polymorphonuclear leukocytes (PMN) and HL60 cells released a soluble CR1 fragment not detected by mCR1-ELISA.
  • Inflammatory stimuli (FMLP, TNF-α, LPS) accelerated sCR1 release from PMN, while GM-CSF sustained CR1 expression and release.

Conclusions:

  • Soluble CR1 is produced by proteolytic cleavage of cell surface CR1.
  • A significant portion of human plasma sCR1 is released from PMN.
  • Leukocyte-derived sCR1 may regulate complement activation at inflammatory sites.