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Related Experiment Videos

Biosynthesis of properdin.

T C Farries1, J P Atkinson

  • 1Howard Hughes Medical Institute Laboratories, St. Louis, MO 63110.

Journal of Immunology (Baltimore, Md. : 1950)
|February 1, 1989
PubMed
Summary
This summary is machine-generated.

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Properdin (P) is synthesized by HL-60 cells and undergoes intracellular polymerization before secretion. This process, involving N-linked carbohydrate modification, is crucial for P

Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Properdin (P) is a key complement system protein.
  • Its synthesis and post-translational modifications are not fully understood.

Purpose of the Study:

  • To investigate the intracellular synthesis, processing, and polymerization of Properdin (P).
  • To characterize the role of glycosylation in Properdin's functional activity and secretion.

Main Methods:

  • HL-60 cell line differentiation with DMSO.
  • Pulse-chase experiments and metabolic labeling.
  • Physicochemical characterization of secreted and intracellular Properdin.
  • Binding assays using C3iBb-Sepharose and C3i-Sepharose.
  • Enzymatic deglycosylation studies (Endoglycosidases F and H) and tunicamycin treatment.

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Main Results:

  • HL-60 cells synthesize and secrete Properdin (P) that is functionally similar to plasma-derived P.
  • Intracellular P shows a lower molecular weight and reversible binding to C3iBb-Sepharose, indicating early polymerization.
  • N-linked high-mannose carbohydrate is processed to a complex form before secretion.
  • Glycosylation is not essential for P polymerization, secretion, or function.

Conclusions:

  • Properdin polymerization is an early intracellular event, occurring before secretion.
  • The N-linked carbohydrate moiety is modified during intracellular transit but does not influence polymerization or function.
  • Controlled intracellular polymerization may prevent aberrant aggregation of Properdin.