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Related Experiment Videos

Multimerin processing by cells with and without pathways for regulated protein secretion.

C P Hayward1, Z Song, S Zheng

  • 1Departments of Pathology and Molecular Medicine, Laboratory Medicine, and Medicine, McMaster University, Hamilton, Ontario, Canada.

Blood
|August 10, 1999
PubMed
Summary
This summary is machine-generated.

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Multimerin, a factor V-binding protein, is processed differently in various cells. Endothelial cells constitutively secrete multimerin, while regulated secretion cells show altered processing, impacting its function.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Protein Science

Background:

  • Multimerin is a large, soluble protein found in platelet alpha-granules and vascular endothelium.
  • Endothelial cells store multimerin in granules lacking P-selectin and constitutively secrete it.
  • The posttranslational processing and storage of multimerin are not fully understood.

Purpose of the Study:

  • To investigate the posttranslational processing and storage of multimerin in different cellular contexts.
  • To compare multimerin processing in cells with constitutive versus regulated secretion pathways.
  • To identify factors influencing multimerin's final form and secretion.

Main Methods:

  • Expression of human endothelial cell prepromultimerin in various cell lines (e.g., HEK 293, neuroendocrine cells).

Related Experiment Videos

  • Analysis of recombinant multimerin for variations in glycosylation, proteolytic processing, and multimer profile.
  • Comparison of multimerin processing in cells with constitutive and regulated secretion pathways.
  • Main Results:

    • Recombinant multimerin exhibited diverse glycosylation, proteolytic processing, and multimer profiles across different cell lines.
    • Human embryonic kidney 293 cells replicated the constitutive secretion processing seen in endothelial cells.
    • Multimerin targeted for regulated secretion underwent more extensive proteolysis than in platelets.
    • Specific endoproteases, potentially from megakaryocytes, may be necessary for platelet-type multimerin production.

    Conclusions:

    • Cell type and secretion pathway significantly influence multimerin's posttranslational processing and storage.
    • Constitutive secretion in endothelial cells involves specific processing pathways.
    • Regulated secretion pathways lead to altered, more extensive proteolysis of multimerin.
    • Tissue-specific processing differences may impact multimerin's functions and its interaction with factor V.