Amniotic fluid fibronectin: Characterization and synthesis by cells in culture

Ed Crouch, Gary Balian, Karen Holbrook, Dan Duksin, Paul Bornstein

Research output: Contribution to journalArticle

74 Scopus citations

Abstract

A glycoprotein immunologically related to plasma cold-insoluble globulin (CIG) and fetal skin fibroblast fibronectin has been purified from second-trimester human amniotic fluid. This protein (amniotic fluid fibronectin) migrated more slowly than CIG on sodium dodecyl sulfate gel electrophoresis and showed greater polydispersity which could result, at least in part, from heterogeneity in glycosylation. Cloned human amniotic fluid epithelioid and fibroblastic cells synthesized and secreted a protein with similar properties into the culture medium. Fibronectin was shown to be associated with the pericellular and extracellular matrix of cultured amniotic fluid cells by immunofluorescence, lactoperoxidase-catalyzed iodination, and labeling with ferritin-conjugated antibodies. The kinetics of secretion of the protein were consistent with its role as a matrix protein. We anticipate that amniotic fluid fibronectin will prove to be the same protein which elsewhere in the body is incorporated into connective tissues and basement membranes. Amniotic fluid could, therefore, serve as a convenient source of in vivo synthesized fibronectin for biological and structural studies.

Original languageEnglish
Pages (from-to)701-715
Number of pages15
JournalJournal of Cell Biology
Volume78
Issue number3
DOIs
StatePublished - Sep 1 1978
Externally publishedYes

Keywords

  • Amniotic fluid cells
  • Cold insoluble
  • Extracellular matrix
  • Fibronectin
  • Globulin
  • Glycoproteins
  • LETS protein
  • Secretion

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