Amniotic fluid fibronectin. Characterization and synthesis by cells in culture.
J Cell Biol
; 78(3): 701-15, 1978 Sep.
Article
en En
| MEDLINE
| ID: mdl-701356
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.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Glicoproteínas
/
Líquido Amniótico
/
Proteínas de la Membrana
Idioma:
En
Año:
1978
Tipo del documento:
Article