Adsorption of fetal surfactant protein SP-B on the human amnion at term and on amniocytes incubated with fetal surfactant in vitro

• Published in: Reproduction fertility and development Vol. 3; no. 4; p. 421
• Main Authors: Newman, G E, Phizackerley, P J, Lopez Bernal, A, Noble, G R, Willis, A C
• Format: Journal Article
• Language: English
• Published: Australia 1991
• Subjects: Adsorption; Amino Acid Sequence; Amnion - metabolism; Amnion - physiology; Cells, Cultured; Female; Fetus - metabolism; Humans; Immunohistochemistry; Molecular Sequence Data; Pregnancy; Prostaglandins - biosynthesis; Proteolipids - metabolism; Proteolipids - pharmacology; Pulmonary Surfactants - metabolism; Pulmonary Surfactants - pharmacology
• ISSN: 1031-3613; 1448-5990
• DOI: 10.1071/RD9910421

Fetal surfactant stimulates the synthesis of prostaglandins by slices of human amnion at term and by a human amnion cell line, and these effects are partly dependent upon surfactant apoproteins. In this paper, methods are described for the purification of surfactant from human amniotic fluid and from post-mortem human lung. A procedure is described for the purification of surfactant protein SP-B from human amniotic fluid, and the sequence of 20 amino acids at the N-terminal has been determined. A monoclonal antibody generated against human lung surfactant has been shown to react with SP-B from amniotic-fluid surfactant, and the presence of SP-B on the surface of the amnion at term has been demonstrated by immunohistochemical methods. It has also been shown that SP-B from surfactant is present on the surface of amniocytes incubated with surfactant in vitro.