Human Surfactant Protein B: Structure, Function, Regulation, and Genetic
Disease.
Whitsett, Jeffrey A., Lawrence M. Nogee, Timothy E. Weaver, and Ann D.
Horowitz.
Division of Pulmonary Biology, Children's Hospital Medical Center,
Cincinatti, Ohio, and Dept. of Pediatrics, John's Hopkins School of Medicine,
Baltimore, MD.
APStracts 2:0014P, 1995.
ABSTRACT
Elucidation of the structure and function of the hydrophobic surfactant
protein (SP-B) and the SP-B gene has provided critical insight into surfactant
homeostasis and control of respiratory epithelial cell gene expression.
Surfactant protein B, in concert with surfactant protein A (SP-A), surfactant
protein C (SP-C), and surfactant phospholipids, contributes to the structure
and function of surfactant particles, determining surface activities and
pathways by which surfactant phospholipids and proteins are processed, routed,
packaged, and secreted from lamellar bodies by type II epithelial cells. After
secretion, SP-B plays an essential role in determining the structure of
tubular myelin, the stability and rapidity of spreading, and the recycling of
surfactant phospholipids. The biochemical and structural signals underlying
the homeostasis of alveolar surfactant are likely mediated by interactions
between the surfactant proteins and phospholipids producing discrete
structural forms that vary in size, aproprotein, and phospholipid content.
Distinctions in structure, protein, and size are likely to determine the
function of surfactant particles, their catabolism, or recycling by alveolar
macrophages and airway epithelial cells. Analysis of the genetic controls
governing the SP-B gene has led to the definition of DNA-protein interactions
that determine respiratory epithelial cell gene expression in general. The
important role of SP-B in lung function was defined by the study of a lethal
neonatal respiratory disease, hereditary SP-B deficiency, caused by mutations
in the human SP-B gene.
APS Manuscript Number P-0016-5.
Article publication scheduled October 1995 Physiological Reviews.
ISSN 1080-4757 Copyright 1995 The American Physiological Society.
Published in APStracts on 23 September 1995.