期刊
CELLULAR PHYSIOLOGY AND BIOCHEMISTRY
卷 25, 期 1, 页码 41-54出版社
KARGER
DOI: 10.1159/000272062
关键词
Lung surfactant; Surfactant protein-A; P63/CKAP4; Type II alveolar pneumocytes; Receptors; Receptor-mediated interactions
资金
- National Heart, Lung and Blood Institute [HL-19737]
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [P01HL019737] Funding Source: NIH RePORTER
Surfactant protein-A (SP-A) plays an important role in the clearance of surfactant from the lung alveolar space and in the regulation of surfactant secretion and uptake by type II pneumocytes in culture. Two pathways are important for the endocytosis of surfactant by type II cells and the intact lung, a receptor-mediated clathrin-dependent pathway and a non-clathrin, actin-mediated pathway. The critical role of the clathrin/receptor-mediated pathway in normal mice is supported by the finding that SP-A gene-targeted mice use the actin-dependent pathway to maintain normal clearance of surfactant. Addition of SP-A to the surfactant of the SP-A null mice rescued the phenotype, further emphasizing the essential role of the SP-A/receptor-mediated process in surfactant turnover. This review presents an overview of the structure of SP-A and its function in surfactant turnover. The evidence that the interaction of SP-A with type II cells is a receptor-mediated process is presented. A newly identified receptor for SP-A, P63/CKAP4, is described in detail, with elucidation of the specific structural features of this 63 kDa, nonglycosylated, highly coiled, transmembrane protein. The compelling evidence that P63 functions as a receptor for SP-A on type II cells is summarized. Regulation of P63 receptor density on the surface of pneumocytes may be a novel approach for the regulation of surfactant homeostasis by the lung. Copyright (C) 2010 S. Karger AG, Basel
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