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P63 (CKAP4) as an SP-A Receptor: Implications for Surfactant Turnover

Bates S.R.

Author affiliations

Institute for Environmental Medicine, Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia

Corresponding Author

Sandra R. Bates, Ph.D.

Institute for Environmental Medicine, Department of Physiology

University of Pennsylvania School of Medicine

Philadelphia, PA 19104 (USA)

E-Mail batekenn@mail.med.upenn.edu

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Cell Physiol Biochem 2010;25:041–054

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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.

© 2010 S. Karger AG, Basel

Article / Publication Details

First-Page Preview
Abstract of Review

Accepted: July 02, 2009
Published online: December 22, 2009
Issue release date: December 2009

Number of Print Pages: 14
Number of Figures: 0
Number of Tables: 0

ISSN: 1015-8987 (Print)
eISSN: 1421-9778 (Online)

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