Identification of the SP-A receptor SP-R210 as the unconventional MyoXVIIIA

doi:10.1074/jbc.M505229200

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Papers In Press, published online ahead of print August 8, 2005
J. Biol. Chem, 10.1074/jbc.M505229200
Submitted on May 12, 2005
Revised on July 11, 2005
Accepted on August 8, 2005

Identification of the SP-A receptor SP-R210 as the unconventional MyoXVIIIA

Ching-Hui Yang, Jacek Szeliga, Jeremy Jordan, Shawn Faske, Zvjezdana Sever-Chroneos, Bre Dorsett, Robert E. Christian, Robert E. Settlage, Jeffrey Shabanowitz, Donald F. Hunt, Jeffrey A. Whitsett, and Zissis C. Chroneos

The Center of Biomedical Research, University of Texas Health Center at Tyler, Tyler, TX 75708-3154

Corresponding Author: zissis.chroneos{at}uthct.edu

Mass spectrometric characterization of the SP-A receptor SP-R210 led to the identification of Myosin XVIIIA and non-muscle Myosin IIA. Antibodies generated against the unique c–terminal tail of MyoXVIIIA revealed that MyoXVIIIA, MyoIIA, and SP-R210 have overlapping tissue distribution, all being highly expressed in myeloid cells, bone marrow, spleen, lymph nodes and lung. Western blot analysis of COS-1 cells stably transfected with either MyoXVIIIA or MyoIIA indicated that SP-R210 antibodies recognize MyoXVIIIA. Further, MyoXVIIIA but not MyoIIA localized to the surface of COS-1 cells and, importantly, expression of MyoXVIIIA in COS-1 cells conferred SP-A binding. Western analysis of recombinant MyoXVIIIA domains expressed in bacteria mapped the epitopes of previously derived SP-R210 antibodies to the neck region of MyoXVIIIA. Antibodies raised against the neck domain of MyoXVIIIA blocked the binding of SP-A to macrophages. Together, these findings indicate that MyoXVIIIA constitutes a novel receptor for SP-A.

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