TY - JOUR
T1 - Identification of the surfactant protein A receptor 210 as the unconventional myosin 18A
AU - Yang, Ching Hui
AU - Szeliga, Jacek
AU - Jordan, Jeremy
AU - Faske, Shawn
AU - Sever-Chroneos, Zvjezdana
AU - Dorsett, Bre
AU - Christian, Robert E.
AU - Settlage, Robert E.
AU - Shabanowitz, Jeffrey
AU - Hunt, Donald F.
AU - Whitsett, Jeffrey A.
AU - Chroneos, Zissis C.
PY - 2005/10/14
Y1 - 2005/10/14
N2 - Mass spectrometric characterization of the surfactant protein A (SP-A) receptor 210 (SP-R210) led to the identification of myosin (Myo) XVIIIA and nonmuscle 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. Furthermore, MyoXVIIIA but not MyoIIA localized to the surface of COS-1 cells, and most 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.
AB - Mass spectrometric characterization of the surfactant protein A (SP-A) receptor 210 (SP-R210) led to the identification of myosin (Myo) XVIIIA and nonmuscle 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. Furthermore, MyoXVIIIA but not MyoIIA localized to the surface of COS-1 cells, and most 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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U2 - 10.1074/jbc.M505229200
DO - 10.1074/jbc.M505229200
M3 - Article
C2 - 16087679
AN - SCOPUS:27144482229
SN - 0021-9258
VL - 280
SP - 34447
EP - 34457
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 41
ER -