Journal of Biochemistry Advance Access originally published online on May 26, 2009
Journal of Biochemistry 2009 146(3):369-373; doi:10.1093/jb/mvp079
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Human C21orf63 is a Heparin-binding Protein
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1Glycogene Function Team; 2Molecular Medicine Team; and 3Lectin Application and Analysis Team, Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan
To whom correspondence should be addressed. Tel: +81-6-6879-8424 (ext: 2480), E-mail: angata{at}sanken.osaka-u.ac.jp
Received March 3, 2009; Accepted May 18, 2009
| Abstract |
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Human C21orf63 is a type-1 transmembrane protein of hitherto unknown function, with two repeats of putative galactose-binding lectin domains'. By using glycan microarray analysis and other assays, we found that human C21orf63 interacts with heparin and to a lesser extent with heparan sulphate. The C-terminal galactose-binding lectin domain of C21orf63 is necessary for heparin binding. The inability of other human proteins with galactose-binding lectin domains to interact with heparin suggests that heparin binding is a unique property of C21orf63. Results of real-time polymerase chain reaction and tissue immunostaining imply that C21orf63 is expressed on epithelia of various human tissues.
Key Words: C21orf63, glycan microarray, heparan sulphate, heparin, lectins
Abbreviations: BSA, bovine serum albumin; CS, chondroitin sulphate; ELISA, enzyme-linked immunosorbent assay; GAG, glycosaminoglycan; HS, heparan sulphate; IgG, immunoglobulin G; PBS, phosphate-buffered saline; PBST, PBS containing 0.05% Tween 20; PCR, polymerase chain reaction; RT–PCR, reverse transcription PCR
*Present address: Division of Stem Cell Regulation, Center for Molecular Medicine, Jichi Medical University, 3311-1 Yakushiji, Shimotsuke, Tochigi 329-0498, Japan.
Present address: The Institute of Scientific and Industrial Research, Osaka University, 8-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan.