Journal of Biochemistry Advance Access published online on December 14, 2006
Journal of Biochemistry, doi:10.1093/jb/mvm009
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
© 2006 The Japanese Biochemical Society
Ligand-binding activity and expression profile of annexins in Caenorhabditis elegans
,1
*Graduate School of Humanities and Sciences and the Glycoscience Institute, Ochanomizu University, 2-1-1 Otsuka, Bunkyo-ku, Tokyo 112-8610, Japan
Laboratory of Cellular Biochemistry, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan
1To whom correspondence should be addressed. Tel: +81-3-5978-5345, Fax: +81-3-5978-5345, E-mail: kyoko{at}cc.ocha.ac.jp
Received November 8, 2006; Accepted November 13, 2006
 |
Abstract |
|---|
Mamalian annexins are implicated in several physiological mechanisms based on their calcium-dependent phospholipid/membrane binding and carbohydrate-binding activities. In this study, we investigated gene expression profiles of all four Caenorhabditis elegans annexins, nex-1, –2, –3 and –4, throughout the development, and compared phospholipid- and carbohydrate-binding properties of their protein products, NEX–1, –2, –3 and –4. We found that nex–1 and –3 are transcribed continuously during the developmental stages, while expression of nex–2 and –4 appeared to be temporal, peaking at the L1 stage followed by a gradual decrease toward the adult stage. NEX–1 and –3 were detected as single protein band in total worm extracts by immunoblotting, but NEX–2 was heterogenic in size. NEX–1, –2, and –3 showed the binding activities to phosphatidylserine, phosphatidylinositol and phosphatidylethanolamine, but not to phosphatidylcholine. In contrast to their uniform phospholipids-binding properties, their glycosaminoglycan-binding activities were distinctive. NEX–2 bound to heparan sulfate and chondroitin, NEX–3 bound only to heparan sulfate, and NEX–1 showed no lectin activities under tested conditions. NEX–4 had neither phospholipids- nor carbohydrate-binding properties. Differentiated expression profiles and ligand-binding properties of NEX–1, –2, –3 and –4, shown in our study, may represent distinctive roles for each C. elegans annexins.
Key Words: annexin, lectin, C. elegans, glycosaminoglycan, phospholipid
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  A. Marson, D. E Robinson, P. N Brookes, B. Mulloy, M. Wiles, S. J Clark, H. L Fielder, L. J Collinson, S. A Cain, C. M Kielty, et al. Development of a microtiter plate-based glycosaminoglycan array for the investigation of glycosaminoglycan-protein interactions Glycobiology, December 1, 2009; 19(12): 1537 - 1546. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. Mitsunaga, J. Harada-Itadani, T. Shikanai, H. Tateno, Y. Ikehara, J. Hirabayashi, H. Narimatsu, and T. Angata Human C21orf63 is a Heparin-binding Protein J. Biochem., September 1, 2009; 146(3): 369 - 373. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. Tateno, A. Mori, N. Uchiyama, R. Yabe, J. Iwaki, T. Shikanai, T. Angata, H. Narimatsu, and J. Hirabayashi Glycoconjugate microarray based on an evanescent-field fluorescence-assisted detection principle for investigation of glycan-binding proteins Glycobiology, October 1, 2008; 18(10): 789 - 798. [Abstract] [Full Text] [PDF]
|
|