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J. Biol. Chem., Vol. 281, Issue 15, 10381-10388, April 14, 2006

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Molecular Cloning and Characterization of Chick SPACRCAN^*

Yoko Inoue, Masahiko Yoneda, Jinsong Zhao, Osamu Miyaishi^¶, Akiko Ohno-Jinno, Takuya Kataoka, Zenzo Isogai^||, Koji Kimata^**, Masayoshi Iwaki, and Masahiro Zako¹

From the Departments of Ophthalmology and ^¶Pathology and the ^**Institute for Molecular Science of Medicine, Aichi Medical University, Nagakute, Aichi 480-1195, Japan, the Aichi Prefectural College of Nursing and Health, Nagoya, Aichi 463-8502, Japan, and the ^||Department of Dermatology, National Center for Geriatrics and Gerontology, Aichi 474-8511, Japan

MY-174, a monoclonal antibody that reacts with specific sialylated O-linked glycoconjugates of chick SPACR (sialoprotein associated with cones and rods), also recognizes another molecule of 300 kDa. Here, we verified that this 300-kDa molecule is chick SPACRCAN (sialoproteoglycan associated with cones and rods), another member of a novel interphotoreceptor matrix molecule family. Screening for chick SPACRCAN was carried out by plaque hybridization using a probe for chick SPACR. Specific polyclonal antibodies raised against chick SPACRCAN were used for the following experiments. To determine whether the 300-kDa molecule detected by MY-174 was identical to 300-kDa chick SPACRCAN, the migrations of these bands were examined after various glycosidase digestions. Furthermore, the expression levels were measured during retinal development and compared with those of chick SPACR. The results demonstrated that the 300-kDa molecule recognized by MY-174 was chick SPACRCAN, and we further identified it as a proteoglycan with chondroitin sulfate chains. SPACRCAN had heavily sialylated N- and O-linked glycoconjugates, and its MY-174 antigenicity was abolished by O-glycanase treatment after neuraminidase treatment, as observed for chick SPACR. During retinal development, the mRNA and core protein expression levels, MY-174 antigenicity, and hyaluronan binding ability of SPACRCAN peaked around embryonic day 17 and then gradually decreased, whereas the corresponding expression levels of SPACR simply increased, but not its hyaluronan binding ability. The MY-174 reactivity of SPACRCAN in the adult retina was decreased compared with that in the newborn retina, whereas that of SPACR was increased. The decreased hyaluronan binding of SPACR was induced by an inhibitory effect of the excess of sialic acids in the adult stage. Thus, with similar core protein structures and specific sialylated glycoconjugates but distinct chondroitin sulfate chains, SPACRCAN and SPACR may have separate roles in the retina due to their differing expression profiles during development.

Received for publication, July 26, 2005 , and in revised form, December 8, 2005.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AB 204591.

^* This work was supported in part by Grant-in-aid for Scientific Research 15591881 from the Ministry of Education, Culture, Sports, Science, and Technology, Japan. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Dept. of Ophthalmology, Aichi Medical University, Nagakute-cho, Aichi-gun, Aichi-ken 480-1195, Japan. Tel.: 81-52-264-4811; Fax: 81-561-63-7255; E-mail: zako{at}aichi-med-u.ac.jp.

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