Expression and Characterization of a Very Low Density Lipoprotein Receptor Variant Lacking the O-Linked Sugar Region Generated by Alternative Splicing
Identifieur interne : 002760 ( Main/Exploration ); précédent : 002759; suivant : 002761Expression and Characterization of a Very Low Density Lipoprotein Receptor Variant Lacking the O-Linked Sugar Region Generated by Alternative Splicing
Auteurs : Hiroaki Iijima ; Masaaki Miyazawa ; Juro Sakai ; Kenta Magoori ; Mitsuko R. Ito ; Hiroyuki Suzuki ; Masato Nose ; Yutaka Kawarabayasi ; Tokuo T. Yamamoto [Japon]Source :
- The Journal of Biochemistry [ 0021-924X ] ; 1998.
Abstract
The very low density lipoprotein receptor (VLDLR) gene contains an exon encoding a region of clustered serine and threonine residues immediately outside the membrane-spanning sequence, and this region has been proposed to be the site of clustered O-linked carbohydrate chains. Two forms of VLDLR transcripts, with and without the O-linked sugar region, are generated through alternative splicing. Reverse transcription polymerase chain reaction with RNAs from various rabbit tissues revealed that the VLDLR transcript with the O-linked sugar region (type-1 VLDLR) is the major transcript in heart and muscle, while the VLDLR transcript without the O-linked sugar region (type-2 VLDLR) predominates in non-muscle tissues, including cerebrum, cerebellum, kidney, spleen, adrenal gland, testis, ovary, and uterus. Hamster fibroblasts expressing type-2 VLDLR bound with relatively low affinity to β-migrating very low density lipoprotein compared with type-1 VLDLR-transfected cells. In contrast, the internalization, dissociation, and degradation of the ligand were not significantly impaired in either type of VLDLR-transfected cell. The receptor proteins in type-2 VLDLR-transfected cells underwent rapid degradation and accumulated in the culture medium, while those in type-1 VLDLR-transfected cells were stable and resistant to proteolytic cleavage. Analysis of the O-linked sugars of both types of transfected cells suggested that the O-linked sugar region is the major site for O-glycosylation.
Url:
DOI: 10.1093/oxfordjournals.jbchem.a022175
Affiliations:
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Ito</name><affiliation><wicri:noCountry code="subField">981-8555</wicri:noCountry></affiliation></author><author><name sortKey="Suzuki, Hiroyuki" sort="Suzuki, Hiroyuki" uniqKey="Suzuki H" first="Hiroyuki" last="Suzuki">Hiroyuki Suzuki</name><affiliation><wicri:noCountry code="subField">981-8555</wicri:noCountry></affiliation></author><author><name sortKey="Nose, Masato" sort="Nose, Masato" uniqKey="Nose M" first="Masato" last="Nose">Masato Nose</name><affiliation><wicri:noCountry code="subField">585-8511</wicri:noCountry></affiliation></author><author><name sortKey="Kawarabayasi, Yutaka" sort="Kawarabayasi, Yutaka" uniqKey="Kawarabayasi Y" first="Yutaka" last="Kawarabayasi">Yutaka Kawarabayasi</name><affiliation><wicri:noCountry code="subField">981-8555</wicri:noCountry></affiliation></author><author><name sortKey="Yamamoto, Tokuo T" sort="Yamamoto, Tokuo T" uniqKey="Yamamoto T" first="Tokuo T." last="Yamamoto">Tokuo T. Yamamoto</name><affiliation></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Japon</country></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Japon</country></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">The Journal of Biochemistry</title><idno type="eISSN">-</idno><idno type="ISSN">0021-924X</idno><imprint><publisher>Oxford University Press</publisher><date when="1998-10">1998</date><biblScope unit="vol">124</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="747">747</biblScope><biblScope unit="page" to="755">755</biblScope></imprint><idno type="ISSN">0021-924X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0021-924X</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">The very low density lipoprotein receptor (VLDLR) gene contains an exon encoding a region of clustered serine and threonine residues immediately outside the membrane-spanning sequence, and this region has been proposed to be the site of clustered O-linked carbohydrate chains. Two forms of VLDLR transcripts, with and without the O-linked sugar region, are generated through alternative splicing. Reverse transcription polymerase chain reaction with RNAs from various rabbit tissues revealed that the VLDLR transcript with the O-linked sugar region (type-1 VLDLR) is the major transcript in heart and muscle, while the VLDLR transcript without the O-linked sugar region (type-2 VLDLR) predominates in non-muscle tissues, including cerebrum, cerebellum, kidney, spleen, adrenal gland, testis, ovary, and uterus. Hamster fibroblasts expressing type-2 VLDLR bound with relatively low affinity to β-migrating very low density lipoprotein compared with type-1 VLDLR-transfected cells. In contrast, the internalization, dissociation, and degradation of the ligand were not significantly impaired in either type of VLDLR-transfected cell. The receptor proteins in type-2 VLDLR-transfected cells underwent rapid degradation and accumulated in the culture medium, while those in type-1 VLDLR-transfected cells were stable and resistant to proteolytic cleavage. Analysis of the O-linked sugars of both types of transfected cells suggested that the O-linked sugar region is the major site for O-glycosylation.</div></front></TEI><affiliations><list><country><li>Japon</li></country></list><tree><noCountry><name sortKey="Iijima, Hiroaki" sort="Iijima, Hiroaki" uniqKey="Iijima H" first="Hiroaki" last="Iijima">Hiroaki Iijima</name><name sortKey="Ito, Mitsuko R" sort="Ito, Mitsuko R" uniqKey="Ito M" first="Mitsuko R." last="Ito">Mitsuko R. 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