Isolation and sequencing of a cDNA clone encoding 107 kDa sialoglycoprotein in rat liver lysosomal membranes

Masaru Himeno, Youichiro Noguchi, Hiroyuki Sasaki, Yoshitaka Tanaka, Koji Furuno, Akira Kono, Yoshiyuki Sakaki, Keitaro Kato

研究成果: ジャーナルへの寄稿記事

40 引用 (Scopus)

抄録

A cDNA for 107 kDa sialoglycoprotein (LGP 107), the major protein component of rat liver lysosomal membranes, was isolated and sequenced. The 1.8 kbp cDNA contained an open reading frame encoding a polypeptide consisting of 386 amino acid residues (Mr 41914). The deduced NH2-terminal 10-residue sequence is identical with that determined for purified LGP 107. The primary structure deduced for LGP 107 contains 20 potential N-glycosylation sites and exhibits 82.5, 43 and 60% sequence similarities to mouse LAMP-1, chicken LEP 100, and a 120-kDa human lysosomal glycoprotein, respectively. Among these lysosomal glycoproteins, the amino acid sequence of the putative transmembrane segment is highly conserved. Northern blot hybridization analysis identified a single species of LGP 107 mRNA (2.1 kbp in length) in rat liver, kidney, brain, lung, spleen, heart and pancreas, although its level in pancreas was very low.

元の言語英語
ページ(範囲)351-356
ページ数6
ジャーナルFEBS Letters
244
発行部数2
DOI
出版物ステータス出版済み - 2 27 1989

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Sialoglycoproteins
Liver
Rats
Pancreas
Glycoproteins
Complementary DNA
Clone Cells
Glycosylation
Membranes
Amino Acids
Northern Blotting
Open Reading Frames
Amino Acid Sequence
Chickens
Brain
Spleen
Kidney
Lung
Messenger RNA
Peptides

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

これを引用

Isolation and sequencing of a cDNA clone encoding 107 kDa sialoglycoprotein in rat liver lysosomal membranes. / Himeno, Masaru; Noguchi, Youichiro; Sasaki, Hiroyuki; Tanaka, Yoshitaka; Furuno, Koji; Kono, Akira; Sakaki, Yoshiyuki; Kato, Keitaro.

:: FEBS Letters, 巻 244, 番号 2, 27.02.1989, p. 351-356.

研究成果: ジャーナルへの寄稿記事

Himeno, Masaru ; Noguchi, Youichiro ; Sasaki, Hiroyuki ; Tanaka, Yoshitaka ; Furuno, Koji ; Kono, Akira ; Sakaki, Yoshiyuki ; Kato, Keitaro. / Isolation and sequencing of a cDNA clone encoding 107 kDa sialoglycoprotein in rat liver lysosomal membranes. :: FEBS Letters. 1989 ; 巻 244, 番号 2. pp. 351-356.
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abstract = "A cDNA for 107 kDa sialoglycoprotein (LGP 107), the major protein component of rat liver lysosomal membranes, was isolated and sequenced. The 1.8 kbp cDNA contained an open reading frame encoding a polypeptide consisting of 386 amino acid residues (Mr 41914). The deduced NH2-terminal 10-residue sequence is identical with that determined for purified LGP 107. The primary structure deduced for LGP 107 contains 20 potential N-glycosylation sites and exhibits 82.5, 43 and 60{\%} sequence similarities to mouse LAMP-1, chicken LEP 100, and a 120-kDa human lysosomal glycoprotein, respectively. Among these lysosomal glycoproteins, the amino acid sequence of the putative transmembrane segment is highly conserved. Northern blot hybridization analysis identified a single species of LGP 107 mRNA (2.1 kbp in length) in rat liver, kidney, brain, lung, spleen, heart and pancreas, although its level in pancreas was very low.",
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AU - Himeno, Masaru

AU - Noguchi, Youichiro

AU - Sasaki, Hiroyuki

AU - Tanaka, Yoshitaka

AU - Furuno, Koji

AU - Kono, Akira

AU - Sakaki, Yoshiyuki

AU - Kato, Keitaro

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N2 - A cDNA for 107 kDa sialoglycoprotein (LGP 107), the major protein component of rat liver lysosomal membranes, was isolated and sequenced. The 1.8 kbp cDNA contained an open reading frame encoding a polypeptide consisting of 386 amino acid residues (Mr 41914). The deduced NH2-terminal 10-residue sequence is identical with that determined for purified LGP 107. The primary structure deduced for LGP 107 contains 20 potential N-glycosylation sites and exhibits 82.5, 43 and 60% sequence similarities to mouse LAMP-1, chicken LEP 100, and a 120-kDa human lysosomal glycoprotein, respectively. Among these lysosomal glycoproteins, the amino acid sequence of the putative transmembrane segment is highly conserved. Northern blot hybridization analysis identified a single species of LGP 107 mRNA (2.1 kbp in length) in rat liver, kidney, brain, lung, spleen, heart and pancreas, although its level in pancreas was very low.

AB - A cDNA for 107 kDa sialoglycoprotein (LGP 107), the major protein component of rat liver lysosomal membranes, was isolated and sequenced. The 1.8 kbp cDNA contained an open reading frame encoding a polypeptide consisting of 386 amino acid residues (Mr 41914). The deduced NH2-terminal 10-residue sequence is identical with that determined for purified LGP 107. The primary structure deduced for LGP 107 contains 20 potential N-glycosylation sites and exhibits 82.5, 43 and 60% sequence similarities to mouse LAMP-1, chicken LEP 100, and a 120-kDa human lysosomal glycoprotein, respectively. Among these lysosomal glycoproteins, the amino acid sequence of the putative transmembrane segment is highly conserved. Northern blot hybridization analysis identified a single species of LGP 107 mRNA (2.1 kbp in length) in rat liver, kidney, brain, lung, spleen, heart and pancreas, although its level in pancreas was very low.

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