Isolation and sequencing of a cDNA clone encoding 96 kDa sialoglycoprotein in rat liver lysosomal membranes

Youichiro Noguchi, Masaru Himeno, Hiroyuki Sasaki, Yoshitaka Tanaka, Akira Kono, Yasuyuki Sakaki, Keitaro Kato

研究成果: ジャーナルへの寄稿記事

20 引用 (Scopus)

抄録

We isolated and sequenced LGP 96, a cDNA clone corresponding to the entire coding sequence of the rat liver lysosomal membrane sialoglycoprotein with an apparent Mr of 96 K, LGP 96. The deduced amino acid sequence indicates that LGP 96 consists of 411 amino acid residues (Mr 45,163) and the 26 NH2-terminal residues presumably constitute a cleavable signal peptide. The major portion of LGP 96 resides on the luminal side of the lysosome and bears a large number of N-linked heavily sialylated complex type carbohydrate chains, giving the mature molecule of 96 kDa. The protein has 17 potential N-glycosylation sites and 32.1 and 65.3% sequence similarities in amino acid to LGP 107 and human lamp-2,respectively. The glycosylation sites are clustered into two domains separated by a hinge-like structure enriched with proline and threonine. LGP 96 possesses one putative transmembrane domain consisting of 24 hydrophobic amino acids near the COOH-terminus and contains a short cytoplasmic segment constituting 12 amino acid residues at the COOH-terminal end. Comparison of LGP 96 and recently cloned lysosomal membrane glycoprotein sequences reveals strong similarity in the putative transmembrane domain and cytoplasmic tail. It is very likely that these portions are important for the targeting of molecules to lysosomes. A comparison of LGP 96 and LGP 107 showed numberous structural similarities.

元の言語英語
ページ(範囲)1113-1120
ページ数8
ジャーナルBiochemical and Biophysical Research Communications
164
発行部数3
DOI
出版物ステータス出版済み - 11 15 1989

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Sialoglycoproteins
Liver
Rats
Complementary DNA
Clone Cells
Membranes
Amino Acids
Glycosylation
Lysosomes
Lysosome-Associated Membrane Glycoproteins
Threonine
Protein Sorting Signals
Proline
Molecules
Tail
Amino Acid Sequence
Hinges
Electric lamps
Carbohydrates
Proteins

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Isolation and sequencing of a cDNA clone encoding 96 kDa sialoglycoprotein in rat liver lysosomal membranes. / Noguchi, Youichiro; Himeno, Masaru; Sasaki, Hiroyuki; Tanaka, Yoshitaka; Kono, Akira; Sakaki, Yasuyuki; Kato, Keitaro.

:: Biochemical and Biophysical Research Communications, 巻 164, 番号 3, 15.11.1989, p. 1113-1120.

研究成果: ジャーナルへの寄稿記事

Noguchi, Youichiro ; Himeno, Masaru ; Sasaki, Hiroyuki ; Tanaka, Yoshitaka ; Kono, Akira ; Sakaki, Yasuyuki ; Kato, Keitaro. / Isolation and sequencing of a cDNA clone encoding 96 kDa sialoglycoprotein in rat liver lysosomal membranes. :: Biochemical and Biophysical Research Communications. 1989 ; 巻 164, 番号 3. pp. 1113-1120.
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abstract = "We isolated and sequenced LGP 96, a cDNA clone corresponding to the entire coding sequence of the rat liver lysosomal membrane sialoglycoprotein with an apparent Mr of 96 K, LGP 96. The deduced amino acid sequence indicates that LGP 96 consists of 411 amino acid residues (Mr 45,163) and the 26 NH2-terminal residues presumably constitute a cleavable signal peptide. The major portion of LGP 96 resides on the luminal side of the lysosome and bears a large number of N-linked heavily sialylated complex type carbohydrate chains, giving the mature molecule of 96 kDa. The protein has 17 potential N-glycosylation sites and 32.1 and 65.3{\%} sequence similarities in amino acid to LGP 107 and human lamp-2,respectively. The glycosylation sites are clustered into two domains separated by a hinge-like structure enriched with proline and threonine. LGP 96 possesses one putative transmembrane domain consisting of 24 hydrophobic amino acids near the COOH-terminus and contains a short cytoplasmic segment constituting 12 amino acid residues at the COOH-terminal end. Comparison of LGP 96 and recently cloned lysosomal membrane glycoprotein sequences reveals strong similarity in the putative transmembrane domain and cytoplasmic tail. It is very likely that these portions are important for the targeting of molecules to lysosomes. A comparison of LGP 96 and LGP 107 showed numberous structural similarities.",
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AU - Kono, Akira

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AU - Kato, Keitaro

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