Mechanisms of a conversion from membrane associated lysosomal acid phosphatase to content forms

Masaru Himeno, Katsuji Nakamura, Yoshitaka Tanaka, Hidenori Yamada, Taiji Imoto, Keitaro Kato

研究成果: ジャーナルへの寄稿記事

4 引用 (Scopus)

抄録

We reported that membrane-associated APase (M-APase) is anchored in the lipid bilayer through its hydrophobic sequence close to the COOH-terminus [Biochem. Biophys. Res. Commun. (1989) 162, 1044-1053] and is released from lysosomal membranes into the lysosomal contents by limited proteolysis with cathepsin D [J. Biochem. (1990) 108, 287-291]. We here report the conversion process of M-APase to three forms of the content enzyme (C-APase I, II, and III) by assigning the COOH-terminus of each APase in lysosomes. The purified M-APase (67 kDa) was subjected to COOH-terminal determination after digestion with cathepsin D. The COOH-terminus of cathepsin D-digested M-APase (65 kDa) ended at the position of the 382nd leucine residue. The COOH-termini of C-APase I (48 kDa) and III (64 kDa) were also determined. Since the two enzymes ended at the same position of the 373rd alanine residue, this COOH-terminal is 9 amino acid residues shorter than that of cathepsin D-digested M-APase. Then, we compared NH2-terminal sequences of the three enzymes, and found that those of three enzymes are exactly the same. Therefore, protein portions of C-APase I and III proved to be identical. The above results indicate that in lysosomes M-APase is first hydrolyzed between amino acid residues 382 and 383 by cathepsin D, and after solubilization, the enzyme is converted to C-APase III by losing 9 amino acid residues by lysosomal carboxypeptidase(s). Molecular weight differences among three C-APases (III, 64 kDa; II, 55 kDa; I, 48 kDa) probably are due to different degrees of carbohydrate chain degradations as reported previously [J. Biochem. (1989) 105, 449-456].

元の言語英語
ページ(範囲)1483-1489
ページ数7
ジャーナルBiochemical and Biophysical Research Communications
180
発行部数3
DOI
出版物ステータス出版済み - 11 14 1991

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Acid Phosphatase
Cathepsin D
Membranes
Enzymes
Lysosomes
Amino Acids
Proteolysis
Carboxypeptidases
Lipid bilayers
Lipid Bilayers
Protein C
Leucine
Alanine
Digestion
Molecular Weight
Molecular weight
Carbohydrates
Degradation

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Mechanisms of a conversion from membrane associated lysosomal acid phosphatase to content forms. / Himeno, Masaru; Nakamura, Katsuji; Tanaka, Yoshitaka; Yamada, Hidenori; Imoto, Taiji; Kato, Keitaro.

:: Biochemical and Biophysical Research Communications, 巻 180, 番号 3, 14.11.1991, p. 1483-1489.

研究成果: ジャーナルへの寄稿記事

Himeno, Masaru ; Nakamura, Katsuji ; Tanaka, Yoshitaka ; Yamada, Hidenori ; Imoto, Taiji ; Kato, Keitaro. / Mechanisms of a conversion from membrane associated lysosomal acid phosphatase to content forms. :: Biochemical and Biophysical Research Communications. 1991 ; 巻 180, 番号 3. pp. 1483-1489.
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abstract = "We reported that membrane-associated APase (M-APase) is anchored in the lipid bilayer through its hydrophobic sequence close to the COOH-terminus [Biochem. Biophys. Res. Commun. (1989) 162, 1044-1053] and is released from lysosomal membranes into the lysosomal contents by limited proteolysis with cathepsin D [J. Biochem. (1990) 108, 287-291]. We here report the conversion process of M-APase to three forms of the content enzyme (C-APase I, II, and III) by assigning the COOH-terminus of each APase in lysosomes. The purified M-APase (67 kDa) was subjected to COOH-terminal determination after digestion with cathepsin D. The COOH-terminus of cathepsin D-digested M-APase (65 kDa) ended at the position of the 382nd leucine residue. The COOH-termini of C-APase I (48 kDa) and III (64 kDa) were also determined. Since the two enzymes ended at the same position of the 373rd alanine residue, this COOH-terminal is 9 amino acid residues shorter than that of cathepsin D-digested M-APase. Then, we compared NH2-terminal sequences of the three enzymes, and found that those of three enzymes are exactly the same. Therefore, protein portions of C-APase I and III proved to be identical. The above results indicate that in lysosomes M-APase is first hydrolyzed between amino acid residues 382 and 383 by cathepsin D, and after solubilization, the enzyme is converted to C-APase III by losing 9 amino acid residues by lysosomal carboxypeptidase(s). Molecular weight differences among three C-APases (III, 64 kDa; II, 55 kDa; I, 48 kDa) probably are due to different degrees of carbohydrate chain degradations as reported previously [J. Biochem. (1989) 105, 449-456].",
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AU - Himeno, Masaru

AU - Nakamura, Katsuji

AU - Tanaka, Yoshitaka

AU - Yamada, Hidenori

AU - Imoto, Taiji

AU - Kato, Keitaro

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N2 - We reported that membrane-associated APase (M-APase) is anchored in the lipid bilayer through its hydrophobic sequence close to the COOH-terminus [Biochem. Biophys. Res. Commun. (1989) 162, 1044-1053] and is released from lysosomal membranes into the lysosomal contents by limited proteolysis with cathepsin D [J. Biochem. (1990) 108, 287-291]. We here report the conversion process of M-APase to three forms of the content enzyme (C-APase I, II, and III) by assigning the COOH-terminus of each APase in lysosomes. The purified M-APase (67 kDa) was subjected to COOH-terminal determination after digestion with cathepsin D. The COOH-terminus of cathepsin D-digested M-APase (65 kDa) ended at the position of the 382nd leucine residue. The COOH-termini of C-APase I (48 kDa) and III (64 kDa) were also determined. Since the two enzymes ended at the same position of the 373rd alanine residue, this COOH-terminal is 9 amino acid residues shorter than that of cathepsin D-digested M-APase. Then, we compared NH2-terminal sequences of the three enzymes, and found that those of three enzymes are exactly the same. Therefore, protein portions of C-APase I and III proved to be identical. The above results indicate that in lysosomes M-APase is first hydrolyzed between amino acid residues 382 and 383 by cathepsin D, and after solubilization, the enzyme is converted to C-APase III by losing 9 amino acid residues by lysosomal carboxypeptidase(s). Molecular weight differences among three C-APases (III, 64 kDa; II, 55 kDa; I, 48 kDa) probably are due to different degrees of carbohydrate chain degradations as reported previously [J. Biochem. (1989) 105, 449-456].

AB - We reported that membrane-associated APase (M-APase) is anchored in the lipid bilayer through its hydrophobic sequence close to the COOH-terminus [Biochem. Biophys. Res. Commun. (1989) 162, 1044-1053] and is released from lysosomal membranes into the lysosomal contents by limited proteolysis with cathepsin D [J. Biochem. (1990) 108, 287-291]. We here report the conversion process of M-APase to three forms of the content enzyme (C-APase I, II, and III) by assigning the COOH-terminus of each APase in lysosomes. The purified M-APase (67 kDa) was subjected to COOH-terminal determination after digestion with cathepsin D. The COOH-terminus of cathepsin D-digested M-APase (65 kDa) ended at the position of the 382nd leucine residue. The COOH-termini of C-APase I (48 kDa) and III (64 kDa) were also determined. Since the two enzymes ended at the same position of the 373rd alanine residue, this COOH-terminal is 9 amino acid residues shorter than that of cathepsin D-digested M-APase. Then, we compared NH2-terminal sequences of the three enzymes, and found that those of three enzymes are exactly the same. Therefore, protein portions of C-APase I and III proved to be identical. The above results indicate that in lysosomes M-APase is first hydrolyzed between amino acid residues 382 and 383 by cathepsin D, and after solubilization, the enzyme is converted to C-APase III by losing 9 amino acid residues by lysosomal carboxypeptidase(s). Molecular weight differences among three C-APases (III, 64 kDa; II, 55 kDa; I, 48 kDa) probably are due to different degrees of carbohydrate chain degradations as reported previously [J. Biochem. (1989) 105, 449-456].

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