Cloning, expression, purification, and characterization of the murine lysosomal acid α-mannosidase
Catabolism of α-linked mannose residues on eukaryotic glycoproteins is accomplished by a broad specificity lysosomal α-mannosidase (EC 3.2.1.24). Based on regions of protein sequence conservation between the lysosomal α-mannosidase from Dictyostelium discoideum and the murine Golgi glycoprotein proc...
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Published in | Biochimica et biophysica acta Vol. 1336; no. 2; pp. 132 - 146 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
29.08.1997
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Subjects | |
Online Access | Get full text |
ISSN | 0304-4165 0006-3002 1872-8006 |
DOI | 10.1016/S0304-4165(97)00023-8 |
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Abstract | Catabolism of α-linked mannose residues on eukaryotic glycoproteins is accomplished by a broad specificity lysosomal α-mannosidase (EC 3.2.1.24). Based on regions of protein sequence conservation between the lysosomal α-mannosidase from
Dictyostelium discoideum and the murine Golgi glycoprotein processing α1,3/1,6-mannosidase, α-mannosidase II, we have cloned a cDNA encoding the murine lysosomal α-mannosidase. The longest of the clones was 3.1 kb in length and encoded a polypeptide of 992 amino acids containing a putative NH
2-terminal signal sequence and 11 potential N-glycosylation sites. The deduced amino acid sequence was 76.5% identical to the human lysosomal α-mannosidase and 38.1% identical to the lysosomal α-mannosidase from
D. discoideum. Expression of the cDNA in
Pichia pastoris resulted in the secretion of an α-mannosidase activity into the culture medium. This recombinant expression product was purified and was shown to have enzymatic characteristics highly similar to the enzyme purified from mammalian sources and to the human lysosomal α-mannosidase cDNA expressed in
Pichia. These characteristics include a similar pH optimum,
K
m,
V
max, inhibition by swainsonine, and activity toward natural substrates. Northern blots identified a major 3.5 kb RNA transcript in all murine tissues tested. A minor transcript of 5.4 kb was also detected in some murine tissues similar to the alternatively spliced transcripts that have been previously identified in human tissues. |
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AbstractList | Catabolism of α-linked mannose residues on eukaryotic glycoproteins is accomplished by a broad specificity lysosomal α-mannosidase (EC 3.2.1.24). Based on regions of protein sequence conservation between the lysosomal α-mannosidase from
Dictyostelium discoideum and the murine Golgi glycoprotein processing α1,3/1,6-mannosidase, α-mannosidase II, we have cloned a cDNA encoding the murine lysosomal α-mannosidase. The longest of the clones was 3.1 kb in length and encoded a polypeptide of 992 amino acids containing a putative NH
2-terminal signal sequence and 11 potential N-glycosylation sites. The deduced amino acid sequence was 76.5% identical to the human lysosomal α-mannosidase and 38.1% identical to the lysosomal α-mannosidase from
D. discoideum. Expression of the cDNA in
Pichia pastoris resulted in the secretion of an α-mannosidase activity into the culture medium. This recombinant expression product was purified and was shown to have enzymatic characteristics highly similar to the enzyme purified from mammalian sources and to the human lysosomal α-mannosidase cDNA expressed in
Pichia. These characteristics include a similar pH optimum,
K
m,
V
max, inhibition by swainsonine, and activity toward natural substrates. Northern blots identified a major 3.5 kb RNA transcript in all murine tissues tested. A minor transcript of 5.4 kb was also detected in some murine tissues similar to the alternatively spliced transcripts that have been previously identified in human tissues. Catabolism of alpha-linked mannose residues on eukaryotic glycoproteins is accomplished by a broad specificity lysosomal alpha-mannosidase (EC 3.2.1.24). Based on regions of protein sequence conservation between the lysosomal alpha-mannosidase from Dictyostelium discoideum and the murine Golgi glycoprotein processing alpha 1,3/1,6-mannosidase, alpha-mannosidase II, we have cloned a cDNA encoding the murine lysosomal alpha-mannosidase. The longest of the clones was 3.1 kb in length and encoded a polypeptide of 992 amino acids containing a putative NH2-terminal signal sequence and 11 potential N-glycosylation sites. The deduced amino acid sequence was 76.5% identical to the human lysosomal alpha-mannosidase and 38.1% identical to the lysosomal alpha-mannosidase from D. discoideum. Expression of the cDNA in Pichia pastoris resulted in the secretion of an alpha-mannosidase activity into the culture medium. This recombinant expression product was purified and was shown to have enzymatic characteristics highly similar to the enzyme purified from mammalian sources and to the human lysosomal alpha-mannosidase cDNA expressed in Pichia. These characteristics include a similar pH optimum, Km, Vmax, inhibition by swainsonine, and activity toward natural substrates. Northern blots identified a major 3.5 kb RNA transcript in all murine tissues tested. A minor transcript of 5.4 kb was also detected in some murine tissues similar to the alternatively spliced transcripts that have been previously identified in human tissues.Catabolism of alpha-linked mannose residues on eukaryotic glycoproteins is accomplished by a broad specificity lysosomal alpha-mannosidase (EC 3.2.1.24). Based on regions of protein sequence conservation between the lysosomal alpha-mannosidase from Dictyostelium discoideum and the murine Golgi glycoprotein processing alpha 1,3/1,6-mannosidase, alpha-mannosidase II, we have cloned a cDNA encoding the murine lysosomal alpha-mannosidase. The longest of the clones was 3.1 kb in length and encoded a polypeptide of 992 amino acids containing a putative NH2-terminal signal sequence and 11 potential N-glycosylation sites. The deduced amino acid sequence was 76.5% identical to the human lysosomal alpha-mannosidase and 38.1% identical to the lysosomal alpha-mannosidase from D. discoideum. Expression of the cDNA in Pichia pastoris resulted in the secretion of an alpha-mannosidase activity into the culture medium. This recombinant expression product was purified and was shown to have enzymatic characteristics highly similar to the enzyme purified from mammalian sources and to the human lysosomal alpha-mannosidase cDNA expressed in Pichia. These characteristics include a similar pH optimum, Km, Vmax, inhibition by swainsonine, and activity toward natural substrates. Northern blots identified a major 3.5 kb RNA transcript in all murine tissues tested. A minor transcript of 5.4 kb was also detected in some murine tissues similar to the alternatively spliced transcripts that have been previously identified in human tissues. Catabolism of alpha-linked mannose residues on eukaryotic glycoproteins is accomplished by a broad specificity lysosomal alpha-mannosidase (EC 3.2.1.24). Based on regions of protein sequence conservation between the lysosomal alpha-mannosidase from Dictyostelium discoideum and the murine Golgi glycoprotein processing alpha 1,3/1,6-mannosidase, alpha-mannosidase II, we have cloned a cDNA encoding the murine lysosomal alpha-mannosidase. The longest of the clones was 3.1 kb in length and encoded a polypeptide of 992 amino acids containing a putative NH2-terminal signal sequence and 11 potential N-glycosylation sites. The deduced amino acid sequence was 76.5% identical to the human lysosomal alpha-mannosidase and 38.1% identical to the lysosomal alpha-mannosidase from D. discoideum. Expression of the cDNA in Pichia pastoris resulted in the secretion of an alpha-mannosidase activity into the culture medium. This recombinant expression product was purified and was shown to have enzymatic characteristics highly similar to the enzyme purified from mammalian sources and to the human lysosomal alpha-mannosidase cDNA expressed in Pichia. These characteristics include a similar pH optimum, Km, Vmax, inhibition by swainsonine, and activity toward natural substrates. Northern blots identified a major 3.5 kb RNA transcript in all murine tissues tested. A minor transcript of 5.4 kb was also detected in some murine tissues similar to the alternatively spliced transcripts that have been previously identified in human tissues. |
Author | Merkle, Roberta K Lal, Anita Moremen, Kelley W Liao, Yung-Feng Ruest, Paul J Zhang, Yong |
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Keywords | Pichia pastoris expression cDNA cloning Glycoprotein catabolism α-Mannosidosis ORF, open reading frame pNPMan, p-nitrophenyl-α- d-mannoside PCR, polymerase chain reaction TBS, Tris-buffered saline PA, pyridylamine Lysosomal α-mannosidase RT-PCR, reverse transcription-polymerase chain reaction |
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Snippet | Catabolism of α-linked mannose residues on eukaryotic glycoproteins is accomplished by a broad specificity lysosomal α-mannosidase (EC 3.2.1.24). Based on... Catabolism of alpha-linked mannose residues on eukaryotic glycoproteins is accomplished by a broad specificity lysosomal alpha-mannosidase (EC 3.2.1.24). Based... |
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SubjectTerms | alpha-Mannosidase Amino Acid Sequence Animals Base Sequence cDNA cloning Cloning, Molecular DNA, Complementary - isolation & purification Glycoprotein catabolism Glycoproteins - metabolism Lysosomal α-mannosidase Lysosomes - enzymology Mannosidases - genetics Mannosidases - isolation & purification Mannosidases - metabolism Mice Molecular Sequence Data Molecular Weight Pichia - genetics Pichia pastoris expression Recombinant Proteins - isolation & purification α-Mannosidosis |
Title | Cloning, expression, purification, and characterization of the murine lysosomal acid α-mannosidase |
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