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 inBiochimica et biophysica acta Vol. 1336; no. 2; pp. 132 - 146
Main Authors Merkle, Roberta K, Zhang, Yong, Ruest, Paul J, Lal, Anita, Liao, Yung-Feng, Moremen, Kelley W
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 29.08.1997
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ISSN0304-4165
0006-3002
1872-8006
DOI10.1016/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.
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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Issue 2
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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StartPage 132
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
URI https://dx.doi.org/10.1016/S0304-4165(97)00023-8
https://www.ncbi.nlm.nih.gov/pubmed/9305783
https://www.proquest.com/docview/79295170
Volume 1336
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