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alpha mannosidase/atrophy
Врската е зачувана во таблата со исечоци
Страница 1 од 37 резултати
Relevance of Class I α-Mannosidases to Cassava Postharvest Physiological Deterioration.
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Class I α-mannosidases (MNSs) play important roles in protein N-glycosylation. However, no data are currently available about MNSs in cassava (Manihot esculenta), of which the functions are therefore not known, particularly in relevance to postharvest physiological deterioration (PPD). A
Role of two glycosidases (alpha-mannosidase and beta-N-acetylglucosaminidase) on in vitro bovine embryonic development.
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Glycosidases are enzymes that might play a role in embryonic development. The aims of the present project were to evaluate if bovine in vitro produced embryos: (1) release beta-N-acetylglucosaminidase (beta-NAGASE) and alpha-mannosidase in culture medium and (2) to investigate if these glycosidases
The N-glycan processing enzymes alpha-mannosidase and beta-D-N-acetylhexosaminidase are involved in ripening-associated softening in the non-climacteric fruits of capsicum.
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Excessive softening of fruits during the ripening process leads to deterioration. This is of significant global importance as softening-mediated deterioration leads to huge postharvest losses. N-glycan processing enzymes are reported to play an important role during climacteric fruit softening:
Characterization of a novel mouse recombinant processing alpha-mannosidase.
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In previous work (Herscovics et al., J. Biol. Chem., 269, 9864-9871), a novel mouse alpha-mannosidase cDNA was isolated by homology, taking advantage of identical regions between the amino acid sequences of the yeast and rabbit liver processing alpha 1,2-mannosidases of different specificities to
Identification and analysis of a class 2 alpha-mannosidase from Aspergillus nidulans.
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A Class 2 alpha-mannosidase gene was cloned and sequenced from the filamentous fungus Aspergillus nidulans. A portion of the gene was amplified using degenerate oligonucleotide primers which were designed based on similarity between the Saccharomyces cerevisiae vacuolar and rat ER/cytosolic Class 2
The effects of swainsonine on the activity and expression of α-mannosidase in BRL-3A cells.
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Swainsonine (SW) is the principal toxic ingredient of locoweeds, which can cause intensive vacuolar degeneration because of α-mannosidase inhibition after animal ingestion. While SW can lead to obvious liver damage in vivo, the mechanism of hepatotoxic damage caused by SW is not clear. Therefore,
Glycoprotein biosynthesis in Saccharomyces cerevisiae. Isolation and characterization of the gene encoding a specific processing alpha-mannosidase.
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We have isolated the gene from Saccharomyces cerevisiae encoding an alpha-mannosidase of unique specificity which catalyzes the removal of one mannose residue from Man9GlcNAc to produce a single isomer of Man8GlcNAc (Jelinek-Kelly, S., and Herscovics, A. (1988) J. Biol. Chem. 263, 14757-14763).
Isolation, characterization, and expression of cDNA encoding a rat liver endoplasmic reticulum alpha-mannosidase.
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We have isolated a cDNA encoding an endoplasmic reticulum alpha-mannosidase, an asparagine-linked oligosaccharide processing enzyme, from a rat liver lambda gt11 library. Two degenerate oligonucleotides, based on amino acid sequence data from the purified enzyme, were used as primers in the
Isolation and characterization of a class II alpha-mannosidase cDNA from lepidopteran insect cells.
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Lepidopteran insect cells are used routinely as hosts for foreign glycoprotein expression by recombinant baculoviruses, but the precise nature of their N-glycosylation pathway remains poorly defined. These cells clearly have processing glucosidases and mannosidases that can convert precursors to
A donor-age-dependent change in the activity of alpha-mannosidase in human cultured RPE cells.
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Six acidic glycosidase activities in cultured human retinal pigment epithelium (RPE) cells from donors of different ages (19 to 80 years) were studied with regard to pH optimum, Km, Vmax and specific activity. For alpha-mannosidase we found significant age-dependent decreases in specific activity
Retinal and optic nerve degeneration in α-mannosidosis.
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BACKGROUND
α-mannosidosis is a rare, autosomal-recessive, lysosomal storage disease caused by a deficient activity of α-mannosidase. Typical symptoms include intellectual, motor and hearing impairment, facial coarsening, and musculoskeletal abnormalities. Ocular pathologies reported previously were
Accumulation of free oligosaccharides and tissue damage in cytosolic α-mannosidase (Man2c1)-deficient mice.
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Free Man(7-9)GlcNAc2 is released during the biosynthesis pathway of N-linked glycans or from misfolded glycoproteins during the endoplasmic reticulum-associated degradation process and are reduced to Man5GlcNAc in the cytosol. In this form, free oligosaccharides can be transferred into the lysosomes
Molecular cloning and expression of rat liver endo-alpha-mannosidase, an N-linked oligosaccharide processing enzyme.
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A clone containing the open reading frame of endo-alpha-D-mannosidase, an enzyme involved in early N-linked oligosaccharide processing, has been isolated from a rat liver lambdagt11 cDNA library. This was accomplished by a strategy that involved purification of the endomannosidase from rat liver
Characterization of the class I alpha-mannosidase gene family in the filamentous fungus Aspergillus nidulans.
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We describe the cloning and sequence characterization of three Class I alpha-1,2-mannosidase genes from the filamentous fungus Aspergillus nidulans. We used degenerate PCR primers to amplify a portion of the alpha-1,2-mannosidase IA gene and used the PCR fragment to isolate the 2495 nt genomic gene
Spontaneous and experimental glycoprotein storage disease of goats induced by Ipomoea carnea subsp fistulosa (Convolvulaceae).
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Spontaneous and experimental poisoning with the swainsonine-containing and calystegine-containing plant Ipomoea carnea subsp fistulosa is described. Three of 8 goats presenting with emaciation, weakness, symmetrical ataxia, posterior paresis, proprioceptive deficits, abnormal posture, abnormal
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