Linked Life Data

20384789

Source:http://linkedlifedata.com/resource/pubmed/id/20384789

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2010-6-11
pubmed:abstractText
Lepidoptera such as the domestic silkworm (Bombyx mori) produce proteins modified with unsialylated, mannose-rich moieties known as 'high mannose-type'N-glycans. However, we observed that, under intrinsic acetylglucosaminidase (GlcNAcase)-inhibited conditions, moth cells tend to synthesize different types of glycoform with sialic acid modification. To identify molecules essential to assemble Lepidoptera-specific N-glycans, we performed BLAST analysis on the silkworm genetic database and isolated the entire coding sequence of novel Bombyx GlcNAcase, BmGlcNAcase 2. This enzyme showed weak homology to currently known, lysosome-associated eukaryotic hexosaminidases, but it revealed remarkable similarity with recently reported glycosyl hydrolases of Spodoptera and Bombyx. Interestingly, BmGlcNAcase 2 was found to be expressed in embryos and in certain tissues of molting larvae (i.e. ovary, fat bodies, mid-intestine, skin), but not in pupae, suggesting its unique function in the carbohydrate metabolism of juvenile silkworm.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1365-2443
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
525-36
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Molecular cloning and expression profile analysis of a novel beta-D-N-acetylhexosaminidase of domestic silkworm (Bombyx mori).
pubmed:affiliation
Advanced Biologicals, National Institute of Animal Health, NARO, 3-1-5 Kannondai, Tsukuba, Ibaraki 305-0856, Japan. takehiro@affrc.go.jp
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural