Linked Life Data

8702812

Source:http://linkedlifedata.com/resource/pubmed/id/8702812

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
34
pubmed:dateCreated
1996-10-11
pubmed:databankReference
pubmed:abstractText
A detailed understanding of the mechanism of lipid transport in insects has been hampered by the inability to identify the proapolipophorin gene that encodes apolipophorins I and II, the principal protein components of lipophorin, the lipid transport vehicle. Here we provide the first molecular description of the Drosophila gene encoding a retinoid- and fatty acid-binding glycoprotein (RFABG) and present evidence that it is a member of the proapolipophorin gene family. The gene, localized to the chromosome 4 (102 F region), encodes a 3351-amino acid protein that could serve as the precursor for the approximately 70-kDa and >200-kDa polypeptides associated with RFABG. The N-terminal sequence of the approximately 70-kDa polypeptide and that predicted for the >200-kDa polypeptide showed high sequence similarity to blowfly apolipophorin II and apolipophorin I, respectively. The RFABG precursor contains a signal peptide and exhibits a multidomain mosaic protein structure, which is typical of extracellular proteins. It has structural domains similar to lipid-binding proteins, namely vitellogenins and apolipoprotein B. The protein also contains a domain similar to the D domain of von Willebrand factor and mucin. The gene is expressed in the Drosophila embryo during development in cells that make up the amnioserosa and fat bodies. Immunolocalizations using specific antibodies against RFABG reveal that the protein is initially dispersed through the embryonic amnioserosa sac and latter concentrated at skeletal muscle-epidermis apodemeal contact junctions during larval development. This novel gene may play an important role in the transport of lipids, including retinoids and fatty acids, in insects.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
20641-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8702812-Amino Acid Sequence, pubmed-meshheading:8702812-Animals, pubmed-meshheading:8702812-Base Sequence, pubmed-meshheading:8702812-Carrier Proteins, pubmed-meshheading:8702812-Chromosome Mapping, pubmed-meshheading:8702812-Drosophila Proteins, pubmed-meshheading:8702812-Drosophila melanogaster, pubmed-meshheading:8702812-Fatty Acid-Binding Proteins, pubmed-meshheading:8702812-Fatty Acids, pubmed-meshheading:8702812-Gene Expression Regulation, Developmental, pubmed-meshheading:8702812-Genes, Insect, pubmed-meshheading:8702812-Glycoproteins, pubmed-meshheading:8702812-Lipoproteins, pubmed-meshheading:8702812-Molecular Sequence Data, pubmed-meshheading:8702812-Protein Structure, Secondary, pubmed-meshheading:8702812-RNA, Messenger, pubmed-meshheading:8702812-Retinoids, pubmed-meshheading:8702812-Sequence Alignment, pubmed-meshheading:8702812-Sequence Homology, Amino Acid
pubmed:year
1996
pubmed:articleTitle
Molecular characterization and developmental expression of a retinoid- and fatty acid-binding glycoprotein from Drosophila. A putative lipophorin.
pubmed:affiliation
Laboratory of Retinal Cell and Molecular Biology, NEI, National Institutes of Health, Bethesda, Maryland 20892, USA.
pubmed:publicationType
Journal Article, Comparative Study