Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
1992-12-22
|
pubmed:abstractText |
We have purified and characterized a galactose-binding lectin from the gonads of the mollusk Aplysia californica that modulates neurite outgrowth from cultured Aplysia neurons. Agglutination of sheep red blood cells (RBC) by this lectin, termed Aplysia gonad lectin (AGL), is inhibited strongly by galactose and to a lesser extent by fucose. On SDS-PAGE, AGL appears as a single species with a molecular weight of 34 kD under reducing conditions, and 65 kD under nonreducing conditions. This suggests that AGL is a disulfide-linked dimer in its native state. Amino terminal sequence analysis of purified AGL indicates a similarity to another galactose-binding lectin, phytohemagglutinin-E (E-PHA), found in red kidney beans. By using polyclonal antibodies prepared against AGL, we have found that the lectin is present in the gonads and eggs but not in other tissues of adult Aplysia californica. We have examined biological actions of AGL on Aplysia neurons growing in primary cell culture. AGL affects several properties of these neurons. The addition of 100 nM AGL to cultured neurons enhances neurite outgrowth from the cell soma, resulting in a greater number of primary processes. In addition, AGL acts as a neurotrophic agent, increasing neurite viability in vitro. This trophic effect is not seen with concanavalin A (con A), another lectin known to affect several properties of cultured Aplysia neurons. The results are consistent with the suggestion that AGL may play a role in neuronal differentiation and/or maintenance of viability.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0022-3034
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
23
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
739-50
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:1431843-Amino Acid Sequence,
pubmed-meshheading:1431843-Animals,
pubmed-meshheading:1431843-Aplysia,
pubmed-meshheading:1431843-Blotting, Western,
pubmed-meshheading:1431843-Cell Aggregation,
pubmed-meshheading:1431843-Cells, Cultured,
pubmed-meshheading:1431843-Concanavalin A,
pubmed-meshheading:1431843-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1431843-Erythrocytes,
pubmed-meshheading:1431843-Galectins,
pubmed-meshheading:1431843-Hemagglutinins,
pubmed-meshheading:1431843-Iodine Radioisotopes,
pubmed-meshheading:1431843-Molecular Sequence Data,
pubmed-meshheading:1431843-Neurons,
pubmed-meshheading:1431843-Sheep
|
pubmed:year |
1992
|
pubmed:articleTitle |
Modulation of growth of Aplysia neurons by an endogenous lectin.
|
pubmed:affiliation |
Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|