Linked Life Data

1478888

Source:http://linkedlifedata.com/resource/pubmed/id/1478888

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1993-2-9
pubmed:abstractText
The discovery of endogenous lectins having specific and high affinity for the carbohydrate portions of glycoproteins has opened up new directions in the field of cell adhesion and cell recognition. Two endogenous lectins, termed as CSL and R1, initially isolated from the rat cerebellum and having a wide distribution in mammalian tissues, have been shown to participate in essential mechanisms of cell adhesion. The membrane-bound lectin R1 seems to be involved in transient recognition between neuronal cells, followed by elimination of the glycoprotein ligands at the surface of the recognized cell. In contrast, CSL is a molecule involved in adhesion between various normal or transformed cells since it participates in the formation of tight junctions. The glycoprotein ligands recognized with higher affinity by these two lectins seem to possess a special structure which defines a sub-class of oncofetal HNK-1 glycans. The over-expression of the glycoprotein ligands of these lectins in most transformed cells provides new tools for understanding the underlying mechanism of malignant transformation as well as the generation of signals through cell adhesion.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0018-2214
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
791-804
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Glycoproteins and lectins in cell adhesion and cell recognition processes.
pubmed:affiliation
Laboratoire de Neurobiologie Moléculaire des Interactions Cellulaires, CNRS UPR 416, Strasbourg, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't