Linked Life Data

7556146

Source:http://linkedlifedata.com/resource/pubmed/id/7556146

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-11-14
pubmed:abstractText
It has been proposed that unconjugated type I ribosome-inactivating proteins (RIP) enter cells through passive mechanisms such as fluid-phase pinocytosis. However, some observations, such as the difference in sensitivity to type I RIP among different cell types, and the organ-specific toxicity of type I RIP, indicate a specific mechanism for the entry of these proteins into target cells. The alpha 2-macroglobulin receptor (alpha 2MR) is responsible for the binding and endocytosis of several ligands, including alpha 2-macroglobulin/proteinase complexes, plasminogen-activator-inhibitor complexes, apoE-enriched beta-very low density lipoproteins, and lipoprotein lipase. Here we demonstrate that saporin, a potent type I RIP, binds specifically to purified alpha 2MR and the binding is prevented by some alpha 2MR ligands. Moreover, the occupancy of specific ligand-binding sites on cell surface alpha 2MR decreases the cytotoxicity of saporin. The A chain of ricin, a type II RIP, also interacts with alpha 2MR. This, and the fact that saporin and ricin A chain both interact also with alpha 2-macroglobulin, indicates a general mechanism of complex interactions between RIP and cellular membranes that is mediated by alpha 2-macroglobulin and the alpha 2MR system.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
232
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
165-71
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Alpha 2-macroglobulin receptor mediates binding and cytotoxicity of plant ribosome-inactivating proteins.
pubmed:affiliation
Department of Biological and Technological Research, San Raffaele Scientific Institute, Milano, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't