Linked Life Data

2450119

Source:http://linkedlifedata.com/resource/pubmed/id/2450119

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1988-4-20
pubmed:abstractText
We have used electron microscopic immunocytochemistry to compare the distribution of LAMP-1, a marker for lysosomal membranes, with the intracellular localization of alpha 2-macroglobulin (alpha 2-M) and transferrin at various time points after their endocytosis into cultured NIH 3T3 cells. The purposes of this study were (a) to determine how soon endocytic ligands reach lysosomal organelles, (b) to examine whether the intermediate endocytic vesicles gained lysosomal markers gradually or in a precipitous, discrete event, and (c) to examine the relationship, if any, between the pathway of recycling ligands and lysosomes. At early time points (0-5 min) after initiation of endocytosis, most structures containing alpha 2-M labeled with colloidal gold (receptosomes) were not labeled by anti-LAMP-1 detected using ferritin bridge or peroxidase immunocytochemistry. At late time points (greater than or equal to 15 min), the structures containing alpha 2-M (lysosomes) were strongly labeled by anti-LAMP-1. In contrast, transferrin that was directly labeled with ferritin was mostly located in LAMP-1-negative structures at all time points studied. The proportion of alpha 2-M-gold containing vesicles strongly labeled for LAMP-1 roughly paralleled the proportion of alpha 2-M-gold-containing structures positive for cytochemically detectable acid phosphatase. Our data indicate that ligands such as transferrin that are internalized through coated pits and receptosomes, but not delivered to lysosomes, do not traverse a lysosomal organelle compartment as marked by LAMP-1 content. Ligands such as alpha 2-M that are destined for lysosomal delivery reach a LAMP-1-positive organelle compartment only after they traverse LAMP-1-negative, non-lysosomal vesicles previously described as receptosomes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-1554
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
391-400
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:2450119-Acid Phosphatase, pubmed-meshheading:2450119-Animals, pubmed-meshheading:2450119-Antibodies, Monoclonal, pubmed-meshheading:2450119-Antigens, CD, pubmed-meshheading:2450119-Cell Line, pubmed-meshheading:2450119-Endocytosis, pubmed-meshheading:2450119-Gold, pubmed-meshheading:2450119-Histocytochemistry, pubmed-meshheading:2450119-Humans, pubmed-meshheading:2450119-Immunoassay, pubmed-meshheading:2450119-Immunoenzyme Techniques, pubmed-meshheading:2450119-Kinetics, pubmed-meshheading:2450119-Lysosome-Associated Membrane Glycoproteins, pubmed-meshheading:2450119-Lysosomes, pubmed-meshheading:2450119-Membrane Glycoproteins, pubmed-meshheading:2450119-Mice, pubmed-meshheading:2450119-Microscopy, Electron, pubmed-meshheading:2450119-Organoids, pubmed-meshheading:2450119-Transferrin, pubmed-meshheading:2450119-alpha-Macroglobulins
pubmed:year
1988
pubmed:articleTitle
Pre-lysosomal divergence of alpha 2-macroglobulin and transferrin: a kinetic study using a monoclonal antibody against a lysosomal membrane glycoprotein (LAMP-1).
pubmed:affiliation
Laboratory of Molecular Biology, National Cancer Institute, Bethesda, Maryland.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't