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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1990-1-30
|
| pubmed:abstractText |
The ultrastructure of binding, internalization, and translocation of beta-migrating very low density lipoprotein (beta-VLDL) and acetylated low density lipoprotein (Ac-LDL) by cultured pigeon monocytes was examined using lipoprotein-gold conjugates. Through morphometry, differences in the binding and uptake of beta-VLDL-gold and Ac-LDL-gold were documented. Cells exposed to either beta-VLDL-gold or Ac-LDL-gold for 2 hr at 4 degrees C had the label over noncoated regions of the plasma membrane. Upon warming the cells to 37 degrees C for 2 min, 35% of the surface-bound beta-VLDL-gold was within coated pits on the cell surface. Although coated pits occupied less than 2% of the surface, binding of beta-VLDL-gold was 53 times more concentrated in coated pits as compared to noncoated membrane regions. In contrast, Ac-LDL-gold neither bound to coated pits nor relocated into coated regions of the membrane upon warming to 37 degrees C. Both the beta-VLDL-gold and the Ac-LDL-gold were internalized when the cells were rewarmed at 37 degrees C. Most of the internalized gold particles for both lipoproteins were located in electron-lucent vesicles; however, 9% of the intracellular beta-VLDL-gold was observed within coated vesicles at early times. Upon prolonged rewarming (30-90 min), both lipoprotein-gold conjugates were within acid phosphatase-positive lysosomes. Ultimately 83% of the Ac-LDL-gold and 90% of the beta-VLDL-gold were within electron-dense and electron-lucent lysosomes. These results suggested that the receptor-mediated binding and internalization of beta-VLDL and Ac-LDL by pigeon monocyte macrophages proceeded by separate, distinct routes; beta-VLDL by both coated and noncoated pathways while Ac-LDL was internalized exclusively by noncoated mechanisms. Regardless of these internalization differences, both lipoproteins were delivered to lysosomes for degradation.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acid Phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, VLDL,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Scavenger,
http://linkedlifedata.com/resource/pubmed/chemical/VLDL receptor,
http://linkedlifedata.com/resource/pubmed/chemical/acetyl-LDL
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0014-4800
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
51
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
243-63
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:2513225-Acid Phosphatase,
pubmed-meshheading:2513225-Animals,
pubmed-meshheading:2513225-Cell Adhesion Molecules,
pubmed-meshheading:2513225-Cell Compartmentation,
pubmed-meshheading:2513225-Cells, Cultured,
pubmed-meshheading:2513225-Coated Pits, Cell-Membrane,
pubmed-meshheading:2513225-Columbidae,
pubmed-meshheading:2513225-Electron Probe Microanalysis,
pubmed-meshheading:2513225-Endocytosis,
pubmed-meshheading:2513225-Foam Cells,
pubmed-meshheading:2513225-Immunohistochemistry,
pubmed-meshheading:2513225-Lipoproteins, LDL,
pubmed-meshheading:2513225-Lipoproteins, VLDL,
pubmed-meshheading:2513225-Lysosomes,
pubmed-meshheading:2513225-Macrophages,
pubmed-meshheading:2513225-Monocytes,
pubmed-meshheading:2513225-Organelles,
pubmed-meshheading:2513225-Receptors, LDL,
pubmed-meshheading:2513225-Receptors, Scavenger
|
| pubmed:year |
1989
|
| pubmed:articleTitle |
Morphological characterization of beta-VLDL and acetylated-LDL binding and internalization by cultured pigeon monocytes.
|
| pubmed:affiliation |
Department of Pathology, Wake Forest University, Bowman Gray School of Medicine, Winston-Salem, North Carolina 27103.
|
| pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|