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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1996-12-27
|
| pubmed:abstractText |
Artificial fatty acylation of proteins has attracted significant attention during the last decade as a method for modification of protein specificity and efficacy of action on mammalian cells (A. V. Kabanov and V. Yu. Alakhov (1994) J. Contr. Release 28, 15-35). Horse radish peroxidase (HRP) is used in this work to study the interaction of a fatty acylated protein with various mammalian cells. The HRP is modified with the chloranhydride of the stearic acid in the reversed micelles of sodium bis-(2-ethylhexyl)sulfosuccinate (Aerosol OT) in octane, a convenient protocol allowing production of protein molecules with a controlled, low modification degree (A.V. Kabanov et al. (1987) Ann. N. Y. Acad. Sci. 501, 63-66). The influence of the hydrophobic group on the binding and internalization of HRP in MDCK, P3-X63-Ag8, CHO, and HepG2 cells is examined. The major results are as follows: (i) the fatty acylation of a protein significantly enhances its binding to all tested mammalian cell lines, with a line-specific efficiency; (ii) the binding efficiency can be modified by changing growth conditions in a defined medium; (iii) along with the enhancement of protein adsorption on the plasma membrane, fatty acylation increases internalization of the protein during incubations at 37 degrees C; (iv) internalized protein was observed in endocytic vesicles; no evidence was obtained for a cytoplasmic distribution. These results are discussed in connection with previously observed effects of the fatty acylated proteins on cell activity.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
1043-1802
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
6
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
608-15
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8974461-Acylation,
pubmed-meshheading:8974461-Adsorption,
pubmed-meshheading:8974461-Animals,
pubmed-meshheading:8974461-Biological Transport, Active,
pubmed-meshheading:8974461-CHO Cells,
pubmed-meshheading:8974461-Cell Line,
pubmed-meshheading:8974461-Cell Membrane,
pubmed-meshheading:8974461-Cricetinae,
pubmed-meshheading:8974461-Dogs,
pubmed-meshheading:8974461-Fatty Acids,
pubmed-meshheading:8974461-Horseradish Peroxidase,
pubmed-meshheading:8974461-Humans,
pubmed-meshheading:8974461-Mice,
pubmed-meshheading:8974461-Micelles,
pubmed-meshheading:8974461-Models, Biological,
pubmed-meshheading:8974461-Protein Processing, Post-Translational,
pubmed-meshheading:8974461-Proteins,
pubmed-meshheading:8974461-Subcellular Fractions
|
| pubmed:articleTitle |
Fatty acid acylated peroxidase as a model for the study of interactions of hydrophobically-modified proteins with mammalian cells.
|
| pubmed:affiliation |
Laboratory of Biopolymer Chemistry, Russian Research Center of Molecular Diagnostics and Therapy (RCMDT), Moscow, Russia.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|