Bibliographic Citation
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| Title | Acylation of cellular proteins with endogenously synthesized fatty acids |
| Creator/Author | Towler, D. ; Glaser, L. |
| Publication Date | 1986 Feb 25 |
| OSTI Identifier | OSTI ID: 5623581 |
| Other Number(s) | Journal ID: CODEN: BICHA |
| Resource Type | Journal Article |
| Resource Relation | Journal Name: Biochemistry; (United States); Journal Volume: 4 |
| Research Org | Washington Univ. School of Medicine, St. Louis, MO |
| Subject | 59 BASIC BIOLOGICAL SCIENCES; CARBOXYLIC ACIDS; BIOCHEMICAL REACTION KINETICS; PROTEINS; ACYLATION; LABELLING; ACETATES; ANIMAL CELLS; COVALENCE; MICE; MUSCLES; TRACER TECHNIQUES; TRITIUM COMPOUNDS; TUMOR CELLS; ANIMALS; CARBOXYLIC ACID SALTS; CHEMICAL REACTIONS; ISOTOPE APPLICATIONS; KINETICS; LABELLED COMPOUNDS; MAMMALS; ORGANIC ACIDS; ORGANIC COMPOUNDS; REACTION KINETICS; RODENTS; VERTEBRATES |
| Description/Abstract | A number of cellular proteins contain covalently bound fatty acids. Previous studies have identified myristic acid and palmitic acid covalently linked to protein, the former usually attached to proteins by an amide linkage and the latter by ester or thio ester linkages. While in a few instances specific proteins have been isolated from cells and their fatty acid composition has been determined, the most frequent approach to the identification of protein-linked fatty acids is to biosynthetically label proteins with fatty acids added to intact cells. This procedure introduces possible bias in that only a selected fraction of proteins may be labeled, and it is not known whether the radioactive fatty acid linked to the protein is identical with that which is attached to the protein when the fatty acid is derived from endogenous sources. We have examined the distribution of protein-bound fatty acid following labeling with (/sup 3/H)acetate, a general precursor of all fatty acids, using BC/sup 3/H1 cells (a mouse muscle cell line) and A431 cells (a human epidermoid carcinoma). Myristate, palmitate, and stearate account for essentially all of the fatty acids linked to protein following labeling with (/sup 3/H)acetate, but at least 30% of the protein-bound palmitate in these cells was present in amide linkage. In BC3H1 cells, exogenous palmitate becomes covalently bound to protein such that less than 10% of the fatty acid is present in amide linkage. These data are compatible with multiple protein acylating activities specific for acceptor protein fatty acid chain length and linkage. |
| Country of Publication | United States |
| Language | English |
| Format | Medium: X; Size: Pages: 878-884 |
| System Entry Date | 2009 Dec 16 |
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