Chick skin slices were incubated with [35S]methionine and labeled apoA-I was immunoprecipitated from incubation medium and tissue homogenate. ApoA-I accounted for approximately 13 and 2.5% of radioactive medium and cell proteins, respectively. After ultracentrifugation of the medium, 55% of labeled apoA-I was found as a constituent of lipoproteins (d less than 1.210 g/ml) and 45% in a lipid-poor form (1.210-1.260 g/ml). To ascertain whether this large proportion of lipid-poor apoA-I was due to a dissociation of this peptide from medium lipoproteins during ultracentrifugation, labeled incubation medium was applied to an anti-chick apoA-I immunoaffinity column. The material bound to the column was analyzed by nondenaturing polyacrylamide gradient gel electrophoresis and found to contain three subpopulations of lipoproteins with a particle size of 12, 11, and 9 nm, respectively. The radioactivity of these subpopulations accounted for 82% of total radioactive medium apoA-I. ApoA-I was localized by immunohistochemistry in the viable cells of the epidermis and in the stratum corneum. Rat skin slices were found to synthesize and secrete apoE but no apoA-I. ApoA-I and apoE secreted by chick and rat skin, respectively, may play a role in the secretion of lipids from the differentiating keratinocytes and thus contribute to the formation of the hydrophobic barrier of the skin.
|Data di pubblicazione:||1991|
|Titolo:||Synthesis and secretion of apolipoprotein A-I by chick skin.|
|Autore/i:||Tarugi P; Albertazzi L; Nicolini S; Ottaviani E; Calandra S.|
|Codice identificativo ISI:||WOS:A1991FJ34200063|
|Codice identificativo Scopus:||2-s2.0-0025821268|
|Citazione:||Synthesis and secretion of apolipoprotein A-I by chick skin. / Tarugi P; Albertazzi L; Nicolini S; Ottaviani E; Calandra S.. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - STAMPA. - 266(1991), pp. 7714-7720.|
|Tipologia||Articolo su rivista|
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