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Absence of apolipoprotein B-48 in the chick, Gallus domesticus - PubMed

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  • PMID: 2341807

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Absence of apolipoprotein B-48 in the chick, Gallus domesticus

P Tarugi et al. J Lipid Res. 1990 Mar.

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Abstract

This study was designed to investigate: a) whether multiple forms of apoB are present in chick plasma lipoproteins; and b) which forms of apoB are produced in vitro by liver and intestine at various stages of pre- and post-natal development. Plasma lipoproteins of d less than 1.019 g/ml, isolated from fasted and nonfasted chicks, contained exclusively the high molecular weight apoB form (apoB-100) that comigrated with human and rat apoB-100 on SDS-PAGE gel. No apoB-48 was detected either in overloaded Coomassie blue-stained gels or after immunoblotting. ApoB-100 but no apoB-48 was found in portomicrons, the triglyceride-rich lipoproteins equivalent to chylomicrons, that in the chick are transported via the porto-mesenteric venous system. To ascertain whether a minute amount of apoB-48 was present in chick plasma, [35S]methionine was injected intraduodenally and the 35S-labeled d less than 1.019 g/ml plasma lipoproteins were isolated 45 min later from the systemic and the porto-mesenteric circulation. Only apoB-100 was found to be labeled in these lipoproteins. Cholesterol feeding did not induce the appearance of apoB-48 in plasma despite a marked accumulation of cholesterol-rich d less than 1.040 g/ml lipoproteins in the plasma. In vitro synthesis of apoB forms was studied in liver and intestinal slices isolated from chick embryos (8 and 5 days before hatching), newly hatched chicks (2 and 7 days after hatching), and young chicks (21 days old) that were incubated in the presence of [35S]methionine. At each stage of development, liver slices secreted predominantly apoB-100. Intestinal slices of newly hatched and young chicks secreted two forms of apoB: apoB-100 and an additional form with an electrophoretic mobility similar to rat plasma apoB-95. No apoB-48 was synthesized or secreted by the intestine. Our results indicate that the absence of apoB-48 in chick plasma reflects the lack of synthesis of this peptide in the intestine. It is conceivable that in chick intestine the recently described molecular mechanism responsible for the co/posttranscriptional modification of apoB mRNA leading to the formation of apoB-48 is lacking or defective.

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