LDL receptors in coated vesicles isolated from bovine adrenal cortex: Binding sites unmasked by detergent treatment

Mello, Robert J.; Brown, Michael S.; Goldstein, Joseph L.; Anderson, Richard G. W.

doi:10.1016/0092-8674(80)90329-3

Cited by 58 publications

(28 citation statements)

References 22 publications

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“…More recently, and consistent with their putative role in intracellular transport, coated vesicles isolated from bovine adrenal cortex, human placenta, and rat liver have been shown to contain receptors specific for low density lipoproteins (13), transferrin (12), and insulin (23), respectively. The present study was undertaken in an attempt to ascertain whether the specific hepatic receptor for asialoglycoproteins (9,24) was detectable in highly purified coated vesicles from rat liver and, if so, to determine its topological orientation within the vesicle.…”

mentioning

confidence: 84%

“…Since then, similar, if not identical appearing structures were isolated from a number of tissue sources (12)(13)(14)(15)(16)(17). All these preparations have a common and distinguishing feature in the remarkable surface lattice of rod-like molecules which surround a lipid-protein bilayer and appear to be organized in a defined network of pentagons and hexagons…”

mentioning

confidence: 99%

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Evidence For the Presence of the Asialoglycoprotein Receptor in Coated Vesicles Isolated from Rat Liver

Steer

Wall²,

Ashwell³

1983

Hepatology

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Coated vesicles were isolated from rat liver by a modification of the procedure described by Nandi et al. for bovine brain (Proc. Natl. Acad. Sci. U.S.A. 1982; 79:5881-5885). The hepatic receptor for asialoglycoproteins was shown to be an integral constitutent of these vesicles as evidenced by their ability to bind 12sI-asialo-orosomucoid in a specific and saturable manner. The specific binding activity of the purified vesicles was 17-fold greater than that of the original liver homogenate based on a protein determination. Binding was 97% latent and was made fully manifest only after removal of the clathrin coat and disruption of the exposed smooth membrane vesicles by detergent. Based on this finding, it was concluded that the binding protein for asialoglycoproteins was oriented toward the inner surface of the vesicle. In addition, evidence is presented that purification procedures employing detergent may result in coated vesicles deficient in one or more integral membrane proteins.

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mentioning

confidence: 84%

mentioning

confidence: 99%

Evidence For the Presence of the Asialoglycoprotein Receptor in Coated Vesicles Isolated from Rat Liver

Steer

Wall²,

Ashwell³

1983

Hepatology

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“…108, 140,172). The first step in their isolation therefore usually involves the removal of endo-and plasma membranes by centrifuging the (filtered) homogenate at 20,000-40,000 g for 30-60 min.…”

Section: Methods For Purificationmentioning

confidence: 99%

“…140,228), as well as immunocytochemically in situ with gold-labeled receptor antibodies or ligands (e.g. 107) , by performing ligand-binding assays on isolated CVs (e.g.…”

Section: Glucan Sy Nthasesmentioning

confidence: 99%

Coated Vesicles

Robinson¹,

Depta²

1988

Annu. Rev. Plant. Physiol. Plant. Mol. Biol.

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“…In each case, maximal binding activity was achieved only upon exposure of the vesicle's membrane to various detergents suggesting that the receptor binding sites face the interior of the vesicle. Mello and coworkers (124) reported that the binding of 1251-LDL to coated vesicles isolated from bovine adrenal cortex increased 10-fold upon exposure of the vesicles to the detergent octylglucoside. Electron microscopy revealed that the isolated coated vesicles were uniform, with a mean diameter of 60 nm.…”

Section: Molecular and Biochemical Aspects Of Isolatedmentioning

confidence: 99%