{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,19]],"date-time":"2026-01-19T08:57:03Z","timestamp":1768813023995,"version":"3.49.0"},"reference-count":36,"publisher":"The Company of Biologists","issue":"4","license":[{"start":{"date-parts":[[1989,4,1]],"date-time":"1989-04-01T00:00:00Z","timestamp":607392000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.biologists.com\/user-licence-1-1\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1989,4,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n               <jats:p>Retinal pigment epithelial cells, derived from human donor eyes, have been grown in culture as monolayers on membrane filters or plastic surfaces and shown to possess transferrin receptors with a monomeric molecular mass of 93000. These receptors internalize 12SI-labelled transferrin and recycle it to the surrounding medium in a similar manner to other cell types. Scatchard analyses show that there are about 100 000 high-affinity receptors on the surface of each cell and most of these receptors are associated with the cytoskeleton. In total cell extracts, there are additional low-affinity binding sites that do not appear to be strongly associated with the cytoskeleton. The apparent interaction of transferrin receptors with the cytoskeleton was confirmed in two ways: first, using 200 kV electron microscopy for stereo analyses, skeleton-associated transferrin receptors were detected by a monoclonal anti-receptor antibody and a colloidal gold-conjugated second antibody after Triton X-100 extraction of pigment epithelial cells grown directly on laminin-coated gold grids; and, second, when cell surface receptors were labelled with radioiodinated transferrin and then incubated for various periods of time, the labelled transferrin was observed to move from a Triton X-100-insoluble fraction (a putative cytoskeletal compartment) to a Triton-soluble compartment that was not associated with the cytoskeleton. Using either horseradish peroxidase or colloidal gold-labelled transferrin, it has been shown that basolateral and apical surface-located receptors participate in receptor-mediated endocytosis via clathrin-coated pits, endosomes and tubular structures. Initially, transferrin internalized from the apical surface is observed in small endosomes that often appear to be embedded in an apical layer of microfilaments. From these peripheral regions of the cells, the labelled receptors move to larger endosomes and multivesicular bodies deeper in the cytoplasm. These structures have no apparent association with cytoskeletal elements.<\/jats:p>","DOI":"10.1242\/jcs.92.4.655","type":"journal-article","created":{"date-parts":[[2021,4,26]],"date-time":"2021-04-26T21:27:28Z","timestamp":1619472448000},"page":"655-666","source":"Crossref","is-referenced-by-count":41,"title":["Transferrin receptors on the surfaces of retinal pigment epithelial cells are associated with the cytoskeleton"],"prefix":"10.1242","volume":"92","author":[{"given":"Richard C.","family":"Hunt","sequence":"first","affiliation":[{"name":"Departments of Microbiology and Ophthalmology, University of South Carolina Medical School, Columbia, SC 29208, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Art","family":"Dewey","sequence":"additional","affiliation":[{"name":"Departments of Microbiology and Ophthalmology, University of South Carolina Medical School, Columbia, SC 29208, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alberta A.","family":"Davis","sequence":"additional","affiliation":[{"name":"Departments of Microbiology and Ophthalmology, University of South Carolina Medical School, Columbia, SC 29208, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"237","published-online":{"date-parts":[[1989,4,1]]},"reference":[{"key":"2023071212445341800_JOCES_92_4_655C1","first-page":"136","article-title":"Retinoids in Photosensitive Systems","volume":"2","author":"Bridges","year":"1984","journal-title":"The Retinoids"},{"key":"2023071212445341800_JOCES_92_4_655C2","first-page":"C96","article-title":"Occluding junctions in cultured epthelial monolayers","volume":"9","author":"Cereuido","year":"1980","journal-title":"Am. J. Physiol."},{"key":"2023071212445341800_JOCES_92_4_655C3","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/B978-0-12-044276-8.50009-6","article-title":"The Cell Biology of the Retinal Pigment Epithelium","volume":"2","author":"Clark","year":"1986","journal-title":"The Retina - A Model for Cell Biology Studies,"},{"key":"2023071212445341800_JOCES_92_4_655C4","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/0006-8993(86)90576-7","article-title":"The distribution of transferrin immunoreactivity in the rat central nervous system","volume":"368","author":"Connor","year":"1986","journal-title":"Brain Res."},{"key":"2023071212445341800_JOCES_92_4_655C5","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1007\/BF02620947","article-title":"Location and possible function of fibronectin and laminin in clones of chick retinal pigmented epithelial cells","volume":"21","author":"Crawford","year":"1985","journal-title":"In Vitro cell, devl Biol."},{"key":"2023071212445341800_JOCES_92_4_655C6","doi-asserted-by":"crossref","first-page":"2258","DOI":"10.1073\/pnas.80.8.2258","article-title":"pH and the recycling of transferrin during receptor-mediated endocytosis","volume":"80","author":"Dautry-Varsat","year":"1983","journal-title":"Proc. natn. Acad. Sci. U.SA."},{"key":"2023071212445341800_JOCES_92_4_655C7","doi-asserted-by":"crossref","first-page":"15 368","DOI":"10.1016\/S0021-9258(18)66719-5","article-title":"Selective externalisation of an ATP-binding protein structurally related to the clathrin uncoating ATPase\/heat shock protein in vesicles containing terminal transferrin receptors during reticulocyte maturation. J","volume":"261","author":"Davis","year":"1986","journal-title":"biol. Chem."},{"key":"2023071212445341800_JOCES_92_4_655C8","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1002\/j.1939-4640.1986.tb00945.x","article-title":"Transferrin-mediated transcellular transport of 19Fe across confluent epithelial sheets of sertoli cells grown in bicameral cell culture chambers","volume":"7","author":"Djakiew","year":"1986","journal-title":"J. Androl."},{"key":"2023071212445341800_JOCES_92_4_655C9","first-page":"294a","article-title":"Transepithelial transport of retinol by monolayers of human RPE in vitro","volume":"27","author":"Flannery","year":"1986","journal-title":"Invest. Ophthal."},{"key":"2023071212445341800_JOCES_92_4_655C10","doi-asserted-by":"crossref","first-page":"1767","DOI":"10.1083\/jcb.103.5.1767","article-title":"Transferrin receptor polarity and recycling accuracy in \u201ctight\u201d and \u201cleaky\u201d strains of Madin-Darby canine kidney cells","volume":"103","author":"Fuller","year":"1986","journal-title":"J. Cell Biol."},{"key":"2023071212445341800_JOCES_92_4_655C11","doi-asserted-by":"crossref","first-page":"1938","DOI":"10.1172\/JCI105068","article-title":"The selectivity of the human placenta in the transfer of plasma proteins from mother to fetus. J","volume":"43","author":"Gitlin","year":"1964","journal-title":"clin. Invest."},{"key":"2023071212445341800_JOCES_92_4_655C12","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1177\/14.4.291","article-title":"The early stages of absorption of injected horse radish peroxidase in the proximal tubules of mouse kidney: ultrastructural cytochemistry by a new technique","volume":"14","author":"Graham","year":"1966","journal-title":"J. Histochem. Cytochem."},{"key":"2023071212445341800_JOCES_92_4_655C13","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1007\/978-1-4615-6904-6_5","article-title":"Transferrin: receptor-mediated endocytosis and iron delivery","volume-title":"Endocytosis","author":"Hanover","year":"1985"},{"issue":"Suppl","key":"2023071212445341800_JOCES_92_4_655C14","first-page":"286","article-title":"Evidence for a mannose-sensitive receptor involved in RPE phagocytosis","volume":"25","author":"Heth","year":"1984","journal-title":"Invest. 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