Sorting of an apical plasma membrane glycoprotein occurs before it reaches the cell surface in cultured epithelial cells.
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In Madin-Darby canine kidney (MDCK) cells (a polarized epithelial cell line) infected with influenza virus, the hemagglutinin behaves as an apical plasma membrane glycoprotein. To determine biochemically the domain on the plasma membrane, apical or basolateral, where newly synthesized hemagglutinin first appears, cells were cultured on Millipore filters to make both cell surface domains independently accessible. Hemagglutinin in virus-infected cells was pulse-labeled, chased, and detected on the plasma membrane with a sensitive trypsin assay. Under all conditions tested, newly made hemagglutinin appeared simultaneously on both domains, with the bulk found in the apical membrane. When trypsin was continuously present on the basolateral surface during the chase, little hemagglutinin was cleaved relative to the amount transported apically. In addition, specific antibodies against the hemagglutinin placed basolaterally had no effect on transport to the apical domain. These observations suggested that most newly synthesized hemagglutinin does not transiently appear on the basolateral surface but rather is delivered directly to the apical surface in amounts that account for its final polarized distribution.
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The sorting and transport of materials that occur in neurons must be considerably more sophisticated than that in other polarized cells.
“Thus, the sorting and transport of materials that occur in neurons must be considerably more sophisticated than that in other polarized cells (e.g., Matlin and Simons, 1984).”
From Immunocytochemical localization of tubulin and microtubule-associated protein 2 during the development of hippocampal neurons in culture (1986) · cites this paper as Matlin and Simons, 1984
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- Authors
- Matlin, K. S., & Simons, K.
- ORCID
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1984-12-01
- Volume
- 99
- Issue
- 6
- Pages
- 2131-2139
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2113546
- OpenAlex
- W2124287787
- Cited by
- 253
- References
- 33
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2022: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 1 · 2012: 2
- FWCI
- 9.24
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- hemagglutinin, apical membrane, membrane protein sorting, epithelial polarity, basolateral membrane, influenza, MDCK cells, trypsin accessibility, protein trafficking
- MeSH terms
- Animals, Cell Division, Cell Line, Cell Membrane, Dogs, Epithelial Cells, Epithelium, Glycoproteins, Hemagglutinins, Kidney, Kinetics, Membrane Proteins, Microscopy, Electron, Protein Processing, Post-Translational
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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