ArticleThe Biochemical journal1994
Identification of a keratin-associated protein that localizes to a membrane compartment.
Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 19 citations in OpenAlex.
- Keratin 8 phosphorylation regulates keratin reorganization and migration of epithelial tumor cells.Journal of cell science · 2012Article
- Seven kinds of intermediate filament networks in the cytoplasm of polarized cells: structure and function.Acta histochemica et cytochemica · 2010Article
- Keratin 20 expressed in the endocrine and exocrine cells of the rabbit duodenum.Acta histochemica et cytochemica · 2007Article
- Identification of novel principles of keratin filament network turnover in living cells.Molecular biology of the cell · 2004Article
- 14-3-3 proteins associate with phosphorylated simple epithelial keratins during cell cycle progression and act as a solubility cofactor.The Journal of cell biology · 1996Article
- Dynamics of human keratin 18 phosphorylation: polarized distribution of phosphorylated keratins in simple epithelial tissues.The Journal of cell biology · 1995Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We describe the characterization of an acidic glycoprotein (molecular mass approximately 85 kDa) that associates with keratin intermediate filaments of 'simple'-type epithelia. Using a number of anti-keratin monoclonal antibodies, the 85 kDa glycoprotein was identified by co-immunoprecipitation with keratin polypeptides 8 and 18 (K8/18) from the human colonic epithelial cell line HT29 and several other epithelial cell lines. This Keratin-Associated Protein (termed KAP85) was readily detected after in vitro galactosylation of K8/18 immunoprecipitates obtained from mitosis-arrested cells. Its solubilization and detection were dependent on the detergent used, and it was barely detected after in vitro galactosylation of asynchronously growing G0/G1-phase cells. Its poor in vitro galactosylation in G0/G1-phase cells is likely a reflection of the lack of available terminal N-acetylglucosamine residues, since it can be labelled to a similar extent in G0/G1- and G2/M-phase cells using NaIO4/NaB3H4. Glycosidase digestion showed that KAP85 contains high mannose and complex oligosaccharides. Fractionation of total cellular K8/18 into soluble and cytoskeletal insoluble pools showed that KAP85 associates exclusively with the cytoskeletal K8/18 pool. Subcellular fractionation showed that KAP85 co-localizes with a plasma-membrane-enriched fraction that includes the transferrin receptor and KS-1 antigen. Our results demonstrate in vitro evidence of a membrane-associated glycoprotein (KAP85) which may serve as an attachment site for filamentous K8/18.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.