Endocytosis of Candida albicans by vascular endothelial cells is associated with tyrosine phosphorylation of specific host cell proteins
Open accessAbstract
Candida albicans escapes from the bloodstream by invading the endothelial cell lining of the vasculature. In vitro, C. albicans invades endothelial cells by inducing its own endocytosis. We examined whether this process is regulated by the tyrosine phosphorylation of endothelial cell proteins. We found that endocytosis of wild-type C. albicans was accompanied by the tyrosine phosphorylation of two endothelial cell proteins with molecular masses of 80 and 82 kDa. The phosphorylation of these proteins was closely associated with the endocytosis of C. albicans because these proteins were phosphorylated in response to the endocytosis of both live and killed organisms, but they were not phosphorylated in endothelial cells infected with a poorly endocytosed strain of C. albicans. The tyrosine kinase inhibitors genistein and tyrphostin 47 blocked the phosphorylation of the two endothelial cell proteins and significantly reduced endocytosis of C. albicans. Therefore, C. albicans probably induces its own endocytosis by stimulating the tyrosine phosphorylation of two endothelial cell proteins.
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Endothelial cell endocytosis of C. albicans is dependent on extracellular calcium and is governed at least in part by the tyrosine phosphorylation of endothelial cell proteins.
“Endothelial cell endocytosis of C. albicans is dependent on extracellular calcium and is governed at least in part by the tyrosine phosphorylation of endothelial cell proteins [9,11].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [11]
The Discussion reports that tyrosine kinase inhibitors reduced endothelial uptake of C. albicans and concludes that phosphorylation of at least one endothelial protein is likely required for endocytosis. That supports the claim’s qualified phosphorylation component. Neither the supplied passages nor searches for extracellular calcium and related terms establish that endocytosis depends on extracellular calcium. (LLM, conf=0.88)
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- Authors
- Belanger, P. H., Johnston, D. A., Fratti, R. A., Zhang, M., & G. Filler, S.
- Affiliations
- University of California, Los Angeles (US)
- University of Nevada, Reno (US)
- Venue
- Cellular Microbiology
- Publisher
- Hindawi Limited
- Published
- 2002-12
- Volume
- 4
- Issue
- 12
- Pages
- 805-812
- ISSN
- 1462-5814 (ISSN-L)
- 1462-5822
- OpenAlex
- W2030447042
- Cited by
- 34
- References
- 38
- Citations by year
- 2026: 1 · 2023: 1 · 2020: 2 · 2018: 1 · 2017: 2 · 2015: 1 · 2014: 2 · 2013: 2
- FWCI
- 1.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cellular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Burroughs Wellcome Fund
- American Heart Association
- National Institutes of Health (R01 AI19990, RR00425)
- National Institute of Allergy and Infectious Diseases (P01 AI-37194, R29AI040636, R01AI019990, R01-AI19990, P01AI037194)
- National Center for Research Resources (M01RR000425, M01-RR00425)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- Candida albicans, endocytosis, vascular endothelial cells, tyrosine phosphorylation, host cell proteins, tyrosine kinase inhibitors, genistein, fungal virulence, host-pathogen interaction
- MeSH terms
- Bacterial Adhesion, Candida albicans, Cells, Cultured, Endocytosis, Endothelium, Vascular, Enzyme Inhibitors, Humans, Phosphorylation, Protein-Tyrosine Kinases, Proteins, Tyrosine, Genistein, Tyrphostins
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