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An Antiviral Soluble Form of the LDL Receptor Induced by Interferon
Abstract
Interferons, which induce several intracellular antiviral proteins, also induce an extracellular soluble protein that inhibits vesicular stomatitis virus (VSV) infection. This 28-kilodalton soluble protein was purified to homogeneity and identified by protein sequencing as the ligand-binding domain of the human 160-kilodalton low density lipoprotein receptor (LDLR). The existence of an antiviral soluble LDLR was confirmed by immunoaffinity chromatography with monoclonal antibody to LDLR. This soluble receptor mediates most of the interferon-triggered antiviral activity against VSV, apparently by interfering with virus assembly or budding, and not by inhibiting virus attachment to cells.
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LDLR and its family members such as VLDLR, apoER, and LRP1 undergo ectodomain shedding to release soluble forms into extracellular fluids such as cerebrospinal fluid and blood.
“LDLR and its family members such as VLDLR, apoER and LRP1 undergo ectodomain shedding to release their soluble forms into the extracellular milieu such as cerebrospinal fluid and blood12,29,30.”
From Membrane type 1 matrix metalloproteinase promotes LDL receptor shedding and accelerates the development of atherosclerosis (2021) · cites this paper as [12]
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Research works printed but not linked: 34
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Metadata
- Authors
- Fischer, D. G., Tal, N., Novick, D., Barak, S., & Rubinstein, M.
- Venue
- Science
- Published
- 1993-10-08
- Volume
- 262
- Issue
- 5131
- Pages
- 250-253
- ISSN
- 0036-8075
- 1095-9203
- Cited by
- 63
- References
- 0
- Language
- en
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