Isolation and characterization of a 30 kDa membrane glycoprotein from human stratum corneum |
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| Affiliation: | 1. Department of Dermatology, The University of Texas Medical Branch, Galveston, TX 77550 U.S.A.;2. Department of Pathology, The University of Texas Medical Branch, Galveston, TX 77550 U.S.A.;3. Department of Internal Medicine, The University of Texas Medical Branch, Galveston, TX 77550 U.S.A.;4. Department of Microbiology, The University of Texas Medical Branch, Galveston, TX 77550 U.S.A.;5. Department of Human Biological Chemistry and Genetics, The University of Texas Medical Branch, Galveston, TX 77550 U.S.A.;1. LEPABE - Laboratory for Process Engineering, Environment, Biotechnology and Energy, Faculty of Engineering, University of Porto, Rua Dr. Roberto Frias, 4200-465, Porto, Portugal;2. ALiCE - Associate Laboratory in Chemical Engineering, Faculty of Engineering, University of Porto, Rua Dr. Roberto Frias, 4200-465, Porto, Portugal;1. University of Amsterdam, Biomedical Engineering and Physics, Academic Medical Center, 1105 AZ Amsterdam, The Netherlands;2. Co van Ledden Hulsebosch Center (CLHC), University of Amsterdam, 1098 XH Amsterdam, The Netherlands;1. Department of Environmental Toxicology, University of California - Davis, Davis, CA, United States;2. Department of Biotechnology, Quaid-i-Azam University Islamabad, Pakistan;3. Proteomic Core Facility, Genome Center, University of California - Davis, Davis, CA, United States |
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| Abstract: | Using iodinated concanavalin A in conjunction with gel electrophoresis, we have identified a 30 kDa glycoprotein in the stratum corneum of human skin. We isolated this glycoprotein by extraction in nonionic detergent, affinity chromatography and preparative gel electrophoresis. It binds to concanavalin A but not to three other lectins. The purified glycoprotein migrates at 30 kDa whether or not reducing agents are present. It is rich in histidine and lysine, but lacks arginine, proline, tyrosine and methionine. It is clearly distinct from fillaggrin. We prepared a monospecific polyclonal antibody to this glycoprotein and localized it by immuno-histochemistry exclusively to the cell membrane of corneocytes. We postulate that the glycoprotein may play a role in the cohesion and desquamation of corneocytes. |
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