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Mass Spectrometric Analysis of Glycosphingolipid Antigens
Published on: April 16, 2013
Biochemical analysis of a 130,000 molecular weight glycoprotein on human melanoma cells
Abstract:
A monomeric sialoglycoprotein of 130,000 molecular weight (gp 130) is a membrane protein detected by mouse monoclonal antibodies on human melanoma cells and in lesser amounts on a wide range of normal and malignant cell types. Eight monoclonal antibodies reacting with gp 130 detect at least four spatially distinct epitopes on the exposed surface of the gp 130 molecule. Biosynthetic studies have shown that gp 130 is synthesized through two precursor forms: a 100 kD glycosylated species and an 80 kD unglycosylated species, presumably the primary translational product of the encoding mRNA.
Insights
Researchers identified a 130,000 molecular weight sialoglycoprotein (gp 130) on melanoma cells. This membrane protein, detected by monoclonal antibodies, also appears on other cell types and has distinct surface epitopes.
Area of Science:
- Biochemistry
- Cell Biology
- Immunology
Background:
- A monomeric sialoglycoprotein, gp 130 (130,000 molecular weight), is a cell surface membrane protein.
- gp 130 is detected on human melanoma cells and various normal and malignant cell types.
Purpose of the Study:
- To characterize the gp 130 molecule and its epitopes.
- To investigate the biosynthesis of gp 130.
Main Methods:
- Utilized mouse monoclonal antibodies to detect and characterize gp 130.
- Performed biosynthetic studies to analyze gp 130 precursor forms.
Main Results:
- Eight monoclonal antibodies identified at least four distinct surface epitopes on gp 130.
- Biosynthetic studies revealed two precursor forms: a 100 kD glycosylated species and an 80 kD unglycosylated species.
Conclusions:
- gp 130 is a cell surface sialoglycoprotein with multiple distinct epitopes.
- gp 130 is synthesized via precursor forms, suggesting complex post-translational modifications.
