Arterial chondroitin sulfate proteoglycan: localization with a monoclonal antibody
| Autor: | Thomas N. Wight, Tet-Kin Yeo, Henderson Mar, M. W. Lark, Stephanie Lara, I. Hellstrom, K.-E. Hellstrom |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Histology
Immunoelectron microscopy Fluorescent Antibody Technique Matrix (biology) Muscle Smooth Vascular Extracellular matrix Immunoenzyme Techniques chemistry.chemical_compound Interstitial matrix Animals Chondroitin sulfate Cells Cultured Hybridomas biology Antibodies Monoclonal Immunogold labelling Molecular biology Immunohistochemistry Precipitin Tests Extracellular Matrix Microscopy Electron Biochemistry chemistry Proteoglycan Chondroitin Sulfate Proteoglycans Chondroitin sulfate proteoglycan biology.protein Chromatography Gel Cattle Proteoglycans Anatomy Macaca nemestrina |
| Zdroj: | The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society. 36(10) |
| ISSN: | 0022-1554 |
| Popis: | We generated a monoclonal antibody (Mab) against a large chondroitin sulfate proteoglycan (CSPG) isolated from bovine aorta. This Mab (941) immunoprecipitates a CSPG synthesized by cultured monkey arterial smooth muscle cells. The immunoprecipitated CSPG is totally susceptible to chondroitinase ABC digestion and possesses a core glycoprotein of Mr approximately 400-500 KD. By use of immunofluorescence light microscopy and immunogold electron microscopy, the PG recognized by this Mab was shown to be deposited in the extracellular matrix of monkey arterial smooth muscle cell cultures in clusters which were not part of other fibrous matrix components and not associated with the cell's plasma membrane. With similar immunolocalization techniques, the CSPG antigen was found enriched in the intima and present in the medial portions of normal blood vessels, as well as in the interstitial matrix of thickened intimal lesions of atherosclerotic vessels. Immunoelectron microscopy revealed that this CSPG was confined principally to the space within the extracellular matrix not occupied by other matrix components, such as collagen and elastic fibers. These results indicate that this particular proteoglycan has a specific but restricted distribution in the extracellular matrix of arterial tissue. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|