| Autor: |
Frenette, G P, Ruddon, R W, Krzesicki, R F, Naser, J A, Peters, B P |
| Zdroj: |
Journal of Biological Chemistry; February 1989, Vol. 264 Issue: 6 p3078-3088, 11p |
| Abstrakt: |
The basal lamina components laminin, heparan sulfate proteoglycan (HSPG), and type IV collagen were synthesized and codeposited in the extracellular matrix (ECM) by a cultured human cell line from gestational choriocarcinoma (JAR). Laminin and HSPG formed a noncovalent complex detected by the coimmunoprecipitation of HSPG with laminin from cell lysates and culture media. The complex was stable in the cell lysis buffer that contained detergents (1% Triton X-100, 0.5% deoxycholate, and 0.1% sodium dodecyl sulfate) and sodium chloride (from 0.15 to 1.0 M), but was dissociated by adding 8 M urea to the detergent lysates. Even though JAR cells produced roughly equal amounts of HSPG and chondroitin sulfate proteoglycan, only HSPG complexed with laminin, suggesting a specific interaction between these basal lamina components. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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