Nickel Inhibits Binding of 2-Macroglobulin-Methylamine to the Low-Density Lipoprotein Receptor-Related Protein/
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- 作者：Audrey R. Odom ; Uma K. Misra ; and Salvatore V. Pizzo
- 刊名：Biochemistry
- 出版年：1997
- 出版时间：October 14, 1997
- 年：1997
- 卷：36
- 期：41
- 页码：12395 - 12399
- 全文大小：138K
- 年卷期：v.36,no.41(October 14, 1997)
- ISSN：1520-4995
文摘
A previous study demonstrated that activated
2-macroglobulin (2M*) binding to thelow-density receptor-related protein/2-macroglobulin receptor(LRP/2MR) is blocked by Ni2+[Hussain, M.M., et al. (1995) Biochemistry 34,16074-16081]. We now report that the effect ofNi2+ is on a regionof the 2M molecule upstream of the carboxyl terminalreceptor recognition domain. This observationis consistent with previous observations from this laboratorysuggesting that 2M* binding toLRP/2MRinvolves a region of the 2M molecule immediatelyupstream of the receptor recognition domain [Enghild,J. J., et al. (1989) Biochemistry 28,1406-1412]. We further demonstrate that Ni2+ hasno effect on thebinding of 2M* or a cloned and expressed receptorbinding fragment (RBF) to the recently described2M signaling receptor as assessed by direct binding andsignal transduction studies.
2-macroglobulin (2M*) binding to thelow-density receptor-related protein/2-macroglobulin receptor(LRP/2MR) is blocked by Ni2+[Hussain, M.M., et al. (1995) Biochemistry 34,16074-16081]. We now report that the effect ofNi2+ is on a regionof the 2M molecule upstream of the carboxyl terminalreceptor recognition domain. This observationis consistent with previous observations from this laboratorysuggesting that 2M* binding toLRP/2MRinvolves a region of the 2M molecule immediatelyupstream of the receptor recognition domain [Enghild,J. J., et al. (1989) Biochemistry 28,1406-1412]. We further demonstrate that Ni2+ hasno effect on thebinding of 2M* or a cloned and expressed receptorbinding fragment (RBF) to the recently described2M signaling receptor as assessed by direct binding andsignal transduction studies.