The binding properties of the human receptor for the cellular uptake of vitamin B12

被引:32
|
作者
Quadros, EV
Nakayama, Y
Sequeira, JM
机构
[1] Suny Downstate Med Ctr, Dept Biochem, Brooklyn, NY 11203 USA
[2] Suny Downstate Med Ctr, Dept Med, Brooklyn, NY 11203 USA
关键词
vitamin B-12; cobalamin; transcobalamin; receptor;
D O I
10.1016/j.bbrc.2004.12.103
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cellular uptake of vitamin B-12 (cobalamin, Cbl) is mediated by a receptor expressed on the plasma membrane that binds transcobalamin (TC) saturated with Cbl and internalizes the TC-Cbl by endocytosis. A few reports have described the characterization of the receptor protein. However, many discrepancies have emerged in the functional and structural properties of the receptor and therefore, the identity and primary structure of this protein remains unconfirmed. In this report, we provide evidence of a 58 kDa monomeric protein as the likely receptor for the uptake of TC-Cbl and that the functional activity is not associated with a 72/144 kDa monomer/dimer with immunoglobulin Fc structural domain that has been purported to be the receptor in a number of publications. (C) 2004 Elsevier Inc. All rights reserved.
引用
收藏
页码:1006 / 1010
页数:5
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