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Construction and Function of Erythrocyte Membrane Protein Band 4.2


Wei-Yan Peng, Xiang Wang*, Wei Gao, Chuan Jiang, Jia-Xin Xie, Yao-Jin Li
Bioengineering College of Chongqing University, Chongqing 400030, China
Abstract: Protein 4.2 is a major erythrocyte membrane skeletal protein which has been immunologically detected in a variety of cell types and is apparently essential for normal erythrocyte membrane function. It is a transglutaminase-like molecule with no enzymatic cross-linking activity. Protein 4.2 associates with the cytoplasmic domain of band 3 and interacts with ankyrin in the erythrocyte membrane. Protein 4.2 is N-myristylated. It is playing an important role in maintaining the integrity and stability of the membrane. Individuals with protein 4.2 deficiency in their erythrocyte membranes exhibit spherocytosis and experience various degrees of hemolytic anemia, which may necessitate a splenectomy. In humans, several point mutations and a frame shift mutation of protein 4.2 are associated with protein 4.2 deficiency in hemolytic anemia. Band 4.2 may serve as an accessory linking protein between the membrane skeleton and the overlying lipid bilayer. This article has reviewed the progress of the research on the construction and the function of protein 4.2.


CSTR: 32200.14.cjcb.2007.05.0013