CHARACTERIZATION OF RECOMBINANT HUMAN INTERLEUKIN-4 RECEPTOR FROM CHO CELLS - ROLE OF N-LINKED OLIGOSACCHARIDES

被引：20

作者：

RAJAN, N ^{[1
]}

TSARBOPOULOS, A ^{[1
]}

KUMARASAMY, R ^{[1
]}

ODONNELL, R ^{[1
]}

TAREMI, SS ^{[1
]}

BALDWIN, SW ^{[1
]}

SEELIG, GF ^{[1
]}

FAN, XD ^{[1
]}

PRAMANIK, B ^{[1
]}

LE, HV ^{[1
]}

机构：

[1] SCHERING PLOUGH CORP,KENILWORTH,NJ 07033

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 206卷 / 02期

关键词：

D O I：

10.1006/bbrc.1995.1098

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：

Interleukin 4 (IL-4) mediates its biological activities through interaction with its receptor on the cell surface. A recombinant extracellular domain of the alpha subunit of human interleukin 4 receptor was expressed in CHO cells and purified to homogeneity by a combination of ion exchange and immunoaffinity chromatography. Analysis of the purified protein by MALDI MS provided an average mass of 38,241 Da while microsequencing identified the site of the signal sequence processing to be SeT23-G1Y(24) The receptor was highly glycosylated,containing N-linked complex oligosaccharides with bi-, tri-, and tetraantennary structures. Five of the six potential glycosylation sites could be assigned to Asn residues 53, 98, 128, 134 and 176. N-deglycosylation increased aggregation and reduced solubility of the receptor but did not affect its IL-4 binding activity. These observations provide preliminary insights into the role of N-linked oligosaccharides in IL-4 receptor biosynthesis and function at the cell surface. (C) 1995 Academic Press, Inc.

引用

页码：694 / 702

页数：9

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