Molecular cloning and biochemical characterization of a truncated, secreted member of the human family of Ca2+-activated Cl- channels'

被引:56
作者
Gruber, AD [1 ]
Pauli, BU [1 ]
机构
[1] Cornell Univ, Coll Vet Med, Canc Biol Labs, Dept Mol Med, Ithaca, NY 14853 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 1999年 / 1444卷 / 03期
关键词
trachea; molecular cloning; protein chemistry; chloride channel; (human spleen);
D O I
10.1016/S0167-4781(99)00008-1
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
A novel family of chloride channel proteins has recently been discovered including two bovine (Lu-ECAM-1, bCLCA1), one murine (mCLCA1), and two human (hCLCA1 and hCLCA2) members. Here, we describe the cloning, expression, and molecular characterization of a truncated human homolog, tentatively named hCLCA3. It was cloned from a human spleen cDNA library and is expressed in numerous tissues including lung, trachea, spleen, thymus, and mammary gland as determined by reverse transcriptase-polymerase chain reaction. Unlike all previously known CLCA family members which consistently encode an approximately 125-kDa transmembrane protein that is cleaved to form a heterodimer of two proteins of approximately 90 and 35 kDa, the 3.6-kb hCLCA3 mRNA encodes a 37-kDa glycoprotein that corresponds to the N-terminal extracellular domain of its homologs. Moreover, when expressed in human embryonic kidney 293 or Chinese hamster ovary cells, this 37-kDa glycoprotein is secreted into the culture supernatant. These observations suggest that hCLCA3 is a structurally divergent member of the CLCA family of proteins and that it does not act as a channel protein but has distinct, yet unidentified functions. (C) 1999 Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:418 / 423
页数:6
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