Secreted CEACAM1 splice variants in rat cell lines and in vivo in rat serum

被引：17

作者：

Budt, M ^{[1
]}

Michely, B ^{[1
]}

Müller, MM ^{[1
]}

Reutter, W ^{[1
]}

Lucka, L ^{[1
]}

机构：

[1] Free Univ Berlin, Klinikum Benjamin Franklin, Inst Biochem & Mol Biol, D-14195 Berlin, Germany

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2002年 / 292卷 / 03期

关键词：

carcinoembryonic antigen; CEACAM1; alternative splicing; glycoprotein; serum protein; immunoglobulin superfamily;

D O I：

10.1006/bbrc.2002.6704

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：

The widely expressed adhesion receptor CEACAM1 is a member of the carcinoembryonic antigen (CEA) family within the immunoglobulin (Ig) superfamily of glycoproteins. While the expression of transmembrane isoforms has been described in detail, only little is known about soluble isoforms. By RT-PCR characterization of rat pheochromocytoma PC12 and mammary adenocarcinoma MTC cell lines, two novel splice variants, designated CEACAM1-4C1 and CEACAM1-4C2, lacking the transmembrane region, were identified. In addition, we demonstrate the expression of transmembrane CEACAM1-4L and CEACAM1-4S with a truncated cytoplasmic domain. The C-termini of CEACA-M1-4C2 and CEACAM1-L are identical, which allowed the specific in vitro and in vivo detection of the soluble CEACAM1-4C2 protein by an antiserum generated against the CEACAM1-L cytoplasmic part. Functionally, soluble CEACAM1 could inhibit CEACAM1-mediated aggregation of CHO cells. In conclusion, our data define a new mechanism for the appearance of functionally active rat CEACAM1 protein in body fluids. (C) 2002 Elsevier Science (USA).

引用

页码：749 / 755

页数：7

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