The Long and the Short Isoform of Cell-CAM 105 Show Variant-Specific Modifications in Adult Rat Organs

Baum, Oliver; Troll, S; Hixson, Douglas C.

doi:10.1006/bbrc.1996.1584

Cited by 8 publications

(4 citation statements)

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“…The phosphorylation sites in C‐CAM‐S have not, until now, been identified. In all C‐CAM expressing cells analyzed so far, C‐CAM‐L and C‐CAM‐S are co‐expressed [26], a fact which complicates a detailed biochemical analysis, as the two isoforms are difficult to separate. In this investigation we therefore analyzed transfected CHO cells expressing only the C‐CAM‐S isoform.…”

Section: Resultsmentioning

confidence: 99%

Characterization of protein kinase C‐mediated phosphorylation of the short cytoplasmic domain isoform of C‐CAM

et al. 1998

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C-CAM is a ubiquitously expressed cell adhesion molecule belonging to the carcinoembryonic antigen family. Two co-expressed isoforms, C-CAM-L and C-CAM-S, are known, having different cytoplasmic domains both of which can be phosphorylated in vivo. Here we have characterized the PKCmediated phosphorylation of the short cytoplasmic domain isoform, C-CAM-S. Phorbol myristyl acetate induced phosphorylation of C-CAM-S in transfected CHO cells. Using synthetic peptides and Edman degradation we identified Ser RRW as the PKC-phosphorylated amino acid residue. Binding experiments with modified peptides indicated that this phosphorylation decreases the ability of the cytoplasmic domain of C-CAM-S to bind calmodulin.z 1998 Federation of European Biochemical Societies.

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Section: Resultsmentioning

confidence: 99%

Characterization of protein kinase C‐mediated phosphorylation of the short cytoplasmic domain isoform of C‐CAM

et al. 1998

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“…In most tissues and cells there is a simultaneous expression of C-CAM-L and C-CAM-S [66], and regulation of the L:S ratios as a means of regulating signal transduction by C-CAM is an intriguing possibility. Support for this idea comes from the finding that the expression levels of the two isoforms can indeed be regulated independently of each other in an epithelial rat cell line, NBT-II [67].…”

Section: Inhibition Of Tumor Growth By C-camsmentioning

confidence: 99%

CEA adhesion molecules: multifunctional proteins with signal-regulatory properties

Öbrink

1997

Current Opinion in Cell Biology

253

260

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The carcinoembryonic antigen family comprises a large number of complex molecules, several of which possess cell adhesion activities. The primordial adhesion molecules of this family are the cell-cell adhesion molecules (C-CAMs), which have been found to be multifunctional, signal-regulatory proteins. C-CAMs inhibit tumor growth, interact with calmodulin, protein tyrosine kinases and protein tyrosine phosphatases, and are subject to specific dimerization reactions. These new insights indicate that C-CAMs are important regulators of cellular functions.

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“…In many CEACAM1-expressing cell types, which have been analyzed in depth, it has been found that CEACAM1-L and CEACAM1-S are coexpressed, although at varying ratios (7,20). It has also been demonstrated that both the L and the S isoform can form dimers (21), which is believed to play an important role in the signal-regulating activities of CEACAM1 (4,19).…”

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confidence: 99%

Carcinoembryonic Antigen-Related Cell Adhesion Molecule 1 Expression and Signaling in Human, Mouse, and Rat Leukocytes: Evidence for Replacement of the Short Cytoplasmic Domain Isoform by Glycosylphosphatidylinositol-Linked Proteins in Human Leukocytes

Singer

Scheffrahn

Heymann

et al. 2002

The Journal of Immunology

110

103

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Carcinoembryonic Ag-related cell adhesion molecule 1 (CEACAM1), the primordial carcinoembryonic Ag gene family member, is a transmembrane cell adhesion molecule expressed in leukocytes, epithelia, and blood vessel endothelia in humans and rodents. As a result of differential splicing, CEACAM1 occurs as several isoforms, the two major ones being CEACAM1-L and CEACAM1-S, that have long (L) or short (S) cytoplasmic domains, respectively. The L:S expression ratios vary in different cells and tissues. In addition to CEACAM1, human but not rodent cells express GPI-linked CEACAM members (CEACAM5–CEACAM8). We compared the expression patterns of CEACAM1-L, CEACAM1-S, CEACAM6, and CEACAM8 in purified populations of neutrophilic granulocytes, B lymphocytes, and T lymphocytes from rats, mice, and humans. Human granulocytes expressed CEACAM1, CEACAM6, and CEACAM8, whereas human B lymphocytes and T lymphocytes expressed only CEACAM1 and CEACAM6. Whereas granulocytes, B cells, and T cells from mice and rats expressed both CEACAM1-L and CEACAM1-S in ratios of 2.2–2.9:1, CEACAM1-S expression was totally lacking in human granulocytes, B cells, and T cells. Human leukocytes only expressed the L isoforms of CEACAM1. This suggests that the GPI-linked CEACAM members have functionally replaced CEACAM1-S in human leukocytes. Support for the replacement hypothesis was obtained from experiments in which the extracellular signal-regulated kinases (Erk)1/2 were activated by anti-CEACAM Abs. Thus, Abs against CEACAM1 activated Erk1/2 in rat granulocytes, but not in human granulocytes. Erk1/2 in human granulocytes could, however, be activated by Abs against CEACAM8. We demonstrated that CEACAM1 and CEACAM8 are physically associated in human granulocytes. The CEACAM1/CEACAM8 complex in human cells might accordingly play a similar role as CEACAM1-L/CEACAM1-S dimers known to occur in rat cells.

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The Long and the Short Isoform of Cell-CAM 105 Show Variant-Specific Modifications in Adult Rat Organs

Cited by 8 publications

References 0 publications

Characterization of protein kinase C‐mediated phosphorylation of the short cytoplasmic domain isoform of C‐CAM

Characterization of protein kinase C‐mediated phosphorylation of the short cytoplasmic domain isoform of C‐CAM

CEA adhesion molecules: multifunctional proteins with signal-regulatory properties

Carcinoembryonic Antigen-Related Cell Adhesion Molecule 1 Expression and Signaling in Human, Mouse, and Rat Leukocytes: Evidence for Replacement of the Short Cytoplasmic Domain Isoform by Glycosylphosphatidylinositol-Linked Proteins in Human Leukocytes

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