The Cell Adhesion Molecule CEACAM1-L Is a Substrate of Caspase-3-mediated Cleavage in Apoptotic Mouse Intestinal Cells

The CEACAM1 cell adhesion molecule is a member of the carcinoembryonic antigen family. In the mouse, four distinct isoforms are generated by alternative splicing. These encode either two or four immunoglobulin domains linked through a transmembrane domain to a cytoplasmic domain that encompasses either a short 10-amino acid tail or a longer one of 73 amino acids. Inclusion of exon 7, well conserved in evolution, generates the long cytoplasmic domain. A potential caspase recognition site in mouse, rat, and human CEACAM1-L also becomes available within the peptide encoded by exon 7. We used CEACAM1-L-transfected mouse colon carcinoma CT51 cells treated with three different apoptotic agents to study its fate during cell death. We found that CEACAM1-L is cleaved resulting in rapid degradation of most of its 8-kDa cytoplasmic domain. Caspase-mediated cleavage was demonstrated using purified recombinant caspases. The long cytoplasmic domain was cleaved specifically by caspase-3 in vitro but not by caspase-7 or -8. Moreover cleavage of CEACAM1-L in apoptotic cells was blocked by addition of a selective caspase-3 inhibitor to the cultures. Using point and deletion mutants, the conserved DQRD motif in the membrane-proximal cytoplasmic domain was identified as a caspase cleavage site. We also show that once CEACAM1-L is caspase-cleaved it becomes a stronger adhesion molecule than both the shorter and the longer expressing isoforms. The CEACAM1 cell adhesion molecule is a member of the carcinoembryonic antigen family. In the mouse, four distinct isoforms are generated by alternative splicing. These encode either two or four immunoglobulin domains linked through a transmembrane domain to a cytoplasmic domain that encompasses either a short 10-amino acid tail or a longer one of 73 amino acids. Inclusion of exon 7, well conserved in evolution, generates the long cytoplasmic domain. A potential caspase recognition site in mouse, rat, and human CEACAM1-L also becomes available within the peptide encoded by exon 7. We used CEACAM1-L-transfected mouse colon carcinoma CT51 cells treated with three different apoptotic agents to study its fate during cell death. We found that CEACAM1-L is cleaved resulting in rapid degradation of most of its 8-kDa cytoplasmic domain. Caspase-mediated cleavage was demonstrated using purified recombinant caspases. The long cytoplasmic domain was cleaved specifically by caspase-3 in vitro but not by caspase-7 or -8. Moreover cleavage of CEACAM1-L in apoptotic cells was blocked by addition of a selective caspase-3 inhibitor to the cultures. Using point and deletion mutants, the conserved DQRD motif in the membrane-proximal cytoplasmic domain was identified as a caspase cleavage site. We also show that once CEACAM1-L is caspase-cleaved it becomes a stronger adhesion molecule than both the shorter and the longer expressing isoforms. platelet endothelial cell adhesion molecule-1 carcinoembryonic antigen-related cell adhesion molecule 1 long CEACAM1 isoform short CEACAM1 isoform antibody poly(ADP-ribose) polymerase 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid Apoptosis is an essential process for the development of an organism and its homeostasis. A very specific pattern of cell death occurs during embryogenesis leading to viability of the newborn (1Vaux D.L. Korsmeyer S.J. Cell. 1999; 96: 245-254Abstract Full Text Full Text PDF PubMed Scopus (1369) Google Scholar). Survival also depends on proper control of apoptosis throughout growth and in aging processes. Indeed tumor development ensues from deregulation of apoptosis due to blockage of cell death. Conversely increased cell death occurs in some neurodegenerative diseases (2Thompson C.B. Science. 1995; 267: 1456-1462Crossref PubMed Scopus (6205) Google Scholar). Hallmarks of apoptosis are cell shrinkage, cell membrane blebbing, formation of apoptotic bodies (3Wyllie A.H. Kerr J.F. Currie A.R. Int. Rev. Cytol. 1980; 68: 251-306Crossref PubMed Scopus (6728) Google Scholar), cleavage of genomic DNA (4Wyllie A.H. Nature. 1980; 284: 555-556Crossref PubMed Scopus (4163) Google Scholar), mitochondrial cytochrome c release (5Kluck R.M. Bossy-Wetzel E. Green D.R. Newmeyer D.D. Science. 1997; 275: 1132-1136Crossref PubMed Scopus (4289) Google Scholar, 6Yang J. Liu X. Bhalla K. Kim C.N. Ibrado A.M. Cai J. Peng T.I. Jones D.P. Wang X. Science. 1997; 275: 1129-1132Crossref PubMed Scopus (4422) Google Scholar), and activation of caspases (7Lazebnik Y.A. Kaufmann S.H. Desnoyers S. Poirier G.G. Earnshaw W.C. Nature. 1994; 371: 346-347Crossref PubMed Scopus (2351) Google Scholar). The latter are specific cysteine proteases that either autoactivate themselves or activate other family members in a well defined cascade depending on the type of the apoptotic stimuli (8Earnshaw W.C. Martins L.M. Kaufmann S.H. Annu. Rev. Biochem. 1999; 68: 383-424Crossref PubMed Scopus (2450) Google Scholar). Once caspases are activated, they cleave many different substrates at a specific consensus site always after an aspartic acid residue (Asp). The particular caspase specificity for a substrate resides in the 3 amino acids positioned carboxyl-terminally to the aspartic acid cleavage site (9Thornberry N.A. Rano T.A. Peterson E.P. Rasper D.M. Timkey T. Garcia-Calvo M. Houtzager V.M. Nordstrom P.A. Roy S. Vaillancourt J.P. Chapman K.T. Nicholson D.W. J. Biol. Chem. 1997; 272: 17907-17911Abstract Full Text Full Text PDF PubMed Scopus (1852) Google Scholar). Caspase substrates include a number of essential proteins involved in many different types of functions. For example, Gas2 (10Brancolini C. Benedetti M. Schneider C. EMBO J. 1995; 14: 5179-5190Crossref PubMed Scopus (240) Google Scholar), gelsolin (11Kothakota S. Azuma T. Reinhard C. Klippel A. Tang J. Chu K. McGarry T.J. Kirschner M.W. Koths K. Kwiatkowski D.J. Williams L.T. Science. 1997; 278: 294-298Crossref PubMed Scopus (1042) Google Scholar), spectrin (12Nath R. Raser K.J. Stafford D. Hajimohammadreza I. Posner A. Allen H. Talanian R.V. Yuen P. Gilbertsen R.B. Wang K.K. Biochem. J. 1996; 319: 683-690Crossref PubMed Scopus (398) Google Scholar, 13Cryns V.L. Bergeron L. Zhu H. Li H. Yuan J. J. Biol. Chem. 1996; 271: 31277-31282Abstract Full Text Full Text PDF PubMed Scopus (196) Google Scholar), focal adhesion kinase (14Wen L.P. Fahrni J.A. Troie S. Guan J.L. Orth K. Rosen G.D. J. Biol. Chem. 1997; 272: 26056-26061Abstract Full Text Full Text PDF PubMed Scopus (310) Google Scholar, 15Gervais F.G. Thornberry N.A. Ruffolo S.C. Nicholson D.W. Roy S. J. Biol. Chem. 1998; 273: 17102-17108Abstract Full Text Full Text PDF PubMed Scopus (173) Google Scholar), औ-catenin (16Brancolini C. Lazarevic D. Rodriguez J. Schneider C. J. Cell Biol. 1997; 139: 759-771Crossref PubMed Scopus (198) Google Scholar, 17Herren B. Levkau B. Raines E.W. Ross R. Mol. Biol. Cell. 1998; 9: 1589-1601Crossref PubMed Scopus (231) Google Scholar), plakoglobin (17Herren B. Levkau B. Raines E.W. Ross R. Mol. Biol. Cell. 1998; 9: 1589-1601Crossref PubMed Scopus (231) Google Scholar), and actin (18Kayalar C. Örd T.M. Pia Testa M.P. Zhong L. Bredesen D.E. Proc. Natl. Acad. Sci. U. S. A. 1996; 93: 2234-2238Crossref PubMed Scopus (262) Google Scholar,19Mashima T. Naito M. Noguchi K. Miller D.K. Nicholson D.W. Tsuruo T. Oncogene. 1997; 14: 1007-1012Crossref PubMed Scopus (218) Google Scholar) are molecules involved in cell-extracellular matrix or cell-cell adhesion that are cleaved by caspases during apoptosis. In addition, apoptosis activates metalloproteases that are involved in the cleavage and shedding of extracellular domains of the cell adhesion molecules PECAM-11 (20Ilan N. Mohsenin A. Cheung L. Madri J.A. FASEB J. 2001; 15: 362-372Crossref PubMed Scopus (117) Google Scholar) and vascular endothelial cadherin (17Herren B. Levkau B. Raines E.W. Ross R. Mol. Biol. Cell. 1998; 9: 1589-1601Crossref PubMed Scopus (231) Google Scholar). CEACAM1 (previously Bgp) (21Beauchemin N. Chen T. Draber P. Dveksler G. Gold P. Gray-Owen S. Grunert F. Hammarström S. Holmes K.V. Karlson A. Kuroki M. Lin S.H. Lucka L. Najjar S.M. Neumaier M. Öbrink B. Shively J.E. Skubitz K.M. Stanners C.P. Thomas P. Thompson J.A. Virji M. von Kleist S. Wagener C. Watts S. Zimmermann W. Exp. Cell Res. 1999; 252: 243-249Crossref PubMed Scopus (328) Google Scholar) is a transmembrane protein of the carcinoembryonic antigen family. It consists of either two or four extracellular Ig-like domains, one membrane-spanning region, and a cytoplasmic tail that can either be short (10 amino acids, CEACAM1-S) or long (73 amino acids, CEACAM1-L). The alternative splicing events responsible for generating the short or the long isoforms are illustrated in Fig. 1 (22McCuaig K. Turbide C. Beauchemin N. Cell Growth Differ. 1992; 3: 165-174PubMed Google Scholar). All exons encoding the cytoplasmic tails are found in exons 6–9. To generate the short isoform, exon 6 is alternatively linked to exon 8 that encompasses one TGA stop codon. Exon 7 is only included in the long tail isoform. Introduction of exon 7-encoded sequence in the cytoplasmic domain shifts the open reading frame and makes use of a different TGA stop codon located in exon 9. Exon 7 encodes the most conserved region of the long cytoplasmic tail of the human, mouse, and rat sequences (Fig. 1, gray box). This suggests that important functions rely on the inclusion of this region and might also explain some of the differences between functions of the short versus the long isoform. CEACAM1 functions as an intercellular homophilic adhesion molecule, binding through its amino-terminal domain (23Ocklind C. Öbrink B. J. Biol. Chem. 1982; 257: 6788-6795Abstract Full Text PDF PubMed Google Scholar, 24Cheung P.H. Luo W. Qiu Y. Zhang X. Earley K. Millirons P. Lin S.H. J. Biol. Chem. 1993; 268: 24303-24310Abstract Full Text PDF PubMed Google Scholar, 25Izzi L. Turbide C. Houde C. Kunath T. Beauchemin N. Oncogene. 1999; 18: 5563-5572Crossref PubMed Scopus (71) Google Scholar, 26Öbrink B. Curr. Opin. Cell Biol. 1997; 9: 616-626Crossref PubMed Scopus (234) Google Scholar). The cytoplasmic domain influences the adhesion properties of CEACAM1 as the short isoform triggers more efficient adhesion than the long isoform in aggregation assays (25Izzi L. Turbide C. Houde C. Kunath T. Beauchemin N. Oncogene. 1999; 18: 5563-5572Crossref PubMed Scopus (71) Google Scholar, 26Öbrink B. Curr. Opin. Cell Biol. 1997; 9: 616-626Crossref PubMed Scopus (234) Google Scholar). Our group (27Sadekova S. Lamarche-Vane N. Li X. Beauchemin N. Mol. Biol. Cell. 2000; 11: 65-77Crossref PubMed Scopus (51) Google Scholar) and others (28Schumman D. Chen C.L. Kaplan B. Shively J.E. J. Biol. Chem. 2001; 276: 47421-47433Abstract Full Text Full Text PDF PubMed Scopus (61) Google Scholar) have shown that both the long and short CEACAM1 cytoplasmic tails can be associated with the actin cytoskeleton and that activation of Rho-like GTPase contributes to the localization of CEACAM1-L at cell-cell contacts and to its adhesion function (27Sadekova S. Lamarche-Vane N. Li X. Beauchemin N. Mol. Biol. Cell. 2000; 11: 65-77Crossref PubMed Scopus (51) Google Scholar). Increased CEACAM1-L phosphorylation results in its association with actin via adaptor proteins like tropomyosin (28Schumman D. Chen C.L. Kaplan B. Shively J.E. J. Biol. Chem. 2001; 276: 47421-47433Abstract Full Text Full Text PDF PubMed Scopus (61) Google Scholar) and/or paxillin (29Ebrahimnejad A. Flayeh R. Unteregger G. Wagener C. Brummer J. Exp. Cell Res. 2000; 260: 365-373Crossref PubMed Scopus (28) Google Scholar) for the long cytoplasmic isoform but directly for CEACAM1-S (29Ebrahimnejad A. Flayeh R. Unteregger G. Wagener C. Brummer J. Exp. Cell Res. 2000; 260: 365-373Crossref PubMed Scopus (28) Google Scholar). When tyrosine-phosphorylated, CEACAM1-L also interacts with the and is to a in J. A. U. T. A.M. Wagener C. J. 2001; Full Text Full Text PDF PubMed Scopus (61) Google Scholar). the CEACAM1-S and CEACAM1-L isoforms are in the of the and on endothelial and on and N. Lin S.H. Stanners C.P. Cell and of as a Scholar). CEACAM1 is in the development of and of but its is in N. Lin S.H. Stanners C.P. Cell and of as a Scholar). When but not is the mouse colon carcinoma cell tumor development is by in in This of tumor development is the of the long cytoplasmic tail T. C. Turbide C. Beauchemin N. Oncogene. 1995; 11: Google Scholar) and with its phosphorylation (25Izzi L. Turbide C. Houde C. Kunath T. Beauchemin N. Oncogene. 1999; 18: 5563-5572Crossref PubMed Scopus (71) Google Scholar). of the longer isoform also shown to the cell in an extracellular matrix of the shorter isoform the cell growth to that of a J. Chen Liu P. J. Shively J. Proc. Natl. Acad. Sci. U. S. A. PubMed Scopus Google Scholar). In this of apoptosis in mouse CT51 the cytoplasmic domain of CEACAM1-L is demonstrated using a number of point and deletion mutants, the conserved membrane-proximal DQRD encoded within exon 7, a caspase-3 cleavage site. This cleavage generates a CEACAM1 protein with a of the cytoplasmic domain CEACAM1-S but with stronger adhesion properties than both isoforms. The CT51 mouse colon carcinoma cell was by G. of CT51 and cells in with and at in CEACAM1 or the and as T. C. Turbide C. Beauchemin N. Oncogene. 1995; 11: Google Scholar). of CT51 cells with by cells and of cell and have T. C. Turbide C. Beauchemin N. Oncogene. 1995; 11: Google Scholar). in the of cells expressing or the also generated using cell of the proteins was by assays as T. C. Turbide C. Beauchemin N. Oncogene. 1995; 11: Google Scholar). The CEACAM1-L in the of the (22McCuaig K. Turbide C. Beauchemin N. Cell Growth Differ. 1992; 3: 165-174PubMed Google Scholar) was used as a for The used 1994; PubMed Scopus Google Scholar) involved the of two The is located at within the CEACAM1-L and an site. This was used in with point or deletion The of the was used with the The was generated with the and the the was generated with the and the the was generated with the and the and the of CEACAM1-L was generated with the and the The with a stop codon and was generated with the using the in M. L. P. Houde C. Kunath T. A. Beauchemin N. J. Biol. Chem. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar). The the and of the within the the CEACAM1-L The sequence of the was by DNA The of the for in Apoptosis was in CT51 cells by the addition for of of either or 1 to 8 of a 1 to addition of the apoptotic the of the cells in the and and cells as for The cell was used for CEACAM1 for 6 in a to cells and apoptotic bodies to The at The in of The CEACAM1 to in of and and as for on and by a CEACAM1 to with of peptide for at to the by addition of of spectrin and CEACAM1-L cleavage was by the with at the as the apoptotic agents for the All for in to on the blocked with in from 1 to and for 1 in a was used for antibody used for was from CEACAM1 was using the the CEACAM1 extracellular domains or the the CEACAM1-L cytoplasmic domain M. P. Turbide C. S. D. Beauchemin N. Res. 1993; Google Scholar). The was from and to used as CEACAM1 and with the CEACAM1-L and using the or using of DNA in a for at and at proteins used in cleavage assays with purified recombinant human caspases. The caspases as in J. Nicholson D.W. K.M. M. Y. M. Peterson E.P. Rasper D.M. R. Vaillancourt J.P. Thornberry N.A. Biol. 1996; 3: PubMed Scopus Google and in a of of and to at for 1 and by the addition of of for and to for in acid and and in for to for the of cleaved CEACAM1-L was by was from the is the of substrate at is the substrate and Cell aggregation assays as in (25Izzi L. Turbide C. Houde C. Kunath T. Beauchemin N. Oncogene. 1999; 18: 5563-5572Crossref PubMed Scopus (71) Google Scholar). In cell of either or cells of 3 cells of in 3 of and (10 for 3 at with at by for cells and at on the of CEACAM1 is a transmembrane protein in different When on this protein as a with different due to its When in mouse CT51 the CEACAM1-L and CEACAM1-S proteins as with of and as shown in Fig. 1 The 8-kDa between the two isoforms is due to the long cytoplasmic the CEACAM1-S and are to in the on are (Fig. To apoptotic cleavage within the long cytoplasmic cell to using peptide to as The CEACAM1-L protein as a at (Fig. CEACAM1-S was found at (Fig. A of the two proteins can be different apoptotic agents to the to apoptosis in a CT51 colon carcinoma cell expressing CEACAM1-L T. C. Turbide C. Beauchemin N. Oncogene. 1995; 11: Google Scholar). In a or in the of a CEACAM1-L cleavage after as a (Fig. The cleavage of a well caspase-3 substrate D.W. A. Thornberry N.A. Vaillancourt J.P. M. Y. M. Y.A. N.A. S.M. V.L. Miller D.K. Nature. 1995; PubMed Scopus Google Scholar), was also as a for apoptosis of the three agents to cleavage of after and cleavage after (Fig. as by the of an with results with the of CEACAM1-L cleavage different depending on the apoptotic CEACAM1-L be as as after (Fig. but only be between and after and (Fig. and We also the of the after cleavage apoptotic with the antibody specific for the cytoplasmic domain of CEACAM1-L M. P. Turbide C. S. D. Beauchemin N. Res. 1993; Google Scholar). the protein (Fig. or the cytoplasmic peptide not but it not the cleavage in (Fig. or the that this was cleaved CEACAM1-L is CT51 cells expressing CEACAM1-L treated with for the on to and with specific for the CEACAM1-L cytoplasmic the apoptotic cleavage of CEACAM1-L as a to that of the shorter this that the DQRD membrane-proximal motif might be by the the potential caspase cleavage motif by The at and was to either or to generate expressing CT51 cell expressing cells with a CEACAM1 and cell of CEACAM1 was by cell The was at a and by of the cell These a in to not of the point or in CT51 cells was very three and not be the three apoptotic agents CEACAM1-L cleavage after the was not cleaved results with three different cell The DQRD motif the cleavage site within the CEACAM1-L protein during apoptosis. To a caspase the DQRD in vitro CEACAM1-L proteins to in vitro cleavage assays using purified recombinant and -8. was efficient in the CEACAM1-L cytoplasmic domain (Fig. but caspase-7 (Fig. and not of purified caspase-3 W. to the for CEACAM1-L cleavage by caspase-3 was When CEACAM1-L and protein with only amino acids proteins to assays with a of purified cleaved (Fig. These that and are both essential for CEACAM1-L cleavage at the DQRD To CEACAM1-L caspase-3 cleavage was in the CT51 cells apoptotic with the addition of a inhibitor D. J. Y. S. Roy S. J. Vaillancourt J. J. R. A. R. Nicholson D.W. D.M. J. Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). Fig. that CEACAM1-L cleavage is by in a a spectrin cleavage is also shown to in the cell In and CEACAM1-L cleavage was by after of The cleaved CEACAM1-L generates a of the protein that is very to CEACAM1-S for the inclusion of a DQRD this peptide might or of the shorter cytoplasmic the cleaved adhesion molecule CEACAM1-L in in have shown that CEACAM1-L is efficient at cell aggregation in vitro than CEACAM1-S (25Izzi L. Turbide C. Houde C. Kunath T. Beauchemin N. Oncogene. 1999; 18: 5563-5572Crossref PubMed Scopus (71) Google Scholar, 26Öbrink B. Curr. Opin. Cell Biol. 1997; 9: 616-626Crossref PubMed Scopus (234) Google Scholar). cells expressing or the the caspase-cleaved CEACAM1-L as cell and for cell aggregation a the aggregation properties of cells expressing a also Fig. 8 that CEACAM1-S is a more adhesion molecule than the was more efficient in cell aggregation than both CEACAM1 isoforms as cells as a cell at the of the aggregation This suggests that of the DQRD motif apoptotic cleavage is for the CEACAM1 adhesion CEACAM1-L is a protein in a number of It is in the and In CEACAM1 is found at the membrane of cells the L. F. Wagener C. S. Res. 1995; Google Scholar). It is most in the of the and is from the of the L. F. Wagener C. S. Res. 1995; Google Scholar). In this L. F. Wagener C. S. Res. 1995; Google Scholar), also of CEACAM1 in the in in the of it is associated with linked to the This region of the colon is associated with apoptosis. We have shown that the cell adhesion molecule CEACAM1-L is cleaved apoptotic in CT51 mouse colon carcinoma We identified the DQRD motif only within the long cytoplasmic domain of CEACAM1 as the site cleaved in apoptotic This cleavage site within the most conserved region of the CEACAM1-L In in vitro cleavage have also shown that but not caspase-7 or CEACAM1-L cleavage at The of for CEACAM1-L cleavage by caspase-3 is with that of other substrates as the that CEACAM1-L is cleaved at the DQRD site by in apoptotic the that the in vitro cleavage might the cleavage CEACAM1-L is a transmembrane protein with only 73 of its amino acids in the in When in vitro and not at the cell CEACAM1-L might be and the caspase-3 cleavage site within the tail might be To this used in the in vitro assays to proper of the the in of CEACAM1-L not CEACAM1-L can be as a apoptotic substrate as its cleavage in cells occurs than that of or the kinase inhibitor is used as an apoptotic CEACAM1-L cleavage is as as It is to that phosphorylation of CEACAM1-L or of proteins might be important for of CEACAM1-L phosphorylation site have to be to this A other cell adhesion molecules are caspase substrates or function as in the apoptotic S. J. Cell Biol. 2001; PubMed Scopus Google Scholar) have that or the tails in extracellular cells to the The of tails and contributes to the activation of a process as death S. J. Cell Biol. 2001; PubMed Scopus Google Scholar). In vascular endothelial specific cadherin shedding from the cell as a of during growth apoptosis (17Herren B. Levkau B. Raines E.W. Ross R. Mol. Biol. Cell. 1998; 9: 1589-1601Crossref PubMed Scopus (231) Google Scholar). औ-catenin and cleaved by caspase-3 and vascular endothelial cadherin from the This to of the and of properties (17Herren B. Levkau B. Raines E.W. Ross R. Mol. Biol. Cell. 1998; 9: 1589-1601Crossref PubMed Scopus (231) Google Scholar). In the the cell adhesion molecule also shedding of a from the cell after activation of (20Ilan N. Mohsenin A. Cheung L. Madri J.A. FASEB J. 2001; 15: 362-372Crossref PubMed Scopus (117) Google Scholar). This was due to apoptotic activation of matrix A of the extracellular cleavage was the of a cytoplasmic of this protein with The short with sequences more and than the and cells expressing this a in cell (20Ilan N. Mohsenin A. Cheung L. Madri J.A. FASEB J. 2001; 15: 362-372Crossref PubMed Scopus (117) Google Scholar). within the long cytoplasmic tail of CEACAM1 are essential for with paxillin (29Ebrahimnejad A. Flayeh R. Unteregger G. Wagener C. Brummer J. Exp. Cell Res. 2000; 260: 365-373Crossref PubMed Scopus (28) Google Scholar), J. A. U. T. A.M. Wagener C. J. 2001; Full Text Full Text PDF PubMed Scopus (61) Google Scholar) and as well as 1 and M. L. P. Houde C. Kunath T. A. Beauchemin N. J. Biol. Chem. 1999; Full Text Full Text PDF PubMed Scopus Google Scholar, K.M. K. Skubitz J. 1995; Google Scholar, S.M. N. Y. P. D. 1995; PubMed Scopus Google Scholar, N. Kunath T. J. B. Turbide C. E. A. Oncogene. 1997; 14: PubMed Scopus Google Scholar). CEACAM1-L also shown to have two actin (27Sadekova S. Lamarche-Vane N. Li X. Beauchemin N. Mol. Biol. Cell. 2000; 11: 65-77Crossref PubMed Scopus (51) Google Scholar, D. Chen C.L. Kaplan B. Shively J.E. J. Biol. Chem. 2001; 276: 47421-47433Abstract Full Text Full Text PDF PubMed Scopus (61) Google Scholar) and two M. I. Öbrink B. J. Biol. Chem. 1996; 271: Full Text Full Text PDF PubMed Scopus Google Scholar) binding domains, CEACAM1-S only one binding site to cleavage be to and in functions. In this show that the apoptotic cleaved more adhesion properties than CEACAM1-L or (Fig. The between the short isoform and the cleaved long is the DQRD motif at the of caspase-cleaved of this motif to the adhesion CEACAM1 is to be a homophilic cell-cell adhesion molecule, but that this apoptotic isoform might have different adhesion It demonstrated that intercellular adhesion Ig-like adhesion molecule, to the in cells but interacts with once apoptosis is A. D.L. J. 1999; Google Scholar). This in recognition and of the apoptotic cell by the is for the intercellular adhesion as its and are not during apoptosis. the cleaved adhesion properties a in apoptotic cell and in of the cleaved CEACAM1-L cytoplasmic domain We are to and of for of and We also for in some and

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