TY - JOUR
T1 - Identification of CEACAM6 as an intermediate filament-associated protein expressed in sertoli cells of rat testis
AU - Kurio, Hitoshi
AU - Hatsuda, Hiroshi
AU - Murayama, Emi
AU - Kaneko, Takane
AU - Iida, Hiroshi
PY - 2011/11/1
Y1 - 2011/11/1
N2 - Ceacam6 (carcinoembryonic antigen-related cell adhesion molecule 6 gene) has recently been isolated by differential display followed by RT-PCR and DNA sequence analyses. Ceacam6 is a member of an immunoglobulin superfamily and encodes a protein of 266 amino acid residues possessing one immunoglobulin (Ig)-like domain. RT-PCR analysis showed that Ceacam6 was dominantly expressed in rat testis and its expression level prominently increased after 6 wk of postnatal development in testis. Immunohistochemical analyses using the anti-CEACAM6 antibody revealed that CEACAM6 colocalized with intermediate filaments (vimentin) in Sertoli cells and interstitial cells. The association between CEACAM6 and vimentin was observed throughout postnatal development in rat testis. Transfection experiments performed in COS-7 cells suggested that overexpression of CEACAM6 brought about aggregation of vimentin filament around nuclei with which CEACAM6 colocalized and that the N-terminus region of CEACAM6, including the Ig-like domain, seemed to be required for association with vimentin filaments. Interaction between CEACAM6 and vimentin in rat testis and transfected COS-7 cells was confirmed by immunoprecipitation. Our observations strongly suggested that CEACAM6 might be a novel intermediate filament-associated protein involved in regulation of vimentin architecture in Sertoli cells.
AB - Ceacam6 (carcinoembryonic antigen-related cell adhesion molecule 6 gene) has recently been isolated by differential display followed by RT-PCR and DNA sequence analyses. Ceacam6 is a member of an immunoglobulin superfamily and encodes a protein of 266 amino acid residues possessing one immunoglobulin (Ig)-like domain. RT-PCR analysis showed that Ceacam6 was dominantly expressed in rat testis and its expression level prominently increased after 6 wk of postnatal development in testis. Immunohistochemical analyses using the anti-CEACAM6 antibody revealed that CEACAM6 colocalized with intermediate filaments (vimentin) in Sertoli cells and interstitial cells. The association between CEACAM6 and vimentin was observed throughout postnatal development in rat testis. Transfection experiments performed in COS-7 cells suggested that overexpression of CEACAM6 brought about aggregation of vimentin filament around nuclei with which CEACAM6 colocalized and that the N-terminus region of CEACAM6, including the Ig-like domain, seemed to be required for association with vimentin filaments. Interaction between CEACAM6 and vimentin in rat testis and transfected COS-7 cells was confirmed by immunoprecipitation. Our observations strongly suggested that CEACAM6 might be a novel intermediate filament-associated protein involved in regulation of vimentin architecture in Sertoli cells.
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U2 - 10.1095/biolreprod.111.092437
DO - 10.1095/biolreprod.111.092437
M3 - Article
C2 - 21734260
AN - SCOPUS:81055124151
VL - 85
SP - 924
EP - 933
JO - Biology of Reproduction
JF - Biology of Reproduction
SN - 0006-3363
IS - 5
ER -