Limits...
Expression of CNPY2 in mouse tissues: quantification and localization.

Hatta K, Guo J, Ludke A, Dhingra S, Singh K, Huang ML, Weisel RD, Li RK - PLoS ONE (2014)

Bottom Line: CNPY2 was also detectable in mouse blood and human and mouse uteri.These data demonstrate CNPY2 is widely distributed in tissues and suggest the protein has biological functions that have yet to be identified.Using these new observations we discuss possible functions of the protein.

View Article: PubMed Central - PubMed

Affiliation: Division of Cardiovascular Surgery, Toronto General Research Institute, University Health Network, Toronto, Ontario, Canada; Institute of Medical Sciences, University of Toronto, Toronto, Ontario, Canada.

ABSTRACT
Canopy FGF signaling regulator 2 (CNPY2) is a FGF21-modulated protein containing a saposin B-type domain. In vitro studies have shown CNPY2 is able to enhance neurite outgrowth in neurons and stabilize the expression of low density lipoprotein receptor in macrophages and hepatocytes. However, no in vivo data are available on the normal expression of CNPY2 and information is lacking on which cell types express this protein in tissues. To address this, the present study examined CNPY2 expression at the mRNA and protein levels. Quantitative PCR and ELISA examination of mouse tissues showed that CNPY2 varies between organs, with the highest expression in the heart, lung and liver. Immunohistochemistry detected CNPY2 in a variety of cell types including skeletal, cardiac and smooth muscle myocytes, endothelial cells and epithelial cells. CNPY2 was also detectable in mouse blood and human and mouse uteri. These data demonstrate CNPY2 is widely distributed in tissues and suggest the protein has biological functions that have yet to be identified. Using these new observations we discuss possible functions of the protein.

No MeSH data available.


CNPY2 localization in mouse and human uteri and human trophoblast.Immunoflourescnece for CNPY2 was performed on mouse uteri (A–D) and endometrium (E–H) over the course of the estrous cycle. Endometrial epithelia had luminal expression at estrus (asterisks). Fresh, unfixed endometrial whole-mounts were also examined (I–K). Human uteri (L, M) and human trophoblast (N, O) also expressed CNPY2. Immunofluorescence shows CNPY2 (green), alpha-smooth muscle actin (red) and DAPI (blue).
© Copyright Policy
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4230931&req=5

pone-0111370-g006: CNPY2 localization in mouse and human uteri and human trophoblast.Immunoflourescnece for CNPY2 was performed on mouse uteri (A–D) and endometrium (E–H) over the course of the estrous cycle. Endometrial epithelia had luminal expression at estrus (asterisks). Fresh, unfixed endometrial whole-mounts were also examined (I–K). Human uteri (L, M) and human trophoblast (N, O) also expressed CNPY2. Immunofluorescence shows CNPY2 (green), alpha-smooth muscle actin (red) and DAPI (blue).

Mentions: In humans and mice, uterine endometrial and glandular epithelial cells as well as myometrial smooth muscle cells expressed CNPY2 (Figure 6 A–M). Additionally, human syncytiotrophoblast and cytotrophoblast stained positively for CNPY2 (Figure 6 N, O).


Expression of CNPY2 in mouse tissues: quantification and localization.

Hatta K, Guo J, Ludke A, Dhingra S, Singh K, Huang ML, Weisel RD, Li RK - PLoS ONE (2014)

CNPY2 localization in mouse and human uteri and human trophoblast.Immunoflourescnece for CNPY2 was performed on mouse uteri (A–D) and endometrium (E–H) over the course of the estrous cycle. Endometrial epithelia had luminal expression at estrus (asterisks). Fresh, unfixed endometrial whole-mounts were also examined (I–K). Human uteri (L, M) and human trophoblast (N, O) also expressed CNPY2. Immunofluorescence shows CNPY2 (green), alpha-smooth muscle actin (red) and DAPI (blue).
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4230931&req=5

pone-0111370-g006: CNPY2 localization in mouse and human uteri and human trophoblast.Immunoflourescnece for CNPY2 was performed on mouse uteri (A–D) and endometrium (E–H) over the course of the estrous cycle. Endometrial epithelia had luminal expression at estrus (asterisks). Fresh, unfixed endometrial whole-mounts were also examined (I–K). Human uteri (L, M) and human trophoblast (N, O) also expressed CNPY2. Immunofluorescence shows CNPY2 (green), alpha-smooth muscle actin (red) and DAPI (blue).
Mentions: In humans and mice, uterine endometrial and glandular epithelial cells as well as myometrial smooth muscle cells expressed CNPY2 (Figure 6 A–M). Additionally, human syncytiotrophoblast and cytotrophoblast stained positively for CNPY2 (Figure 6 N, O).

Bottom Line: CNPY2 was also detectable in mouse blood and human and mouse uteri.These data demonstrate CNPY2 is widely distributed in tissues and suggest the protein has biological functions that have yet to be identified.Using these new observations we discuss possible functions of the protein.

View Article: PubMed Central - PubMed

Affiliation: Division of Cardiovascular Surgery, Toronto General Research Institute, University Health Network, Toronto, Ontario, Canada; Institute of Medical Sciences, University of Toronto, Toronto, Ontario, Canada.

ABSTRACT
Canopy FGF signaling regulator 2 (CNPY2) is a FGF21-modulated protein containing a saposin B-type domain. In vitro studies have shown CNPY2 is able to enhance neurite outgrowth in neurons and stabilize the expression of low density lipoprotein receptor in macrophages and hepatocytes. However, no in vivo data are available on the normal expression of CNPY2 and information is lacking on which cell types express this protein in tissues. To address this, the present study examined CNPY2 expression at the mRNA and protein levels. Quantitative PCR and ELISA examination of mouse tissues showed that CNPY2 varies between organs, with the highest expression in the heart, lung and liver. Immunohistochemistry detected CNPY2 in a variety of cell types including skeletal, cardiac and smooth muscle myocytes, endothelial cells and epithelial cells. CNPY2 was also detectable in mouse blood and human and mouse uteri. These data demonstrate CNPY2 is widely distributed in tissues and suggest the protein has biological functions that have yet to be identified. Using these new observations we discuss possible functions of the protein.

No MeSH data available.