TY - JOUR
T1 - Liver-specific ZP domain-containing protein (LZP) as a new partner of Tamm-Horsfall protein harbors on renal tubules
AU - Shen, Hai Lian
AU - Xu, Zhi Gang
AU - Huang, Li Yu
AU - Liu, Dong
AU - Lin, Dao Hong
AU - Cao, Jia Bin
AU - Zhang, Xin
AU - Wang, Zhi Qin
AU - Wang, Wen Hui
AU - Yang, Peng Yuan
AU - Han, Ze Guang
N1 - Funding Information:
Acknowledgment This work was supported by the Chinese high-Tech research and development program (863-2006AA02Z193, 863-2006AA02A305), Chinese national key program on basic research (2004CB518605), National Natural Science Foundation for Outstanding Youth (30425019), National Science Foundation for Postdoctoral Scientists of China (2005038415), Shanghai science and technology developing program (03DZ14024), and the Shanghai Postdoctoral sustentation Fund (0525).
PY - 2009
Y1 - 2009
N2 - Liver-specific ZP domain-containing protein (LZP) was recently identified as a secreted protein that is specifically expressed in liver. However, the physiological effects of LZP are largely unknown. In this study, we found that LZP was detectable in mouse kidneys, testes, ovaries and heart, in addition to liver. LZP was localized in the spermatid cells of testes, corpus luteum cells of ovaries, and cardiac muscle cells of heart. But the protein mainly anchored on the apical membrane of the thick ascending limb of the loop of Henle (TAL) cell in mouse kidney. In rat kidney LZP and Tamm-Horsfall protein (THP) were co-localized in TAL. The in vivo interaction between LZP and THP was confirmed in kidney and urine by co-immunoprecipitation assay, and the in vitro interaction was detected by GST pull-down assay, implying that the interaction could be independent on N-linked glycosylated modification of LZP. Surprisingly, LZPs with intramolecular disulfide bridges could self-interact, and then self-aggregate into spheres of varying sizes, but not polymerize into filaments. The finding that LZP might act as a new partner of THP would provide novel insights into renal functions related to THP and LZP, such as the urothelial permeability barrier and the host defense against the adhesion of pathogens.
AB - Liver-specific ZP domain-containing protein (LZP) was recently identified as a secreted protein that is specifically expressed in liver. However, the physiological effects of LZP are largely unknown. In this study, we found that LZP was detectable in mouse kidneys, testes, ovaries and heart, in addition to liver. LZP was localized in the spermatid cells of testes, corpus luteum cells of ovaries, and cardiac muscle cells of heart. But the protein mainly anchored on the apical membrane of the thick ascending limb of the loop of Henle (TAL) cell in mouse kidney. In rat kidney LZP and Tamm-Horsfall protein (THP) were co-localized in TAL. The in vivo interaction between LZP and THP was confirmed in kidney and urine by co-immunoprecipitation assay, and the in vitro interaction was detected by GST pull-down assay, implying that the interaction could be independent on N-linked glycosylated modification of LZP. Surprisingly, LZPs with intramolecular disulfide bridges could self-interact, and then self-aggregate into spheres of varying sizes, but not polymerize into filaments. The finding that LZP might act as a new partner of THP would provide novel insights into renal functions related to THP and LZP, such as the urothelial permeability barrier and the host defense against the adhesion of pathogens.
KW - LZP
KW - Tamm-Horsfall protein (THP)
KW - Thick ascending limb of the loop of Henle (TAL)
KW - ZP Domain-containing protein
KW - Zona pellucida (ZP) domain
UR - https://www.scopus.com/pages/publications/58249129452
U2 - 10.1007/s11010-008-9921-3
DO - 10.1007/s11010-008-9921-3
M3 - Article
C2 - 18830570
AN - SCOPUS:58249129452
SN - 0300-8177
VL - 321
SP - 73
EP - 83
JO - Molecular and Cellular Biochemistry
JF - Molecular and Cellular Biochemistry
IS - 1-2
ER -