Lipoprotein Receptor Associated Protein (LRPAP1) Insertion/Deletion Polymorphism: Association with Gallbladder Cancer Susceptibility

2007 ◽  
Author(s):  
Sachchida Nand Pandey ◽  
Manjusha Dixit ◽  
Gourdas Choudhuri ◽  
Balraj Mittal
Keyword(s):  
Gallbladder Cancer ◽  
Cancer Susceptibility ◽  
Lipoprotein Receptor ◽  
Deletion Polymorphism ◽  
Receptor Associated Protein

scholarly journals CCR5 Δ32 Polymorphism: Associated with Gallbladder Cancer Susceptibility

2008 ◽  
Vol 67 (5) ◽  
pp. 516-522 ◽  
Author(s):  
A. Srivastava ◽  
S. N. Pandey ◽  
G. Choudhuri ◽  
B. Mittal
Keyword(s):  
Gallbladder Cancer ◽  
Cancer Susceptibility

Association of cancer stem cell markers genetic variants with gallbladder cancer susceptibility, prognosis, and survival

Tumor Biology ◽  
2015 ◽  
Vol 37 (2) ◽  
pp. 1835-1844 ◽  
Author(s):  
Anu Yadav ◽  
Annapurna Gupta ◽  
Neeraj Rastogi ◽  
Sushma Agrawal ◽  
Ashok Kumar ◽  
...  
Keyword(s):  
Stem Cell ◽  
Cancer Stem Cell ◽  
Gallbladder Cancer ◽  
Genetic Variants ◽  
Cancer Susceptibility ◽  
Stem Cell Markers ◽  
Cell Markers ◽  
Cancer Stem Cell Markers

scholarly journals The Low-Density Lipoprotein Receptor-Related Protein (LRP) Mediates Clearance of Coagulation Factor Xa In Vivo

Blood ◽  
1998 ◽  
Vol 91 (2) ◽  
pp. 555-560 ◽  
Author(s):  
Masaaki Narita ◽  
Amy E. Rudolph ◽  
Joseph P. Miletich ◽  
Alan L. Schwartz
Keyword(s):  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Factor Xa ◽  
Coagulation Factor ◽  
Lipoprotein Receptor ◽  
Factor X ◽  
Receptor Associated Protein ◽  
Density Lipoprotein Receptor ◽  
Lipoprotein Receptor Related Protein

Abstract Blood coagulation factor X plays a pivotal role in the clotting cascade. When administered intravenously to mice, the majority of activated factor X (factor Xa) binds to α2-macroglobulin (α2M) and is rapidly cleared from the circulation into liver. We show here that the low-density lipoprotein receptor-related protein (LRP) is responsible for factor Xa catabolism in vivo. Mice overexpressing a 39-kD receptor-associated protein that binds to LRP and inhibits its ligand binding activity displayed dramatically prolonged plasma clearance of 125I-factor Xa. Preadministration of α2M-proteinase complexes (α2M*) also diminished the plasma clearance of125I-factor Xa in a dose-dependent fashion. The clearance of preformed complexes of 125I-factor Xa and α2M was similar to that of 125I-factor Xa alone and was also inhibited by mice overexpressing a 39-kD receptor-associated protein. These results thus suggest that, in vivo, factor Xa is metabolized via LRP after complex formation with α2M.

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