scholarly journals Nuclear Magnetic Resonance Solution Structure of the Recombinant Fragment Containing Three Fibrin-Binding Cysteine-Rich Domains of the Very Low Density Lipoprotein Receptor

Biochemistry ◽  
2018 ◽  
Vol 57 (30) ◽  
pp. 4395-4403 ◽  
Author(s):  
Koyeli Banerjee ◽  
Sergiy Yakovlev ◽  
James M. Gruschus ◽  
Leonid Medved ◽  
Nico Tjandra
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Solution Structure ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Very Low Density Lipoprotein ◽  
Low Density ◽  
Lipoprotein Receptor ◽  
Recombinant Fragment ◽  
Density Lipoprotein Receptor ◽  
Resonance Solution

scholarly journals Very low-density lipoprotein receptor increases in a liver-specific manner due to protein deficiency but does not affect fatty liver in mice

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Yui Oshio ◽  
Yuta Hattori ◽  
Hatsuho Kamata ◽  
Yori Ozaki-Masuzawa ◽  
Arisa Seki ◽  
...  
Keyword(s):  
Fatty Liver ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Protein Restriction ◽  
Very Low Density Lipoprotein ◽  
Low Density ◽  
Lipoprotein Receptor ◽  
Protein Levels ◽  
Specific Manner ◽  
Density Lipoprotein Receptor

AbstractVery low-density lipoprotein receptor (VLDLR) is a member of the LDL receptor family that is involved in the uptake of VLDL into cells. Increased hepatic VLDLR under endoplasmic reticulum (ER) stress has been shown to cause fatty liver. In this study, the effect of dietary protein restriction on hepatic VLDLR and the role of VLDLR in fatty liver were investigated using Vldlr knockout (KO) mice. Growing wild-type (WT) and KO mice were fed a control diet containing 20% ​​protein or a low protein diet containing 3% protein for 11 days. In WT mice, the amount of hepatic Vldlr mRNA and VLDLR protein increased by approximately 8- and 7-fold, respectively, due to protein restriction. Vldlr mRNA and protein levels increased in both type 1 and type 2 VLDLR. However, neither Vldlr mRNA nor protein levels were significantly increased in heart, muscle, and adipose tissue, demonstrating that VLDLR increase due to protein restriction occurred in a liver-specific manner. Increased liver triglyceride levels during protein restriction occurred in KO mice to the same extent as in WT mice, indicating that increased VLDLR during protein restriction was not the main cause of fatty liver, which was different from the case of ER stress.

Very Low-Density Lipoprotein Receptor in Fetal Intestine and Gastric Adenocarcinoma Cells

2000 ◽  
Vol 124 (1) ◽  
pp. 119-122
Author(s):  
Yasuhiro Nakamura ◽  
Munehiko Yamamoto ◽  
Eriko Kumamaru
Keyword(s):  
Cell Line ◽  
Gastric Adenocarcinoma ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Very Low Density Lipoprotein ◽  
Low Density ◽  
Lipoprotein Receptor ◽  
Ags Cells ◽  
Adenocarcinoma Cells ◽  
Density Lipoprotein Receptor

Abstract Background.—A very low-density lipoprotein receptor (VLDLR) was recently identified. This receptor reportedly binds specifically to very low-density lipoproteins; however, its distribution and functions in vivo have yet to be elucidated. We investigated the expression and regulation of VLDLR in fetal and carcinoma cells. Objective.—The expression of VLDLR was examined by immunohistochemistry and reverse-transcriptase polymerase chain reaction using several specimens, including a fetus of 12 to 15 weeks' gestation, various tumors, AGS cells, and INT407 cells. Results.—Immunoreactive VLDLR was abundantly present in human fetal intestinal epithelial and gastric adenocarcinoma cells. This receptor was also noted in the intestinal cell line, INT407, and gastric cancer cell line, AGS. In addition, the VLDLR that was expressed in INT407 cells, AGS cells, and gastric adenocarcinoma tissue was present mainly in a variant form lacking the O-linked sugar domain. Conclusions.—These data suggest that an important function of VLDLR may be the mediation of cell growth in developing tissues, such as fetal intestinal and cancer cells. The INT407 and AGS cell lines appear to be useful for examining the regulation of VLDLR expression.

Effect of overexpression of very low density lipoprotein receptor on cell growth

2000 ◽  
Vol 15 (2) ◽  
pp. 74-80 ◽  
Author(s):  
Yoko Wada ◽  
Yoshimi Homma ◽  
Kazuhiko Nakazato ◽  
Toshiyuki Ishibashi ◽  
Y. Maruyama
Keyword(s):  
Cell Growth ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Very Low Density Lipoprotein ◽  
Low Density ◽  
Lipoprotein Receptor ◽  
Low Density Lipoprotein Receptor ◽  
Density Lipoprotein Receptor

scholarly journals Very-Low-Density Lipoprotein Receptor Fragment Shed from HeLa Cells Inhibits Human Rhinovirus Infection

1998 ◽  
Vol 72 (12) ◽  
pp. 10246-10250 ◽  
Author(s):  
Thomas C. Marlovits ◽  
Christina Abrahamsberg ◽  
Dieter Blaas
Keyword(s):  
Hela Cells ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Intercellular Adhesion Molecule ◽  
Very Low Density Lipoprotein ◽  
Low Density ◽  
Lipoprotein Receptor ◽  
Dependent Manner ◽  
Low Density Lipoprotein Receptor ◽  
Density Lipoprotein Receptor

ABSTRACT The large family of human rhinoviruses, the main causative agents of the common cold, is divided into the major and the minor group based on receptor specificity. Major group viruses attach to intercellular adhesion molecule 1 (ICAM-1), a member of the immunoglobulin superfamily, whereas minor group viruses use low-density lipoprotein receptors (LDLR) for cell entry. During early attempts aimed at isolating the minor group receptor, we discovered that a protein with virus binding activity was released from HeLa cells upon incubation with buffer at 37°C (F. Hofer, B. Berger, M. Gruenberger, H. Machat, R. Dernick, U. Tessmer, E. Kuechler, and D. Blaas, J. Gen. Virol. 73:627–632, 1992). In light of the recent discovery of several new members of the LDLR family, we reinvestigated the nature of this protein and present evidence for its being derived from the human very-low density lipoprotein receptor (VLDLR). A soluble VLDLR fragment encompassing the eight complement type repeats and representing the N-terminal part of the receptor was then expressed in the baculovirus system; both the shed protein and the recombinant soluble VLDLR bind minor group viruses and inhibit viral infection of HeLa cells in a concentration-dependent manner.

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