scholarly journals Molecular cloning of the two very low-density lipoprotein receptor (VLDLR) subtypes in geese and the effect of overfeeding on their MRNA levels

2009 ◽  
Vol 89 (4) ◽  
pp. 441-448 ◽  
Author(s):  
C Han ◽  
J Yao ◽  
J Wang ◽  
L Lu ◽  
L Li
Keyword(s):  
Molecular Cloning ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Very Low Density Lipoprotein ◽  
Low Density ◽  
Lipoprotein Receptor ◽  
Mrna Levels ◽  
Low Density Lipoprotein Receptor ◽  
Density Lipoprotein Receptor ◽  
Landes Geese

The objectives of this study were to verify the existence of two subtypes of the very low-density lipoprotein receptor (VLDLR) gene in geese, to investigate the effect of overfeeding on the plasma concentration of triglycerides (TG) and the very low density lipoprotein (VLDL), the activity of lipoprotein lipase (LPL), and the mRNA level of VLDLR in Sichuan White geese and Landes geese. The results indicate that there are two subtypes of the VLDLR gene in geese, and that they share a high similarity with those of other species. The expression of VLDLR I and VLDLR II was found in both tissues examined. After overfeeding, the expression level of VLDLR I in adipose tissue showed about a onefold increase (P < 0.05) in both breeds. Overfeeding induced a significant decrease of VLDLR I in skeletal muscle of both breeds, and a significant decrease of VLDLR II in Sichuan White geese (P < 0.05), but an obvious increase of VLDLR II in Landes geese (P < 0.05). In addition, overfeeding induced the increase of plasma VLDL, TG concentration and plasma LPL activity. It was concluded that VLDLR may participate in the metabolism of VLDL-TG by regulating the LPL-mediated TG hydrolysis in geese. Key words: Gene expression, geese, molecular cloning, overfeeding, very low-density lipoprotein receptor

Effects of gemfibrozil administration on very low density lipoprotein receptor mRNA levels in rabbits

1996 ◽  
Vol 126 (2) ◽  
pp. 221-226 ◽  
Author(s):  
Naoki Matsuoka ◽  
Hisato Jingami ◽  
Hiroaki Masuzaki ◽  
Megumi Mizuno ◽  
Shigeo Nakaishi ◽  
...  
Keyword(s):  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Very Low Density Lipoprotein ◽  
Low Density ◽  
Lipoprotein Receptor ◽  
Mrna Levels ◽  
Low Density Lipoprotein Receptor ◽  
Receptor Mrna ◽  
Density Lipoprotein Receptor

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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