Detection and characterization of a novel splice mutation in the LDL receptor intron 12 resulting in two different mutant mRNA variants

1997 ◽  
Vol 128 (1) ◽  
pp. 75-83 ◽  
Author(s):  
Henrik Nissen ◽  
Annebirthe Bo Hansen ◽  
Per Guldberg ◽  
Niels Erik Petersen ◽  
Torben Stiig Hansen ◽  
...  
Keyword(s):  
Ldl Receptor ◽  
Splice Mutation ◽  
Mrna Variants

130 Characterization of a novel endothelial receptor, LR3, that defines a new class of receptors related to the LDL receptor family

1997 ◽  
Vol 11 ◽  
pp. 37
Author(s):  
Todd A. Hembrough ◽  
Frances D. Battey ◽  
Jeffrey A. Winkles ◽  
Dudley K. Strickland
Keyword(s):  
Ldl Receptor ◽  
New Class ◽  
Endothelial Receptor ◽  
Receptor Family

Characterization of the LDL receptor in rat promegakaryoblasts in culture

1991 ◽  
Vol 11 (1) ◽  
pp. 15-21 ◽  
Author(s):  
Tracy J. Budd ◽  
Frank W. Hemming ◽  
Bruce Middleton
Keyword(s):  
Cell Biology ◽  
Receptor Cell ◽  
Low Density Lipoprotein ◽  
Ldl Receptor ◽  
Density Lipoprotein ◽  
Classical Type ◽  
Lysosomal Degradation ◽  
High Affinity ◽  
Ldl Binding

Rat promegakaryoblasts (RPM, a precursor platelet cell line) in culture exhibited a capacity to bind, take up and degrade125I-LDL. The low density lipoprotein (LDL) binding showed the following characteristics: (a) high affinity, (b) saturability, (c) specificity, (d) down-regulation, after exposure to 25 hydroxycholesterol. Furthermore the proteolytic degradation of125I-LDL by RPMs was inhibited by chloroquine which interferes with the lysosomal degradation processes. These findings show LDL receptor cell biology of RPM to be of the classical type and to differ from that of platelets.

scholarly journals Identification of Megalin as the Sole Rat Kidney Sialoglycoprotein Containing Poly α2,8 Deaminoneuraminic Acid

1999 ◽  
Vol 10 (2) ◽  
pp. 203-209
Author(s):  
MARTIN ZIAK ◽  
DONTSCHO KERJASCHKI ◽  
MARILYN G. FARQUHAR ◽  
JÜRGEN ROTH
Keyword(s):  
Rat Kidney ◽  
Ldl Receptor ◽  
Amino Acid Sequences ◽  
Purification And Characterization ◽  
Receptor Associated Protein ◽  
Mammalian Tissues ◽  
Convoluted Tubules ◽  
Receptor Family ◽  
Deaminoneuraminic Acid

Abstract. Recently, poly α2,8 deaminoneuraminic acid (poly α2,8 KDN) was demonstrated in various embryonic and adult mammalian tissues. This study reports the purification and characterization of the single poly α2,8 KDN-bearing glycoprotein from rat kidney. Amino acid sequences of proteolytic fragments shared homology with megalin, a member of the LDL receptor family. Immunochemical analysis supported this finding, since immunoprecipitated poly α2,8 KDN-bearing glycoprotein was immunoreactive with anti-megalin antibodies in Western blotting and conversely immunoprecipitated megalin was immunoreactive with the monoclonal anti-poly α2,8 KDN antibody. Furthermore, receptor-associated protein affinity-purified megalin reacted with the anti-poly α2,8 KDN antibody. By immunoelectron microscopy, labeling for both poly α2,8 KDN and megalin coincided in the brush border, endocytic invaginations and vesicles, and apical dense tubules of proximal convoluted tubules. Immunoreactivity for poly α2,8 KDN on purified megalin was abolished by β-elimination reaction but not by N-glycosidase F treatment. These data identified megalin as the sole glycoprotein of rat kidney, which contains poly α2,8 KDN present on O-glycosidically linked oligosaccharides. Furthermore, this study shows that megalin carries N-glycosidically linked hybrid and complex-type oligosaccharides terminating with sialic acid. Both poly α2,8 KDN and sialic acids on megalin may contribute to the binding of Ca2+ and cationic ligands.

scholarly journals Identification and Characterization of Rice OsHKT1;3 Variants

Plants ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 2006
Author(s):  
Shahin Imran ◽  
Yoshiyuki Tsuchiya ◽  
Sen Thi Huong Tran ◽  
Maki Katsuhara
Keyword(s):  
Expression System ◽  
Ion Homeostasis ◽  
Transcript Level ◽  
Absolute Quantification ◽  
Xenopus Laevis Oocytes ◽  
Japonica Rice ◽  
Na Currents ◽  
Mrna Variants ◽  
Identification And Characterization

In rice, the high-affinity K+ transporter, OsHKT1;3, functions as a Na+-selective transporter. mRNA variants of OsHKT1;3 have been reported previously, but their functions remain unknown. In this study, five OsHKT1;3 variants (V1-V5) were identified from japonica rice (Nipponbare) in addition to OsHKT1;3_FL. Absolute quantification qPCR analyses revealed that the transcript level of OsHKT1;3_FL was significantly higher than other variants in both the roots and shoots. Expression levels of OsHKT1;3_FL, and some variants, increased after 24 h of salt stress. Two electrode voltage clamp experiments in a heterologous expression system using Xenopus laevis oocytes revealed that oocytes expressing OsHKT1;3_FL and all of its variants exhibited smaller Na+ currents. The presented data, together with previous data, provide insights to understanding how OsHKT family members are involved in the mechanisms of ion homeostasis and salt tolerance in rice.

scholarly journals Identification and characterization of LDL receptor gene mutations in hyperlipidemic Chinese

2003 ◽  
Vol 44 (10) ◽  
pp. 1850-1858 ◽  
Author(s):  
Jui-Hung Chang ◽  
Ju-Pin Pan ◽  
Der-Yan Tai ◽  
Ai-Chun Huang ◽  
Pi-Hung Li ◽  
...  
Keyword(s):  
Receptor Gene ◽  
Ldl Receptor ◽  
Gene Mutations ◽  
Identification And Characterization
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