[Cloning and identification of human vigilin full-length coding region].

Sichuan Da Xue Xue Bao Yi Xue Ban

Department of Biochemistry and Molecular Biology, West China School of Preclinical and Forensic Medicine, Sichuan University, Chengdu 610041, China.

Published: November 2008

Objective: The full-length of human vigilin encodes 1289 amino acids, containing 14 KH domains. We adopted a five step PCR technique to clone the full-length vigilin coding regions to investigate the functions of full-length vigilin, N-terminal of vigilin, C-terminal of vigilin and different KH.

Methods: Vigilin was dissected into five fragments according to the restrictive endounclease enzymes site of vigilin. The total RNA was extracted from the livers of healthy adults died from accident. The cDNA was amplified by RT-PCR. Then the amplified PCR product was digested and inserted into pUC118 vector and subcloned into pUC118 vector.

Results: Eight gene fragments and full-length of human vigilin were obtained. The gene sequence of vigilin was identical with its cDNA sequence reported (NM:005336) in the GenBank.

Conclusion: The full-length vigilin coding region has been cloned successfully.

Download full-text PDF

Source

Publication Analysis

Top Keywords

human vigilin
12
full-length vigilin
12
vigilin
11
full-length human
8
vigilin coding
8
full-length
6
[cloning identification
4
identification human
4
vigilin full-length
4
full-length coding
4

Similar Publications

Role of Vigilin and RACK1 in dengue virus- interactions.

mSphere

December 2024

Australian Infectious Disease Research Centre, School of Biological Sciences, The University of Queensland, Brisbane, Queensland, Australia.

Vigilin is a large and evolutionary conserved RNA-binding protein (RBP), which can interact with RNA through its KH domain. Vigilin is, therefore, a multifunctional protein reported to be associated with RNA transport and metabolism, sterol metabolism, chromosome segregation, carcinogenesis, and heterochromatin-mediated gene silencing. The receptor for activated C kinase 1 (RACK1) is another highly conserved protein involved in many cellular pathways.

View Article and Find Full Text PDF

Background: Familial chylomicronemia syndrome (FCS) is a rare monogenic form of severe hypertriglyceridemia, caused by mutations in genes involved in triglyceride metabolism. Herein, we report the case of a Korean family with familial chylomicronemia syndrome caused by compound heterozygous deletions of glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 (GPIHBP1).

Case Presentation: A 4-year-old boy was referred for the evaluation of severe hypertriglyceridemia (3734 mg/dL) that was incidentally detected 4 months prior.

View Article and Find Full Text PDF

The high-density lipoprotein binding protein (HDLBP) is the human member of an evolutionarily conserved family of RNA-binding proteins, the vigilin protein family. These proteins are characterized by 14 or 15 RNA-interacting KH (heterologous nuclear ribonucleoprotein K homology) domains. While mainly present at the cytoplasmic face of the endoplasmic reticulum, HDLBP and its homologs are also found in the cytosol and nucleus.

View Article and Find Full Text PDF

Background: Pancreatic neuroendocrine neoplasms (p-NENs) are relatively rare and highly heterogeneous. Dyslipidemia may be related to the risk of developing p-NENs, although dyslipidemia in patients with p-NENs is rarely reported. In this study, the clinical characteristics of p-NENs patients with different lipid levels and their prognostic value in p-NENs patients were evaluated.

View Article and Find Full Text PDF

Background: Severe hypertriglyceridemia can be caused by pathogenic variants in genes encoding proteins involved in the metabolism of triglyceride-rich lipoproteins. A key protein in this respect is lipoprotein lipase (LPL) which hydrolyzes triglycerides in these lipoproteins. Another important protein is glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1) which transports LPL to the luminal side of the endothelial cells.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!