Cloning and characterization of the human lactoferrin receptor gene promoter

Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine
Rulan Jiang, Bo Lönnerdal

Abstract

Lactoferrin (Lf) is a major protein in human milk. Multiple biological functions of Lf are postulated to be mediated by a Lf receptor (LfR). The Lf receptor (LfR) plays an important role in absorption of Lf and Lf-bound iron by intestinal epithelial cells. Here, we cloned and characterized the promoter from a ~ 3.1 kb 5'-flanking region of the human LfR gene. Neither a TATA box nor a CCAAT box is found at the typical positions. The transcription start site was identified as 298 bp upstream of the translation start codon (+ 1) by 5' RLM-RACE. A series of deletions of 5'-flanking sequences of the human LfR gene were cloned into a promoter-less pGL3 luciferase reporter and transiently transfected into an intestinal enterocyte model (Caco-2 cells). A fragment of - 299/+ 63 elicited the maximal promoter activity in transfected Caco-2 cells, suggesting that functional transcription factor binding sites appear in the region of - 299/+ 63. Bioinformatics analysis indicates that the - 299/+ 63 fragment contains two putative Sp1 binding sites. The promoter activity was significantly decreased when the Sp1 binding sites were mutated by site-directed mutagenesis. Additionally, the promoter activity was dramatically inhibited by treating ce...Continue Reading

References

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Citations

May 20, 2018·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Hans J VogelPiera Valenti

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Methods Mentioned

BETA
PCR
transfection
electrophoretic mobility shift
electrophoresis
protein assay
LightShift

Software Mentioned

Primer Express
ABI 7900HT
Prism Graph Pad

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