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Gene Review:

LCN1 - lipocalin 1

Sus scrofa

Synonyms: VEG, VEGP

Burova, T.V. et al., Holzfeind, P. et al., Gamble, H.R. et al., Cepica, S. et al.

Cepica, Schröffel, Redl, Rohrer,

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High impact information on LCN1

The porcine LCN1 gene is approximately 4.6 kb in size and contains six protein-coding exons and a 3'-nontranslated exon [1].
Within the promoter region of the porcine LCN1 a putative TATA box, a CAAT box and two MRE motifs are found [1].
The same MRE motifs are conserved in the human LCN1 promoter, suggesting that they might be of relevance for LCN1 gene expression [1].
The structure of this porcine gene is highly similar, in terms of numbers of exons/introns, in size of exons and in intron phasing, to that of the human LCN1 and rat VEGP genes, thus supporting a very close evolutionary relationship of these genes [1].
The antigens were evaluated with sera from young pigs that had been fed 1-10,000 T. gondii oocysts of the VEG or GT-1 strains [2].

Biological context of LCN1

Thus, the elucidation of the functional behaviour of VEGP is closely related to the exhaustive purging of its endogenous ligands which otherwise very efficiently mask ligand binding sites of this protein [3].
All 5 recombinant antigens, as well as native antigen, detected antibody responses as soon as 3 wk after infection in pigs inoculated with 1 or 10 oocysts of the VEG strain [2].

Anatomical context of LCN1

Von Ebner gland protein (VEGP) and odorant-binding protein (OBP) were purified from porcine lingual epithelium and nasal mucosa, respectively [3].

Associations of LCN1 with chemical compounds

Isothermal titration calorimetry (ITC) did not detect the binding of either aspartame or denatonium saccharide to VEGP nor did it detect binding of 2-isobutyl-3-methoxypyrazine (IBMP) to OBP [3].

Other interactions of LCN1

The unfolding transition of VEGP is observed at extremely high temperatures (about 110 degrees C), which is unexpected for a protein with significant structural homology to OBP and other lipocalins [3].

Analytical, diagnostic and therapeutic context of LCN1

Both VEGP and OBP preparations were homogeneous as indicated by SDS-PAGE, isoelectric focusing, gel-filtration and electrospray mass spectrometry [3].
Linkage mapping of two TaqI PCR-RFLPs within intron 6 of the porcine gene (LCN1) encoding tear lipocalin/von Ebner's gland protein [4].

References

Structure and organization of the porcine LCN1 gene encoding Tear lipocalin/von Ebner's gland protein. Holzfeind, P., Merschak, P., Wojnar, P., Redl, B. Gene (1997) [Pubmed]
Use of recombinant antigens for detection of Toxoplasma gondii infection in swine. Gamble, H.R., Andrews, C.D., Dubey, J.P., Webert, D.W., Parmley, S.F. J. Parasitol. (2000) [Pubmed]
Why has porcine VEG protein unusually high stability and suppressed binding ability? Burova, T.V., Rabesona, H., Choiset, Y., Jankowski, C.K., Sawyer, L., Haertlé, T. Biochim. Biophys. Acta (2000) [Pubmed]
Linkage mapping of two TaqI PCR-RFLPs within intron 6 of the porcine gene (LCN1) encoding tear lipocalin/von Ebner's gland protein. Cepica, S., Schröffel, J., Redl, B., Rohrer, G.A. Anim. Genet. (1999) [Pubmed]

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