Characterization of the oligomerization and ligand-binding properties of recombinant rat lipocalin 11

Gu, Yina; Qiang, Liu; Chen, Peiyan; Guo, Cheng; Liu, Yan; Zhao, Yiming; Zhang, Yonglian; Lin, Donghai

doi:10.1016/j.bbapap.2012.08.018

Cited by 4 publications

(2 citation statements)

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“…Therefore, it is possible that the natural presentation of Can f 4 in dog dander also includes oligomers, a property shared with some other lipocalins. 36 , 39 , 40 To some extent, this property can also be a factor underlying the sensitivity of Can f 4 to denaturation.…”

Section: Discussionmentioning

confidence: 99%

IgE Reactivity of the Dog Lipocalin Allergen Can f 4 and the Development of a Sandwich ELISA for Its Quantification

Rytkönen‐Nissinen

Saarelainen

Randell

et al. 2015

Allergy Asthma Immunol Res

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PurposeDivergent results on the IgE reactivity of dog-allergic subjects to Can f 4 have been reported. The aim of this study was to evaluate the significance of Can f 4 in dog allergy and to develop an immunochemical method for measuring Can f 4 content in environmental samples.MethodsWe purified the natural dog allergen Can f 4 from a dog dander extract by monoclonal antibody-based affinity chromatography and generated its variant in a recombinant form. Sixty-three dog-allergic patients and 12 nonallergic control subjects were recruited in the study. The IgE-binding capacity of natural Can f 4 and its recombinant variant was assessed by ELISA, immunoblotting, and skin prick tests (SPT).ResultsEighty-one percent of the dog-allergic patients showed a positive result to the immunoaffinity-purified natural Can f 4 in IgE ELISA, but only 46% in IgE immunoblotting. Respective results with the recombinant Can f 4 variant were 54% and 49%. SPT results reflected those obtained in ELISA and immunoblotting. The overall IgE reactivity of the immunoaffinity-purified natural Can f 4 was found to depend strongly on the integrity of the allergen's conformation. A sandwich ELISA based on monoclonal antibodies was found to be functional for measuring Can f 4 in environmental samples.ConclusionsCan f 4 is a major allergen of dog together with Can f 1 and Can f 5. In combination with other dog allergens, it improves the reliability of allergy tests in dog allergy.

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Section: Discussionmentioning

confidence: 99%

IgE Reactivity of the Dog Lipocalin Allergen Can f 4 and the Development of a Sandwich ELISA for Its Quantification

Rytkönen‐Nissinen

Saarelainen

Randell

et al. 2015

Allergy Asthma Immunol Res

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“…The solution structure assay and fluorescence titration experiments indicated the high binding affinity for all-trans retinoic acid of the rLCN12 protein, implying that rLCN12 could be involved in retinoic acid transport in the epididymis [ 12 , 13 ] . Recombinant rLCN11 might contain multiple hydrophobic binding sites for ligand binding and work as a dimeric chemoreception protein in male reproduction [14] . rLcn9 , a proximal caput epididymis-specific lipocalin, is regulated by luminal testicular factors and deposited onto the postacrosomal domain of caput epididymal sperm, indicating its potential roles in sperm maturation [15] …”

Section: Introductionmentioning

confidence: 99%

Identification, characterization and expression analysis of <italic>rLcn13</italic>, an epididymal lipocalin in rats

Yao¹,

Xie²,

Wan³

et al. 2023

ABBS

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As the essential tissue for sperm maturation and storage, the epididymis secretes a number of tissue-specific proteins to exert its functions. Among these proteins, epididymal lipocalins have been intensively studied because of their epididymis-specific expression pattern and clustered genomic organization. In this study, rLcn13 , a member of the rat epididymal lipocalin family, is identified and elaborately characterized. The cDNA sequence of rLcn13 consists of 719 nucleotides and encodes a 176 amino-acid protein with a predicted N-terminal signal peptide of 19 amino acids. rLcn13 shares a similar genomic structure and predicted 3D protein structure with other lipocalin family members. A recombinant rLCN13 mature peptide of 157 amino acids is expressed and purified, which is used to raise a polyclonal antibody against rLCN13 with high specificity and sensitivity. Northern blot, western blot, and immunohistochemistry assays reveal that rLcn13 is an epididymis-specific gene which is expressed predominantly in the initial segment and proximal caput epididymis and influenced by androgen. The rLCN13 protein is modified by N-glycosylation and secreted into the epididymal lumen, and then binds to the acrosome region of the sperm. Our data demonstrate that rLcn13 exhibits a specific temporospatial expression pattern and androgen dependence, indicating its potential roles in sperm maturation.

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Expression, purification and characterisation of the recombinant possum lipocalin vulpeculin

Lucarelli¹,

Colbert²,

Cumming³

et al. 2022

Biochimica et Biophysica Acta (BBA) - General Subjects

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Characterization of the oligomerization and ligand-binding properties of recombinant rat lipocalin 11

Cited by 4 publications

References 40 publications

IgE Reactivity of the Dog Lipocalin Allergen Can f 4 and the Development of a Sandwich ELISA for Its Quantification

IgE Reactivity of the Dog Lipocalin Allergen Can f 4 and the Development of a Sandwich ELISA for Its Quantification

Identification, characterization and expression analysis of <italic>rLcn13</italic>, an epididymal lipocalin in rats

Expression, purification and characterisation of the recombinant possum lipocalin vulpeculin

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Characterization of the oligomerization and ligand-binding properties of recombinant rat lipocalin 11

Cited by 4 publications

References 40 publications

IgE Reactivity of the Dog Lipocalin Allergen Can f 4 and the Development of a Sandwich ELISA for Its Quantification

IgE Reactivity of the Dog Lipocalin Allergen Can f 4 and the Development of a Sandwich ELISA for Its Quantification

Identification, characterization and expression analysis of &lt;italic&gt;rLcn13&lt;/italic&gt;, an epididymal lipocalin in rats

Expression, purification and characterisation of the recombinant possum lipocalin vulpeculin

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Identification, characterization and expression analysis of <italic>rLcn13</italic>, an epididymal lipocalin in rats