Glycosylation is essential for translocation of carp retinol-binding protein across the endoplasmic reticulum membrane

Devirgiliis, Chiara; Gaetani, S.; Apreda, Marianna; Bellovino, Diana

doi:10.1016/j.bbrc.2005.04.145

Cited by 4 publications

(2 citation statements)

References 22 publications

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“…These features might be important for both intracellular transport along the secretory pathway and decrease of rbp4 clearance in plasma (Devirgiliis et al 2005). Taken together, these findings provided evidences to sustain the idea that there was another mechanism of plasma retention in fish (Bellovino et al 2001).…”

Section: Discussionsupporting

confidence: 79%

Sequence analysis and expression regulation of rbp4 by 9-cis-RA in Megalobrama amblycephala

Huang

Chen

et al. 2014

Fish Physiol Biochem

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Retinol-binding protein 4 (rbp4) is mainly synthesized in the liver, where it binds retinol and then enters the bloodstream, delivering retinol to cells. The full-length cDNA coding rbp4 was cloned from Megalobrama amblycephala. The amino acid sequence showed strong homology with the homologues of other vertebrates, and all structural and functional domains were highly conserved. The mRNA levels in different tissues and development stages detected by quantitative real-time PCR revealed that M. amblycephala rbp4 was highly expressed in liver (P < 0.001), but the lower levels were also detected in eyes, kidney, intestine, and spleen. During the different development stages, the rbp4 mRNA appeared until 28 hours post-fertilization (hpf), underwent a slight drop, and then gradually increased after 50 hpf. In addition, the promoter sequence of M. amblycephala rbp4 was obtained using thermal asymmetric interlaced PCR. Two single nucleotide polymorphism sites (-385A>G and -329C>T) were found in the promoter. Transfection with recombinant plasmids of two different haplotypes (GT, AC) showed that 9-cis-retinoic acid (RA) increased the promoter activity, but the AC haplotype was more sensitive to RA.

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Section: Discussionsupporting

confidence: 79%

Sequence analysis and expression regulation of rbp4 by 9-cis-RA in Megalobrama amblycephala

Huang

Chen

et al. 2014

Fish Physiol Biochem

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“…However, glycosylation may modulate the function of OBPs as suggested by studies performed with other lipocalins. For example, it has been demonstrated that glycosylation is essential for efficient translocation of the carp RBP across the membrane of the endoplasmic reticulum (Devirgiliis et al ., 2005). Glycodelin, on the other hand, is found in three isoforms differing only in their glycan moieties and that are found in different secretions with distinct functions (Yeung et al ., 2006).…”

Section: Post‐translational Modificationsmentioning

confidence: 99%

Odorant‐binding proteins of mammals

Pelosi

Knoll

2021

Biological Reviews

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Odorant‐binding proteins (OBPs) of vertebrates belong to the lipocalin superfamily and perform a dual function: solubilizing and ferrying volatile pheromones to the olfactory receptors, and complexing the same molecules in specialized glands and assisting their release into the environment. Within vertebrates, to date they have been reported only in mammals, apart from two studies on amphibians. Based on the small number of OBPs expressed in each species, on their sites of production outside the olfactory area and their presence in biological fluids known to be pheromone carriers, such as urine, saliva and sexual secretions, we conclude that OBPs of mammals are specifically dedicated to pheromonal communication. This assumption is further supported by the observation that some OBPs present in biological secretions are endowed with their own pheromonal activity, adding renewed interest to these proteins. Another novel piece of evidence is the recent discovery that glycosylation and phosphorylation can modulate the binding activity of these proteins, improving their affinity to pheromones and narrowing their specificity. A comparison with insects and other arthropods shows a completely different scenario. While mammalian OBPs are specifically tuned to pheromones, those of insects, which are completely different in sequence and structure, include carriers for general odorants in addition to those dedicated to pheromones. Additionally, whereas mammals adopted a single family of carrier proteins for chemical communication, insects and other arthropods are endowed with several families of semiochemical‐binding proteins. Here, we review the literature on the structural and functional properties of vertebrate OBPs, summarize the most interesting new findings and suggest possible exciting future developments.

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Transthyretin and Retinol-Binding Protein: Implications in Fish Physiology

Gaetani

Bellovino

2009

Recent Advances in Transthyretin Evolution, Structure and Biological Functions

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Glycosylation is essential for translocation of carp retinol-binding protein across the endoplasmic reticulum membrane

Cited by 4 publications

References 22 publications

Sequence analysis and expression regulation of rbp4 by 9-cis-RA in Megalobrama amblycephala

Sequence analysis and expression regulation of rbp4 by 9-cis-RA in Megalobrama amblycephala

Odorant‐binding proteins of mammals

Transthyretin and Retinol-Binding Protein: Implications in Fish Physiology

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