Receptor-Ligand Interaction between Vitellogenin Receptor (VtgR) and Vitellogenin (Vtg), Implications on Low Density Lipoprotein Receptor and Apolipoprotein B/E

Li, Ankang; Murali, Sadasivam; Ding, Jeak Ling

doi:10.1074/jbc.m205067200

Cited by 130 publications

(108 citation statements)

References 46 publications

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“…For example, the LBD repeats mediate the interaction between receptor and lipoproteins in mammals [47,48]. In tilapia, it has been reported that the first three ligand-binding repeats of Vtgr interact with the amino-terminal region of Vtg [7]. In general, Vtgr has eight LBD repeats (LR8), one additional repeat than in human LDLRs; however, vtgr cDNAs from fish are more FIG.…”

Section: Discussionmentioning

confidence: 99%

“…With the advent of cloning technology, identification and sequencing of the vgtr has been reported for a handful of fish species, which maintain highly conserved regions; however, two cDNA isoforms have been reported in rainbow trout [3,6], blue tilapia [7], and sole [8]. The isoforms consist of a larger cDNA sequence containing an O-glycan domain and a shorter one devoid of this region.…”

Section: Introductionmentioning

confidence: 99%

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Identification and Transcriptional Modulation of the Largemouth Bass, Micropterus salmoides, Vitellogenin Receptor During Oocyte Development by Insulin and Sex Steroids1

Domínguez¹,

Quattro²,

Denslow³

et al. 2012

Biology of Reproduction

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Fish vitellogenin synthesized and released from the liver of oviparous animals is taken up into oocytes by the vitellogenin receptor. This is an essential process in providing nutrient yolk to developing embryos to ensure successful reproduction. Here we disclose the full length vtgr cDNA sequence for largemouth bass (LMB) that reveals greater than 90% sequence homology with other fish vtgr sequences. We classify LMB Vtgr as a member of the low density lipoprotein receptor superfamily based on conserved domains and categorize as the short variant that is devoid of the O-glycan segment. Phylogenetic analysis places LMB Vtgr sequence into a well-supported monophyletic group of fish Vtgr. Real-time PCR showed that the greatest levels of LMB vtgr mRNA expression occurred in previtellogenic ovarian tissues. In addition, we reveal the effects of insulin, 17beta-estradiol (E 2 ), and 11-ketotestosterone (11-KT) in modulation of vtgr, esr, and ar mRNAs in previtellogenic oocytes. Insulin increased vtgr expression levels in follicles ex vivo while exposure to E 2 or 11-KT did not result in modulation of expression. However, both steroids were able to repress insulin-induced vtgr transcript levels. Coexposure with insulin and E 2 or of insulin and 11-KT increased ovarian esr2b and ar mRNA levels, respectively, which suggest a role for these nuclear receptors in insulin-mediated signaling pathways. These data provide the first evidence for the ordered stage-specific expression of LMB vtgr during the normal reproductive process and the hormonal influence of insulin and sex steroids on controlling vtgr transcript levels in ovarian tissues.insulin, oocyte development, steroid hormones, vitellogenin, vitellogenin receptor

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Identification and Transcriptional Modulation of the Largemouth Bass, Micropterus salmoides, Vitellogenin Receptor During Oocyte Development by Insulin and Sex Steroids1

Domínguez¹,

Quattro²,

Denslow³

et al. 2012

Biology of Reproduction

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“…The N-sheet domain is the predicted receptor binding site of Vgs and presumably essential for the uptake of the protein by oocytes (19). In honey bees, the N-sheet is under strong negative selection (i.e.…”

Section: Discussionmentioning

confidence: 99%

“…The Vg domain consists of two subdomains: the N-sheet domain and the ␣-helical domain. N-sheet alone has been identified as the Vg receptor-binding region in fish (19). The role of the ␣-helical domain is less clear.…”

mentioning

confidence: 99%

Vitellogenin Recognizes Cell Damage through Membrane Binding and Shields Living Cells from Reactive Oxygen Species

Havukainen

Münch

Baumann

et al. 2013

Journal of Biological Chemistry

106

120

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Background: Vitellogenin is a central regulator of honey bee life span by largely unknown mechanisms. Results: Honey bee vitellogenin has membrane affinity that is connected to cell damage recognition and antioxidant function. Conclusion: Membrane binding documents a new molecular behavior among vitellogenins. Significance: Vitellogenins are widespread phylogenetically, and their molecular behavior is essential for fitness traits in many animals.

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“…To date, only a limited number of studies have examined the relationships between receptor proteins and their Vtg ligands. Recently, based on an experiment using a yeast 2-hybrid system (Y2H), the affinity between VtgAb and the Vtg receptor (an orthologue of mammalian very-low-density lipoprotein (VLDL) receptor) was confirmed in tilapia, and the binding regions were revealed to be located in the LvH region of VtgAb and on a ligand-binding repeat of the Vtg receptor [121]. This finding is in agreement with our experimental results, which biochemically demonstrated the presence of a binding region on Lv that binds to the Lr8-type Vtg receptor [65].…”

Section: Future Concernsmentioning

confidence: 99%

Vitellogenesis and choriogenesis in fishes

2016

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Receptor-Ligand Interaction between Vitellogenin Receptor (VtgR) and Vitellogenin (Vtg), Implications on Low Density Lipoprotein Receptor and Apolipoprotein B/E

Cited by 130 publications

References 46 publications

Identification and Transcriptional Modulation of the Largemouth Bass, Micropterus salmoides, Vitellogenin Receptor During Oocyte Development by Insulin and Sex Steroids1

Identification and Transcriptional Modulation of the Largemouth Bass, Micropterus salmoides, Vitellogenin Receptor During Oocyte Development by Insulin and Sex Steroids1

Vitellogenin Recognizes Cell Damage through Membrane Binding and Shields Living Cells from Reactive Oxygen Species

Vitellogenesis and choriogenesis in fishes

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