Chicken Oocytes and Somatic Cells Express Different Splice Variants of a Multifunctional Receptor

Bujo, Hideaki; Lindstedt, Ken A.; Hermann, Marcela; Dalmau, Lourdes Mola; Nimpf, Johannes; Schneider, Wolfgang J.

doi:10.1074/jbc.270.40.23546

Cited by 93 publications

(93 citation statements)

References 51 publications

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“…As described in numerous publications, VLDLR is massively expressed by growing oocytes and mediates the transport of VLDL, VTG, and other minor yolk components from the circulation into the growing germ cell (31). Earlier studies have demonstrated that granulosa cells express a splice variant of VLDLR that differs from the variant expressed in the oocyte by the presence of the O-linked sugar domain of the receptor (VLDLRϩ) (13). Here ( Fig.…”

Section: Resultsmentioning

confidence: 99%

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Signaling by the Extracellular Matrix Protein Reelin Promotes Granulosa Cell Proliferation in the Chicken Follicle

Eresheim

Leeb

Buchegger

et al. 2014

Journal of Biological Chemistry

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Background:The control of rapid proliferation of granulosa cells during chicken oocyte growth is unknown. Results: Reelin is expressed in theca cells and triggers disabled-1 phosphorylation in granulosa cells via ApoER2 and the VLDL receptor. Conclusion:The Reelin signaling pathway stimulates granulosa cell proliferation during folliculogenesis. Significance: This work demonstrates a novel function of Reelin.

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Section: Resultsmentioning

confidence: 99%

“…In another study, ApoER2 has been shown to be preferentially expressed in bovine dominant follicles when compared with subordinate follicles (12). A splice variant of VLDLR, which is the major player in yolk uptake by the oocyte, is also expressed in chicken granulosa cells (13).…”

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confidence: 99%

Signaling by the Extracellular Matrix Protein Reelin Promotes Granulosa Cell Proliferation in the Chicken Follicle

Eresheim

Leeb

Buchegger

et al. 2014

Journal of Biological Chemistry

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“…In Situ Hybridization-Tissue sections from ovarian follicles (small yellow, 5-6 mm in diameter) were prepared for in situ hybridization as described earlier (25,26). The sections (8 m) were hybridized overnight at 45°C with prehybridization solution containing 10% dextran sulfate and ϳ300 pg/l of the digoxigenin-labeled antisense or sense RNA probes.…”

Section: Methodsmentioning

confidence: 99%

“…Thus far, two oocyte-specific LDLR family members have been described. One is the chicken homologue of the mammalian so-called VLDL receptor, termed LR8 for its harboring 8 LDL receptor ligand binding repeats, that serves as a receptor for a broad spectrum of ligands (19,25). The other receptor is an LDL receptor-related protein (LRP) with an apparent M r of ϳ380,000 (28), here termed LRP380.…”

Section: Figmentioning

confidence: 99%

Multiple Involvement of Clusterin in Chicken Ovarian Follicle Development

Mahon¹,

Lindstedt²,

Hermann

et al. 1999

Journal of Biological Chemistry

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The interaction of the female germ cell with somatic cells during the development of the ovarian follicle in the chicken provides a prime system to study gene expression. Here, we have uncovered the involvement of clusterin, the function(s) of which is still poorly understood, in this complex process. As revealed by molecular cloning, chicken clusterin is a 428-residue protein that migrates at 70 kDa on SDS-polyacrylamide gel electrophoresis and possesses most of the structural features of its mammalian successors. However, in contrast to mammalian clusterin, the chicken protein appears not to be cleaved intracellularly into a disulfide-linked heterodimer; possibly as a consequence thereof, it is not secreted constitutively and is absent from the circulation, where most of clusterin is found in mammals. In the ovary, clusterin is a major product of the somatic granulosa cells, in a pattern correlating with the developmental phases of individual follicles. In that, transcript levels are high not only at onset of vitellogenesis, but also in atretic follicles and in the postovulatory follicle sac, i.e. in situations characterized by apoptotic events. Yolk of growing oocytes contains a 43-kDa truncated form of clusterin that does not appear to be synthesized within the oocyte. Rather, we here show for the first time that 70-kDa clusterin interacts not only with megalin, but also with two chicken oocyte-specific members of the low density lipoprotein receptor (LDLR) gene family. These receptors, termed LDLR-related protein with eight ligand binding repeats (LR8) and LDLR-related protein (380 kDa), likely internalize granulosa cell-derived 70-kDa clusterin, which may subsequently be processed to the 43-kDa product. Thus, chicken clusterin could serve as a marker for follicular atresia and resorption, and, based on its ability to bind several other proteins, it may serve as carrier for the receptor-mediated endocytosis into oocytes of components important for embryonic development, two hitherto unknown functions of this intriguing protein.

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“…Chicken oocytes and somatic cells express different splice variants of VLDLR (Bujo et al 1995). There have been no reports about the expression of the two VLDLR subtypes in waterfowl.…”

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confidence: 99%

Molecular cloning of the two very low-density lipoprotein receptor (VLDLR) subtypes in geese and the effect of overfeeding on their MRNA levels

Han¹,

Yao²,

Wang³

et al. 2009

Can. J. Anim. Sci.

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L. 2009. Molecular cloning of the two very-low-density lipoprotein receptor (VLDLR) subtypes in geese and the effect of overfeeding on their MRNA levels. Can. J. Anim. Sci. 89: 441Á448. The objectives of this study were to verify the existence of two subtypes of the very low-density lipoprotein receptor (VLDLR) gene in geese, to investigate the effect of overfeeding on the plasma concentration of triglycerides (TG) and the very low density lipoprotein (VLDL), the activity of lipoprotein lipase (LPL), and the mRNA level of VLDLR in Sichuan White geese and Landes geese. The results indicate that there are two subtypes of the VLDLR gene in geese, and that they share a high similarity with those of other species. The expression of VLDLR I and VLDLR II was found in both tissues examined. After overfeeding, the expression level of VLDLR I in adipose tissue showed about a onefold increase (PB0.05) in both breeds. Overfeeding induced a significant decrease of VLDLR I in skeletal muscle of both breeds, and a significant decrease of VLDLR II in Sichuan White geese (PB0.05), but an obvious increase of VLDLR II in Landes geese (PB0.05). In addition, overfeeding induced the increase of plasma VLDL, TG concentration and plasma LPL activity. It was concluded that VLDLR may participate in the metabolism of VLDL-TG by regulating the LPL-mediated TG hydrolysis in geese.

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Chicken Oocytes and Somatic Cells Express Different Splice Variants of a Multifunctional Receptor

Cited by 93 publications

References 51 publications

Signaling by the Extracellular Matrix Protein Reelin Promotes Granulosa Cell Proliferation in the Chicken Follicle

Signaling by the Extracellular Matrix Protein Reelin Promotes Granulosa Cell Proliferation in the Chicken Follicle

Multiple Involvement of Clusterin in Chicken Ovarian Follicle Development

Molecular cloning of the two very low-density lipoprotein receptor (VLDLR) subtypes in geese and the effect of overfeeding on their MRNA levels

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