Expression of Osteopontin (OPN) mRNA in Bovine Ovarian Follicles and Corpora Lutea

Brunswig-Spickenheier, Bärbel; Mukhopadhyay, A. K.

doi:10.1046/j.1439-0531.2003.00413.x

Cited by 13 publications

(6 citation statements)

References 56 publications

(53 reference statements)

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“…The comparison of fish OP‐L protein with mammalian osteopontin expression patterns indicates that both proteins may play a similar role in calcified tissues and gonads, for example in bone remodeling by mediating osteoclast attachment to the mineralized bone matrix during resorption [23,34–36] and/or in matrix mineralization by regulating calcium phosphate crystal deposition [26,37–39], and in gonads by preventing calcium‐containing‐crystal aggregation[40,41]. The restricted tissue distribution of the OP‐L gene transcript also indicates that fish protein may be less pleiotropic than that from mammals.…”

Section: Discussionmentioning

confidence: 99%

“…However, we cannot rule out the fact that differences in gene expression in soft tissues could be related to different developmental or physiological stages of the specimens used in both studies, as evidenced by the regulation of OP-L gene expression in brook trout ovary during ovulation [19]. The comparison of fish OP-L protein with mammalian osteopontin expression patterns indicates that both proteins may play a similar role in calcified tissues and gonads, for example in bone remodeling by mediating osteoclast attachment to the mineralized bone matrix during resorption [23,[34][35][36] and ⁄ or in matrix mineralization by regulating calcium phosphate crystal deposition [26,[37][38][39], and in gonads by preventing calcium-containing-crystal aggregation 26 [40,41]. The restricted tissue distribution of the OP-L gene transcript also indicates that fish protein may be less pleiotropic than that from mammals.…”

Section: Op-l Protein Plays a Role In The Process Of Mineralizationmentioning

confidence: 99%

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Identification of an osteopontin‐like protein in fish associated with mineral formation

Fonseca¹,

Laizé²,

Valente

et al. 2007

The FEBS Journal

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Fish has been recently recognized as a suitable vertebrate model and represents a promising alternative to mammals for studying mechanisms of tissue mineralization and unravelling specific questions related to vertebrate bone formation. The recently developed Sparus aurata (gilthead seabream) osteoblast‐like cell line VSa16 was used to construct a cDNA subtractive library aimed at the identification of genes associated with fish tissue mineralization. Suppression subtractive hybridization, combined with mirror orientation selection, identified 194 cDNA clones representing 20 different genes up‐regulated during the mineralization of the VSa16 extracellular matrix. One of these genes accounted for 69% of the total number of clones obtained and was later identified as theS. aurata osteopontin‐like gene. The 2138‐bp full‐length S. aurata osteopontin‐like cDNA was shown to encode a 374 amino‐acid protein containing domains and motifs characteristic of osteopontins, such as an integrin receptor‐binding RGD motif, a negatively charged domain and numerous post‐translational modifications (e.g. phosphorylations and glycosylations). The common origin of mammalian osteopontin and fish osteopontin‐like proteins was indicated through an in silico analysis of available sequences showing similar gene and protein structures and was further demonstrated by their specific expression in mineralized tissues and cell cultures. Accordingly, and given its proven association with mineral formation and its characteristic protein domains, we propose that the fish osteopontin‐like protein may play a role in hard tissue mineralization, in a manner similar to osteopontin in higher vertebrates.

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Section: Discussionmentioning

confidence: 99%

Section: Op-l Protein Plays a Role In The Process Of Mineralizationmentioning

confidence: 99%

Identification of an osteopontin‐like protein in fish associated with mineral formation

Fonseca¹,

Laizé²,

Valente

et al. 2007

The FEBS Journal

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show abstract

“…To select a stable reference or housekeeper gene, analysis of putative reference genes was carried out using the geNorm version 3.4 Excel (Microsoft, Redmond, WA) add-in (99). In this study, housekeeping genes analyzed included those for ␤-actin (4), ubiquitin (67), glyceraldehyde phosphate dehydrogenase (14), 18S ribosomal RNA (24), and peptidylprolyl isomerase A (74). The gene stability measure M that geNorm determines is defined as the average pairwise variation V of a particular gene with all other potential reference genes (99).…”

Section: Real-time Quantitative Reverse Transcription Pcrmentioning

confidence: 99%

mRNA expression of genes regulating oxidative phosphorylation in the muscle of beef cattle divergently ranked on residual feed intake

Kelly

Waters

McGee

et al. 2011

Physiological Genomics

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Our objective was to evaluate the effects of phenotypic ranking on residual feed intake (RFI) on the transcription of genes 1) involved in the respiratory chain complex and 2) coding for transcriptional factors regulating mitochondrial biogenesis, across two contrasting diet types. Beef heifers (n = 86) fed a diet comprising 70:30 concentrate-corn silage [low forage (LF)] over a 82-day period were ranked on RFI. The 10 highest (feed inefficient, high-RFI) and 10 lowest (feed efficient, low-RFI) ranking animals were selected for the current study. Biopsies of the M. longissimus dorsi were harvested following initial selection (LF diet) and again following a 6 wk period while the animals were offered a high-forage (HF) grass silage-only diet. Real-time PCR was used to quantify mRNA transcripts of 17 genes associated with cellular energetic efficiency. The mRNA expression of UCP3 tended to be upregulated (2.2-fold, P = 0.06) for the high-RFI compared with the low-RFI animals. mRNA transcripts coding for the transcription factor PGC-1α was 1.7-fold higher (P = 0.01) in low compared with high-RFI animals. A phenotype × diet interaction was evident for the abundance of ANT1 mRNA transcript, with greater (P = 0.04) expression levels detected in the low-RFI phenotype during the HF period, but no difference (P = 0.50) between phenotypes during the LF period. A phenotype × diet interaction was also evident for COX II with greater expression levels detected (P = 0.04) in the low compared with the high RFI phenotype while on LF but not the HF diet (P = 0.22). These data suggest an association between cellular energetic efficiency and RFI in cattle.

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“…Furthermore, a novel ovarian protein, sharing sequence similarity with mammalian and chicken OPNs, was detected in trout periovulatory ovary (Bobe & Goetz 2001). OPN transcripts were also detected in bovine ovarian follicles and corpus lutea (Brunswig-Spickenheier & Mukhopadhyay 2003). Recently, results of a detailed study have indicated that OPN is localized in bovine luteal cells during the luteal phase of the estrous cycle and is involved in the development and regression of the corpus luteum (Poole et al 2013).…”

Section: Introductionmentioning

confidence: 99%

Gonadotropin regulation and role of ovarian osteopontin in the periovulatory period

Kuwabara

Katayama

Tomiyama

et al. 2014

Journal of Endocrinology

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Osteopontin (OPN), a secreted glycoprotein, has multiple physiological functions. This study investigated the regulation and roles of OPN in the mouse ovary during the periovulatory stages. Immature female mice were treated with pregnant mare serum gonadotropin (PMSG) and human chorionic gonadotropin (hCG) to simulate follicle maturation and ovulation. In situ hybridization and real-time RT-PCR were performed to assess expression of Opn in the periovulatory ovary. Granulosa cells (GCs) from PMSGprimed immature mice were cultured with or without hCG in the presence or absence of OPN, and effects on expression of Opn, progesterone synthesis, and vascular endothelial growth factor (VEGF) signaling were assessed by real-time RT-PCR, ELISA, and western blotting analysis. Opn transcripts were significantly upregulated 3 h after hCG treatment, followed by a peak at 16 h, and the transcripts localized to GCs. Incubation with hCG significantly increased quantities of Opn transcripts in GCs and OPN levels in the culture medium at 12 and 24 h. Furthermore, OPN treatment caused a significant increase in the levels of Star protein, P 450 cholesterol side-chain cleavage enzyme (p450scc), 3-betahydroxysteroid dehydrogenase (Hsd3b), and progesterone in the culture medium. OPN treatment promoted Vegf expression in GCs, which was significantly suppressed by a phosphoinositide 3-kinase (PI3K) inhibitor. In addition, OPN treatment stimulated phosphorylation of AKT, a downstream PI3K signaling molecule. In conclusion, expression of Opn was upregulated in mouse ovarian GCs in response to a gonadotropin surge through epidermal growth factor receptor signaling, which enhances progesterone synthesis and Vegf expression during the early-luteal phase.

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Expression of Osteopontin (OPN) mRNA in Bovine Ovarian Follicles and Corpora Lutea

Cited by 13 publications

References 56 publications

Identification of an osteopontin‐like protein in fish associated with mineral formation

Identification of an osteopontin‐like protein in fish associated with mineral formation

mRNA expression of genes regulating oxidative phosphorylation in the muscle of beef cattle divergently ranked on residual feed intake

Gonadotropin regulation and role of ovarian osteopontin in the periovulatory period

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