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26 October 2022 Expression analysis of POSTN gene in ovine follicles
Jiapeng Lin, Chunjie Liu, Liqin Wang, Ying Chen, Xiaolin Li, Yangsheng Wu, Juncheng Huang
Author Affiliations +

The purpose of this study was to explore the potential expression regularity of POSTN in ovarian tissue. In this study, the uterus, ovarian follicles, heart, liver, spleen, lung, kidney, and muscle tissues of Merino sheep (10) were collected and detected by Western blot, real-time quantitative polymerase chain reaction, immunohistofluorescence, and fluorescence staining, respectively. The expression of POSTN in various organizations was analyzed. The results showed that the POSTN in Merino sheep had close homology with Bos mutus and Bos taurus. The expression of POSTN was detected in the uterus, follicle, heart, liver, spleen, lung, kidney, and muscle tissue, among which the expression of POSTN was highest in ovarian tissue. In addition, the expression of POSTN gradually increased with the increase of follicle diameter, among which POSTN was highly expressed in the granulosa cells (GCs) of follicles. Meanwhile, POSTN were distributed throughout the nucleus and cytoplasm of GCs, suggesting that POSTN may be involved in the regulation of follicle development.


Follicle development begins with the activation of resting follicles, then undergoes the growth and development of the follicles, and is accompanied by the sequential differentiation of oocytes (Oo) and surrounding somatic cells, which ultimately leads to the maturation of the follicles and the occurrence of ovulation (Ryu et al. 2018). The occurrence of these events is often affected by changes in hormones. It has been recognized that a variety of hormones have a regulatory effect on follicular development, such as pregnant mare serum gonadotropin (Chen et al. 2020) and luteinizing hormone (LH) (Gal et al. 2014), and follicle-stimulating hormone (Filatov et al. 2017).

Hormonal changes are critical to the formation of extracellular matrix protein (ECM) (Nagyova 2018). The matrix can play a role in the fluid dynamics of a tissue, either by providing osmotic forces that might be important for follicular fluid formation or by filtering soluble materials, possibly across the follicular basal lamina. It can also provide rigid or elastic mechanical support of tissues. In addition, nutrients and hormones and other extracellular signals are often required to traverse the matrix to reach target cells (Irving-Rodgers and Rodgers 2005). The matrix has the ability to bind a variety of growth factors or their binding proteins. Many of the different types of matrix in the ovarian follicles have been reviewed recently. These include those associated with the follicular basal lamina, the stromal matrix of the thecal layers, the matrix of the thecal blood vessels, and that of the cumulus–oocyte complex (COC) (Ouni et al. 2020). Therefore, ECM has a regulatory effect on follicular development (Wolak et al. 2021). Moreover, a large number of studies have shown that the regulation of ECM on follicle development is regulated by a variety of genes and transcription factors (Khan et al. 2011). However, the molecular mechanisms regulating the developmental transition of a dominant preovulatory follicle into an ovulatory follicle are not fully understood.

POSTN (osteoblast-specific factor 2, OSF-2) was first discovered in the ECM protein secreted in mouse osteoblasts and precursor cells (Sugiura et al. 1995). POSTN participates in a variety of life regulation processes, such as promoting the migration of human bone marrow-derived mesenchymal stem cells (Schmidt 2018). In addition, POSTN is also regulated by microRNAs to manage fibrosis progression (Chen et al. 2020), and POSTN activates the PI3K/AKT pathway and induces epithelial–mesenchymal transition to promote the migration and invasion of ovarian cancer cells (Yue et al. 2021). POSTN activates the Wnt/β-catenin signaling pathway to regulate the cell proliferation in GC-1 SPG cells (Li et al. 2021). In addition, recent studies indicate that POSTN may be involved in the growth of porcine granule cells (Kulus et al. 2020). However, the expression of POSTN in sheep has not been reported. Therefore, this study analyzes the correlation between POSTN and follicular development through quantitative detection of POSTN in various tissues and organs of sheep, to provide a theoretical basis for future research on follicular development.

Materials and methods

Reagents and antibodies

Follicle-stimulating hormone (FSH) was purchased from Bioniche (Canada); Dulbecco's phosphate-buffered saline (DPBS) and DMEM/F12 medium were purchased from Gibco (USA); penicillin–astreptomycin and fetal bovine serum were obtained from Gibco Products; Luteinizing hormone (LH) was purchased from Vetoquinol (France); Estradiol (E2), Bovine serum albumin (BSA), and polyvinyl alcohol were all purchased from Sigma Company (Germany); TRIzol, PrimeScript™ RT reagent kit, and SYBR® Premix Ex Taq reagents were purchased from Takara Company (Japan); Revert Aid First Strand cDNA Synthesis Kit was purchased from Thermo Scientific (USA); Polymerase chain reaction (PCR) product purification kit were purchased from TaKaRa Company (Japan); qRT-PCR primers were synthesized by Shenggong Bioengineering Co., Ltd. (Shanghai, China); pMD19-T vector and RNA extraction reagent were purchased from RNAiso Plus; terminal transferase and dATP were purchased from Dalian TaKaRa; and rabbit polyclonal POSTN antibody (19899-1-AP) was purchased from Wuhan Sanying (China). The recovery kit was purchased from Tiangen Company (China). RIPA lysate (P0013B), PMSF (ST506), and BCA protein concentration determination kit (P0010) were purchased from Biyuntian (China).

Experimental animal model and sample preparations

The study was performed in accordance with the Principles of the Care and Use of Laboratory Animals and China Council on Animal Care. All experiments were approved by the Institutional Animal Care and Use Committee of the University. Unmated adult Merino sheep (1.5–2.5 years old) were euthanized (n = 10). The ovaries, heart, liver, spleen, lungs, kidneys, and muscles were collected and rinsed with 37 °C normal saline and sent back to the laboratory for follow-up experiments.

Cloning of POSTN gene

Total RNA was extracted from follicle tissue by the TRIzol method, and its OD230, OD206, and OD208 were detected by UV spectrophotometer and then reverse transcribed to synthesize the first strand after electrophoresis detection. One pair of primers was designed with reference to the sheep cDNA sequence (GenBank accession number: XM_004012111.5)—upstream primer: 5′-TACCTTCAAAGAAATCCCCAT-3′; downstream primer: 5′-GGTGAAACGGTAACTGAAG-3′. PCR amplification was performed using the first strand of cDNA synthesized by reverse transcription as a template. The PCR product was purified, cloned by TA, identified by double restriction digestion, and then sent to Shanghai Sangon Technology Co., Ltd. for sequencing.

Bioinformatics analysis of POSTN gene cDNA

Sheep POSTN nucleic acid and amino acid sequences were analyzed using NCBI online BLAST ( The sequences of Homo sapiens (accession: AAI06711), Rattus norvegicus (accession: AIS73061), Bos taurus (accession: AAS02052), Gallus gallus (accession: AAT72403), Callithrix jacchus (accession: JAB23422), Danio rerio (accession: AAI62274), Pan troglodytes (accession: JAA40911), Bos mutus (accession: ELR48035), Ailuropoda melanoleuca (accession: EFB16759), Salmo trutta (accession: XP_029626198), Chiroxinphia lanceolata (accession: XP_032536357), Bos indicus × Bos taurus (accession: XP_027413176), and Theropithecus gelada (accession: XP_025198) were analyzed using the MEGA software. The phylogenetic tree was constructed using the neighbor-joining method.

Follicles with different diameters and corpus luteum isolation

In the ultra-clean workbench, sheep ovaries were randomly collected, the connective tissue was removed to clean the area to isolate follicles, and they were rinsed at least three times with sterile PBS with DEPC water. The follicles were divided into large follicles (>5.5 mm), medium follicles (3.5–5.4 mm), and small follicles (2–3.4 mm) by detecting the diameter of the follicles, and the follicular fluid of different follicles was collected (). The corpus luteum of the ovary was cut into small pieces about 2 mm in size with sterilized scissors, and they were placed in sterile PBS prepared with diethypyrocarbonate (DEPC) water, washed three times, put in liquid nitrogen, and frozen for subsequent experiments.

Collection of GCs, TCs, COC, and oocyte in follicles of different diameters

COCs and follicular membrane cells (theca cells (TCs)) from follicular fluid of different diameters were isolated. After culturing COCs in vitro in mature fluid for 22–24 h, COCs were treated with 100 IU/mL hyaluronidase for 1–2 min and pipetted several times to get Oo and cumulus cells (CCs). There are three replicates in each group, and each replicate contains about 50–120 Oo cells and the collected CCs were mixed into a pool, and 1 mL RNAiso Plus was added separately and stored at −80 °C for later use. TCs were rinsed with PBS prepared with DEPC water for three times to wash away the granulosa cells (GCs) on the inner wall of the follicular membrane, and 1000 rmp centrifuge to remove the supernatant. There are three replicates in each group (large, medium, and small follicles), and each replicate contains 10 membranes separated from follicles.


The ovarian tissue was soaked in 4% formaldehyde, and paraffin-embedded after different concentrations of alcohol (70%, 80%, 90%, 95%, 100%, and 100%) and dimethylbenzene. The paraffin-embedded tissue was cut into 5 µm sections. The slices were then placed in an oven at 70 °C overnight. The sections were deparaffinized twice in xylene (5 min each time) and then immersed in 100%, 100%, 95%, 90%, 80%, and 70% alcohol for 5 min. The slices were placed in sodium citrate buffer (0.021% citric acid + 0.029% sodium citrate) for 5 min to boil for antigen retrieval. The paraffin sections were then stained using the immunohistochemistry kit (MXB Biotechnologies) according to the instructions. POSTN antibody (Protentech, China, 19899-1-AP) (1:50) was used for section staining. The section was developed using DAB color development kit (MXB Biotechnologies), and then the results were observed using a fluorescence microscope (Olympus, BX53FL).


The cells were washed with PBS, fixed with an immunostaining fixative for 1 h, and then incubated with 0.1% Triton X-100 for 30 min. Then the cells were blocked with 5% donkey serum for 2 h. The cells were then incubated overnight at 4 °C with POSTN (Protentech, China, 19899-1-AP) (1:50) primary antibody. The cells were washed with PBS and stained with donkey anti-rabbit 488. The results were observed using an immunofluorescence microscope.

Western blot

Tissues and cells were lysed with NP40, and then the protein concentration was detected with the BCA protein concentration detection kit and used for aliquoting. Protein samples were aliquoted into 30 µg/15 µL and boiled for 5 min. Then 4% stacking gel and 12% separating gel were used to separate the proteins in the samples. The protein was then transferred to the polyvinylidene fluoride (PVDF) membrane and blocked with 5% skimmed milk, followed by blocking with the following primary antibody overnight. Subsequently, the PVDF membrane was washed with TBS + Tween (TBST) and incubated with the murine monoclonal primary antibody POSTN (Protentech, China, 19899-1-AP) (1:1000) and secondary antibody (Boster, BA1055/BA1051, USA) for 1 h, and then visualized with enhanced chemiluminescence (ECL) hypersensitive luminescent solution.

Real-time quantitative PCR

Total RNA was extracted from sheep follicles, corpus luteum, and cells in each follicle using TRIzol reagent according to the manufacturer's instructions. Total RNA was reverse transcribed into cDNA. Real-time quantitative PCR was performed on a CFX96 system using SYBR Green Supermix. β-actin was used as a reference gene, and the amount of mRNA was calculated with the 2–△△CT method. All real-time quantitative PCR analyses were repeated three times. POSTN primers are shown in Table 1.

Table 1.

Sequences of primers for POSTN.


Statistical analysis

The experiments were repeated at least three times, as detailed in the figure legends. Experimental data were presented as mean ± standard, and statistics were calculated for one-way repeated measure ANOVA using the Prism 5.0 statistical software (GraphPad Software, San Diego, CA, USA). Significant differences were determined by comparing means using the Bonferroni post-test. Values of p  < 0.05 were considered to be statistically significant. Follicles are defined as large follicles (>5.5 mm), medium follicles (3.5–5.4 mm), and small follicles (2–3.4 mm) according to their diameters.


Cloning and bioinformatics analysis of POSTN cDNA sequence

To analyze the characteristics of the POSTN gene, we first analyzed the cluster of differentiation (CD) region of the POSTN gene. The results showed that the sequence of the cloned PCR product was about 2000 bp (  Fig. S1 (cjas-2021-0036_suppla.docx)). Using ORF Finder analysis, it was found that the CDs were 1557 bp in size ( Fig. S2 (cjas-2021-0036_suppla.docx)), encoding a protein consisting of 518 amino acids ( Fig. S3 (cjas-2021-0036_suppla.docx)), and the protein encoded by the cloned CDs was sheep deletion POSTN isoform X3 ( Fig. S4 (cjas-2021-0036_suppla.docx)). Molecular phylogenetic tree analysis found that the cloned POSTN protein has close homology with B. mutus and B. taurus (Fig. 1).

Fig. 1.

The phylogenetic tree of POSTN in ovine.


POSTN gene expression analysis in sheep tissues

The qRT-PCR method was used to detect the relative expression of POSTN gene in eight tissues, including heart, liver, spleen, lung, kidney, muscle, uterus, and ovary. Figure 2 shows that the POSTN gene is expressed in uterus, ovarian large, medium, and small follicles, heart, liver, spleen, lung, kidney, muscle, and especially in the ovary (p < 0.05).

Fig. 2.

The expression mRNA of POSTN in different tissues of ovine. Note: Different letters indicate significant differences between groups (p < 0.05).


Expression of POSTN in follicles and follicular cells of different diameters

To study the expression pattern of POSTN in the development of sheep follicles, qRT-PCR, Western blot, and immunohistochemical staining were used to analyze the expression of POSTN mRNA and protein in antral follicles, corpus luteum, and follicles of different sizes. The results showed that the expression of POSTN gene and protein gradually increased with the increase in follicle diameter (p < 0.05). Meanwhile, the mRNA expression of POSTN in medium and large follicles was significantly higher than that of the corpus luteum (p < 0.05) (Figs. 3A–3C). To further study the expression of POSTN in the development of sheep follicles, qRT-PCR was used to detect POSTN mRNA in GCs, CCs, TCs, Oo, and membrane cells in antral follicles of different sizes. The results showed that POSTN gene is higher in GCs in large follicles, followed by Oo and CCs, while TC expression is relatively low (p < 0.05). The expression of POSTN in CCs and TCs of large, medium, and small follicles had no significant difference (p > 0.05) (Fig. 3D). Moreover, immunohistochemistry was used to analyze the expression of POSTN protein in follicular cells. The results showed that POSTN protein was highly expressed in corpus luteum tissue and primary follicles, secondary follicles, and Oo, CCs, GCs, and TCs with antral follicles (Fig. 3E).

Fig. 3.

The expression and distribution of POSTN in cells of different antrum follicles. (A) Western blot was used to detect the expression of POSTN in follicles of different sizes. Different lowercase letters indicate significant differences between groups (p < 0.05). (B) ImageJ was used to quantify the immunoblot bands of POSTN, and β-actin was used as an internal reference and the ratio was calculated. Different letters indicate significant differences between groups (p < 0.05). (C) Real-time PCR analysis showed the expression of POSTN in small follicle (2–3.4 mm), medium follicle (3.5–5.4 mm), large follicle (>5.5 mm), and corpus follicle. Different capital letters indicate extremely significant differences between groups (p < 0.01). (D) Real-time PCR analysis showed the expression of POSTN in GCs, TCs, CCs, and Oo. Lowercase letters indicate the comparison of the same type of cells in different follicles. A indicates that there is no difference between MGCs, CCs, Oo, and TCs in small follicles. B indicates that there is no difference between MGCs, CCs, Oo, and TCs in the medium follicle. C and D indicate comparisons between MGCs, CCs, Oo, and TCs in large follicles. Different letters indicate significant differences (p < 0.05). (E) Protein in the ovine ovary illustrates (a) primordial follicle, (b) primary follicle, (c) secondary follicle, (d) small antral follicle, (e) a large antral follicle, (f) COC of a large antral follicle, (g) corpus luteum, and (h) negative control.


Position and expression of POSTN in GCs

To further study the role of POSTN in GCs, we then examined the expression of POSTN in GCs using immunofluorescence assays. The results showed that POSTN was expressed in the nucleus and cytoplasm of GCs (Fig. 4).

Fig. 4.

The distribution and expression of POSTN of ovine GCs. Note: GCs were cultured under complete medium. (A) GCs were observed under a microscope. (B) The cell nucleus was restained with DAPI (blue). (C) The POSTN antibody (green) was used for immunofluorescence staining of GCs. (D) DAPI, POSTN, and GC cell images are merged. Scale, 50 µm.



In this study, POSTN CDs and their homology with other species were analyzed, and the expression of POSTN in the ovary was detected. Our experimental results showed that the region of POSTN CDs consists of 518 amino acids in Merino sheep and has high homology to POSTN in B. mutus and B. taurus. Moreover, POSTN is expressed in uterus, ovary, heart, liver, spleen, lung, kidney, and muscle tissues, with the highest expression in the ovary. Meanwhile, the expression level of POSTN in follicles increased with the increase of follicle diameter. The above results indicate that POSTN may be involved in the development of follicles.

POSTN is a homologous protein with insect cell adhesion molecule fasciclin I, which is located on chromosome 13 and contains a typical signal sequence and four cysteines in human (Yu et al. 2021). Due to the existence of a variety of C-terminal domains, POSTN undergoes alternative splicing during the transcription process, resulting in the transcript containing four different spliceosomes (Uchida et al. 2017). As a secreted protein, POSTN has various biological functions. Current studies have shown that POSTN has a characteristic molecular structure containing an integrin-binding domain; so it can bind to a variety of integrin receptors (avβ3, αvβ5, and α6β4), thereby affecting the protein regulation of intracellular signaling pathways associated with PI3K/AKT and focal adhesion kinase (FAK). Thus, the protein plays a role in many cell migrations as well as in the epithelial–mesenchymal transition of cells, and these studies suggest that the interaction of POSTN with signaling factors is critical for cell survival function. At the same time, a large number of studies have identified the expression of POSTN in various animal tissues and organs. However, the expression of POSTN in sheep has not yet been reported. In this study, POSTN cDNA sequence was successfully cloned in sheep ovary. Meanwhile, our data showed that CDS region lacks isoform X3 in the POSTN of the cloned sheep. The gene of POSTN in sheep has extremely high homology with B. mutus and B. taurus, which indicates that POSTN is highly conservative and may play an important role in animal physiology and pathology.

Previous studies have shown that POSTN is expressed in collagen-rich fibrous connective tissues such as bone, periodontal ligament, skin, heart, and endometrium. And we also got the same conclusion that POSTN is widely expressed in heart, liver, spleen, kidney, muscle, uterus, and ovary. Meanwhile, the specific expression of POSTN gene mRNA was significantly upregulated in ovarian tumor tissue, and it participated in the ECM-mediated cell adhesion signaling pathway and was regulated by estrogen (Ismail et al. 2000; Syed et al. 2005). In this study, the expression level of POSTN mRNA was significantly higher than other tissues (heart, liver, spleen, lung, kidney, muscle, and uterus). It showed that POSTN plays a regulatory function in sheep tissues and organs, especially for the development of ovary. Recent studies have found that bone morphogenetic protein, transforming growth factor beta (TGF-β), and connective tissue growth factor 2 induce the expression of POSTN protein (Ranjan et al. 2021). TGF-β1, as an important pro-fibrotic growth factor, plays a crucial role in the occurrence of intrauterine adhesions (Aukkarasongsup et al. 2013). Such factors had activated endometrial stromal cells to produce large amounts of POSTN. On the one hand, the high spatiotemporal expression of POSTN may force POSTN to use its own EMI domain to combine with collagen I and fibronectin to complete the entire process of fibril formation in endometrial tissue. On the other hand, POSTN can also bind BMP-1 through the FSAI region. The LOX activity is further stimulated, and then the network effect of collagen and elastic fibers is formed, forming an ECM with strong toughness and tight arrangement. It helps connect tissue structures and regulate cellular physiological activities. However, the specific mechanism of POSTN in this fibrosis process remains to be studied. This study found that POSTN gene was highly expressed in sheep uterine tissue, suggesting that POSTN gene may be involved in the formation of sheep endometrium. The uterus is an important place for egg development, and the elasticity and flexibility of its inner wall provide the necessary environment for fetal development (Zhou et al. 2012). Therefore, the high expression of POSTN gene in sheep uterus may be closely related to the formation of connective tissue and smooth muscle fibers in the uterus.

The POSTN gene is involved in the regulation, selection, and maturation of human and broiler follicles (Tungmahasuk et al. 2018). In addition, POSTN interacts with the ECM to activate intracellular activation of PI3K/AKT and FAK signaling pathways. Similar functions and activation are also seen in follicular GCs, where integrins are also expressed (Gillan et al. 2002). It can be seen that ECM, integrin, and POSTN genes may all be involved in a series of important life activities such as ovarian development, embryo transfer, and ovulation (Jing et al. 2016). In this study, POSTN gene was expressed in sheep follicles of different sizes, mainly in healthy follicles and Oo, while the expression of POSTN was less in small follicles, and the expression of POSTN also increased with the development of follicles. This suggests that POSTN may be involved in follicular development in sheep.


This research was financially supported by the National Natural Science Foundation of China (No. 31860646).

Data availability

All raw data are available from the corresponding authors.

Author contributions

Conceptualization: JL

Data curation: JL

Formal analysis: JL

Investigation: JL, CL, LW, YC, XL, YW, JH

Methodology: JL

Resources: JL

Software: JL

Validation: JL

Visualization: JL

Writing – original draft: JL

Supplementary material

Supplementary data are available with the article at

Supplementary Material 1 (DOCX / 738 KB).



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© 2022 The Author(s)
Jiapeng Lin, Chunjie Liu, Liqin Wang, Ying Chen, Xiaolin Li, Yangsheng Wu, and Juncheng Huang "Expression analysis of POSTN gene in ovine follicles," Canadian Journal of Animal Science 103(1), 66-72, (26 October 2022).
Received: 3 April 2021; Accepted: 20 June 2022; Published: 26 October 2022
follicle development
granulosa cells
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