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Duhagon, M. MiR-183-5p modulates cell adhesion in PrCa. Encyclopedia. Available online: https://encyclopedia.pub/entry/18975 (accessed on 18 December 2025).
Duhagon M. MiR-183-5p modulates cell adhesion in PrCa. Encyclopedia. Available at: https://encyclopedia.pub/entry/18975. Accessed December 18, 2025.
Duhagon, Maria. "MiR-183-5p modulates cell adhesion in PrCa" Encyclopedia, https://encyclopedia.pub/entry/18975 (accessed December 18, 2025).
Duhagon, M. (2022, January 28). MiR-183-5p modulates cell adhesion in PrCa. In Encyclopedia. https://encyclopedia.pub/entry/18975
Duhagon, Maria. "MiR-183-5p modulates cell adhesion in PrCa." Encyclopedia. Web. 28 January, 2022.
MiR-183-5p modulates cell adhesion in PrCa
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This entry is adapted from the peer-reviewed paper 10.3390/ncrna8010011

Prostate cancer is a major health problem worldwide. MiR-183 is an oncomiR and a candidate biomarker in prostate cancer, affecting various pathways responsible for disease initiation and progression. Overall, cell adhesion was uncovered as a major pathway controlled by miR-183 in prostate cancer, and ITGB1 was identified as a relevant mediator of this effect.

cancer microRNA focal adhesion miR-183 prostate ITGB1 TCGA

1. Introduction

Hsa-miR-183-5p.1 (5′-UAUGGCACUGGUAGAAUUCACU-3′), hereinafter referred to as miR-183, is coded by a member of a highly conserved gene cluster located at the 7q31-34 locus of the human chromosome [1]. Several studies have indicated that miR-183 is abnormally expressed in many tumors [2], showing both oncogenic and tumor suppressor functions, depending on the tissue type. In PrCa, miR-183 has consistently exhibited an oncogenic role, and its overexpression has been validated by mounting PrCa miRNA profiling studies [3][4][5][6][7][8][9][10][11][12]. Additionally, the expression of miR-183 in biopsies has been associated with disease status, diagnosis and prognosis in PrCa [3][4][6][12][13][14]. Ueno et al., have proposed that the inhibition of miR-183 reduces cell proliferation and migration by up-regulating DKK-3 and SMAD4 via WNT/β-catenin signaling [4]. These cellular effects were later confirmed by Dai et al., who identified TPM1 as another direct target of miR-183. The authors also proposed that exosomal-loaded miR-183 can provoke a similar regulation in neighboring cells through paracrine signaling [15]. On the other hand, the overexpression of the miR-183 full cluster was shown to regulate zinc homeostasis by diminishing the labile zinc pool and reducing zinc uptake and to directly repress hZIP1 transcript and protein through miR-182 and miR-96 repressive interaction (not mir-183) [11][16]. Since the decrease in zinc levels promotes disease progression, the study supports an oncogenic function of the cluster in PrCa. More recently, candidate tumor suppressor long non-coding RNAs (lncRNAs) were demonstrated to interact with miR-183 and compete for its target mRNAs binding in PrCa. 
The entry sought to discover the most relevant processes controlled by miR-183 through an unbiased transcriptomic approach using prostate cell lines and patient tissues to identify miR-183 responsive genes and pathways. Gain of function experiments, reporter gene assays, and transcript and protein measurements were conducted to validate predicted functional effects and protein mediators. 

2. Expression of MiR-183 Is Increased in Tumor Tissue and Associates with Worse Clinical Features in PrCa

MiR-183 upregulation in neoplastic tissue compared to normal tissue has been identified in the majority of PrCa miRNA studies, including the two largest published cohorts from the Memorial Sloan-Kettering Cancer Center (MSKCC) [17] and The Cancer Genome Atlas (PRAD-TCGA). Positive associations between miR-183 expression and PSA level at diagnosis and prior to radical prostatectomy and shorter time until recurrence were found in the MSKCC cohort (Table 1). 
Table 1. Expression of miR-183 in the MSKCC [17] and PRAD-TCGA cohorts and its association with clinical variables. The Mann–Whitney test was applied to assess the statistical significance of the difference between conditions.
Cohort Clinical Parameter Conditions Compared Ratio between Conditions p-Value
MSKCC Tissue type Primary tumor vs. Normal 3.3 ± 2.4 <0.0001
Metastasis vs. Normal 5.3 ± 4.1 <0.0001
PSA at diagnosis High vs. Low 1.5 ± 1.1 0.0182
Preoperative PSA High vs. Low 2.5 ± 1.9 <0.0001
Time until recurrence (month) Shorter vs. Longer 1.3 ± 1.9 0.0195
PRAD-TCGA Tissue type Primary tumor vs. Normal 4.3 ± 3.0 <0.0001
Biochemical recurrence YES vs. NO 1.3 ± 1.1 0.0404
Clinical T T3-T4 vs. T1-T2 1.5 ± 1.3 0.0020
Gleason Score 8-9-10 vs. 6-7 1.4 ± 1.0 <0.0001
Pathologic N N1 vs. N0 1.3 ± 0.9 0.0030

3. Overexpression of MiR-183 in Prostate Cells Causes a Decrease in Cell Adhesion In Vitro

The modulation of miR-183 expression after transfection was confirmed by qRT-PCR (Figure 1A). Quantitatively, miR-183-overexpressing DU145, LNCaP and RWPE-1 cells showed statistically significant decreases in adhesion, to 0.73 ± 0.06 (27%), 0,78 ± 0.05 (22%) and 0.79 ± 0.06 (21%), respectively, relative to the control cells (p-value < 0.01), while overexpressing PC-3 cells showed no significant change in adhesion relative to control cells in this experimental condition (Figure 1B). Since adhesion is a complex process, involving not only cell receptors binding to substrate ligands but also the modulation of intracellular signaling and the cytoskeleton, this entry sought to analyze the morphological spreading during adhesion by microscopic visualization of the actin cytoskeleton using phalloidin staining (Figure 1C). After 3 h of seeding, the overexpression of miR-183 produced a decrease in the area (p-value = 0.0374) and a tendency to increase the circularity (p-value = 0.1380) of the cells relative to the control transfected cells (Figure 1D). Therefore, both the quantitative and qualitative results were consistent with a reduction of the ability of the cells to adhere to the plate surface.

Figure 1. Effect of miR-183 on cell adhesion. (A) RT-qPCR measurement of miR-183 relative to RNAU6 (2−∆∆CT) 72 h after transfection of 20 nM miR-183 mimic or control RNAs in the indicated cell lines. (B) For the cell adhesion assay, the cells were harvested 72 h after transfection and seeded on cell culture surface-treated polystyrene 96-well plates, then allowed to adhere for 0.5 or 1 h (depending on the cell line), and the non-adherent cells were removed. Initial and remaining (attached) cells were quantified in independent wells using CellTiter-Glo (Promega). The fraction of attached cells in the miR-183 mimic relative to the control is shown as the mean ± standard deviation from at least three independent experiments. An unpaired t-test was applied to assess the statistical significance of the difference between conditions. (C) 72 h after transfection, the cells were harvested, plated on coverslips and allowed to spread for 3 h. The cells were then fixed, permeabilized and stained with Alexa Fluor 488-conjugated phalloidin to reveal the actin cytoskeleton. Images were captured with a Fluorescent Cell Imager using a monochrome camera and a magnification of 175×. Scale bars show 25 μm. Representative images are shown. (D) Cell area and circularity measured in cell adhesion assays of B were retrieved using ImageJ Software. Approximately 300 individual cells were analyzed for each cell line. A paired t-test was performed, considering the four cell lines as biological replicates, to assess the statistical significance between conditions. ** p-value < 0.1, ns = not significant.

4. ITGB1 Regulation by MiR-183 May by Mediated by a Direct Interaction with the ITGB1 3′UTR in Prostate Cancer

In order to study the molecular basis of the effect of miR-183 on cell adhesion, the direct candidate target gene ITGB1 was selected for further studies. In addition, the top enriched Wikipathway regulated by miR-183, EGF/EGFR, is known to crosstalk and share molecular components with the integrin signal [18]. Since the impact of ITGB1 in cancer progression is controversial, the clinical relevance of ITGB1 in PrCa was firstly studied. For that purpose, the expression of ITGB1 was analyzed in metastatic, primary tumor and normal prostate patient samples from MSKCC and PRAD-TCGA cohorts. It is found that ITGB1 transcript was significantly underexpressed in metastatic tissue compared to tumor and normal tissue in MSKCC samples (p-value ≤ 0.05 and ≤0.01, respectively) and in tumor tissue compared to normal tissue in PRAD-TCGA samples (p-value ≤ 0.0001) (Figure 2A,B), suggesting a tumor suppressor role of ITGB1 in PrCa. Furthermore, the expression of both miR-183 and ITGB1 in the PRAD-TCGA samples is negatively correlated (Spearman r2 = −0.3461, p-value < 0.0001), in agreement with a repressive interaction between them.

Figure 2. Expression of ITGB1 and its association with miR-183 expression in PrCa. (A,B) association of ITGB1 mRNA expression (RPKM) with tissue status in the MSKCC [28] and PRAD-TCGA cohorts, respectively. N = normal, T = primary tumor, M = metastatic tissue. A Mann–Whitney test was applied to assess the statistical significance of the difference between conditions. (C) Correlation between ITGB1 mRNA (Log2 RPKM) and miR-183 (Log2 RPM) expression in metastatic, primary tumor and normal tissue samples from the PRAD-TCGA project, evaluated by a Spearman correlation test. (D) Effect of miR-183 on ITGB1 expression in four PrCa cell lines. Cells were transfected with 20 nM of miR-183 mimic or control RNA. MiR-183 (normalized to RNAU6) and ITGB1 mRNA (normalized to BACT and GAPDH) levels (2−∆∆CT) were assessed by RT-qPCR 72 h after transfection in 2 technical replicates per cell line. ITGB1 protein levels (mean fluorescence intensity) were assessed by flow cytometry 72 h after transfection in at least three independent experiments per cell line. The results of the ratio between miR-183 mimic and control are shown as Log2. A paired t-test was performed considering the four cell lines as biological replicates to assess the statistical significance between conditions. p-value * <0.05, ** <0.01, **** <0.0001, ns = not significant.

To confirm the negative effect of miR-183 on ITGB1 expression in vitro, ITGB1′s mRNA and protein levels were quantified after the forced overexpression of miR-183 in normal and tumor prostate cell lines relative to the control RNA. The mRNA level of ITGB1 decreased 0.1 ± 0.0 (Log2 −2.8, 90%) in DU145, 0.2 ± 0.0 (Log2 −2.6, 80%) in LNCaP, 0.1 ± 0.0 (Log2 −2.9, 90%) in PC-3 and 0.1 ± 0.0 (Log2 3.6, 90%) in RWPE-1 upon miR-183 mimic transfection (p-value < 0.0001). Accordingly, the protein level of ITGB1, measured by flow cytometry with an anti-ITGB1 antibody, was significantly reduced to 0.6 ± 0.0 (Log2 −0.8, 40%) in DU145, 0.6 ± 0.1 (Log2 −0.8, 40%) in LNCaP, 0.4 ± 0.1 (Log2 −1.6, 60%) in PC-3 and 0.2 ± 0.1 (Log2 −2.7, 80%) in RWPE-1 (p-value = 0.0094) (Figure 2D).

The entry next sought to investigate if this repressive effect is due to a direct sequence-specific complementary interaction between ITGB1 mRNA and miR-183 in the prostate tissue. It was initially visualized that the mapping distribution of AGO-PAR-CLIP reads containing the 6-mer miR-183 complementary site along the 3′UTR of the ITGB1 gene from Hamilton et al. [19]. TargetscanHuman [20] predicts three sites for miR-183 in the 3′UTR of ITGB1: a 7merm8 site conserved among vertebrates (position 623–629 nt), an 8-mer site poorly conserved among vertebrates (position 1012–1019 nt) and a 6-mer site (position 83–87 nt). The most covered region of the ITGB1 3′ UTR bearing the 6-mer site complementary to the miR-183 seed in the AGO-PAR-CLIP dataset of PrCa cell lines turned out to be the 7merm8 binding site of miR-183 conserved among vertebrates (GUGCCAU) (Figure 3A). The T-C transition identified in that AGO footprint occurs in 38% of the reads at the U base of ITGB1 transcript, corresponding with position 9 of the miRNA (unpaired), consistent with the characteristics of the PAR-CLIP reads of prototypical miRNA interaction sites (which occur at U positions between the 8 and 13th 5’of the interaction site [21]). This mapping pattern supports a direct interaction of miR-183 on this ITGB1 seed site in prostate cells. Thus, a 140 bp region of the ITGB1 3´UTR comprising this site was cloned into a luciferase reporter plasmid (Figure 3A) and mutations in the 7merm8 conserved putative binding site were introduced for miR-183 (Figure 3B). The luciferase activity of the wild type (wt) ITGB1 3′UTR was significantly reduced to 0.73 when miR-183 was overexpressed by transfection in RWPE-1 cells compared to the transfection of a control RNA (p-value < 0.001). Furthermore, the mutation of three nucleotides in the putative binding site of miR-183 caused a partial loss of this repression to 0.85 (44% recovery, p-value < 0.05) (Figure 3C).

Figure 3. Validation of the direct miR-183 and ITGB1 mRNA interaction in PrCa. (A) Mapping of prostate cell line reads along the putative binding site of miR-183 on ITGB1′s 3′UTR extracted from AGO-PAR-CLIP RNA-seq data [31]. The base identity is represented by four colors, as indicated. Perfect base matches and mismatches (due to base substitutions caused by the photoactivatable ribonucleoside crosslinking) are represented as gray and colored bars, respectively. Forward and reverse primers used to clone the miR-183 binding site of the ITGB1 3′UTR in pmiRGLO are indicated by arrows. The image is a modified screenshot of the IGV Software [42]. (B) Base pairing between miR-183 and the conserved miR-183 putative binding site on ITGB1 wild type and mutated 3′UTR cloned in pmirGLO for reporter gene assays. (C) Reporter gene assay using pmiRGLO, bearing the region of the 3′UTR of ITGB1 with the miR-183 wild type or mutated site, co-transfected with miR-183 mimic or control RNA in the RWPE-1 cell line. Luciferase activity was measured 48 h after transfection. The mean ± SD of four independent experiments is shown. A two-way ANOVA was applied to test the statistical significance of the differences between conditions. p-value * <0.05, ** <0.01, **** <0.0001.

Overall, the results indicate that a negative regulation of ITGB1 by miR-183 may be operative in prostate cancer patient tissue, as well as in cell lines, and might contribute to prostate cancer biology.

5. The Inhibition of Cell Adhesion Provoked by miR-183 May Be Due to a Reduction of Focal Adhesions Mediated by ITGB1 Downregulation

Aiming to evaluate if the modulation of cell adhesion caused by miR-183 (Figure 2) is mediated by ITGB1, this work first incubated untransfected prostate cells with a monoclonal antibody against ITGB1 known to block cell adhesion [22], or an antibody against the nuclear transcription factor TWIST as a control, and measured cell adhesion to the cell culture plate. A decrease in cell adhesion of 0.43 ± 0.05 (57%) in DU145, 0.76 ± 0.06 (24%) in PC-3 and 0.66 ± 0.09 (34%) in RWPE-1 was observed (Figure 4A), resembling the effect of miR-183 overexpression. LNCaP cells did not change cell adhesion under these experimental conditions (Figure 4A). These results indicate that ITGB1 blockade produces a similar effect to miR-183 overexpression in this experimental setting, making it a suitable mediator of the miR-183 adhesive phenotype.

Figure 4. Effect of miR-183 on the number of focal adhesions. (A) Effect of ITGB1 blockade on cell adhesion. Untransfected cells were incubated with an antibody against ITGB1 (ab24693 Abcam) or TWIST (ab50887 Abcam), seeded on polystyrene 96-well plates and allowed to adhere for 0.5 or 1 h (depending on the cell line). Non-adherent cells were removed, and the remaining cells were quantified using CellTiter-Glo (Promega). The results of at least three independent replicates were normalized to the control and are shown as means ± SD. An unpaired t-test was applied to assess the statistical significance of the difference between conditions. (B) Immunocytochemistry of vinculin of prostate cells overexpressing miR-183. Seventy-two hours after transfection of 20 nM of miR-183, the cells were fixed, permeabilized and immunostained for vinculin using an Alexa Fluor 488-conjugated secondary antibody. Nuclei and filamentous actin were counterstained with DAPI and phalloidin-Alexa Fluor 568, respectively. The images were collected on a confocal microscope using a 63X oil immersion objective. Scale bars show 25 μm. Representative images are shown. (C) Effect of miR-183 on focal adhesion density. Quantification of focal adhesions per cell in vinculin immunocytochemical images of the DU145 and RWPE-1 cell lines. Images were processed using ImageJ. A Mann–Whitney test was applied to test the statistical significance of the difference between conditions. p-value ** <0.01, *** <0.001, **** <0.0001.

The interaction between the ECM and the integrins results in the assembly of specialized structures called focal adhesions (FA). They are highly specialized domains of the plasma membrane, consisting of clusters of integrins that form the closest contact with matrix proteins on the extracellular side, and represent the sites where converging actin filaments terminate and interact with integrins on the cytoplasmic side [23]. A variety of biological process involving changes in cell contractility require a change in the number and distribution of focal adhesions [24]. Interestingly, one of the most common integrins found in focal adhesions is α5β1 [25]. Considering that miR-183 and ITGB1 have opposite effects on cell adhesion and meet criteria for a miRNA/target RNA pair, the entry then investigated if miR-183 affects the number of the focal adhesions in the prostate cell line models. For this purpose, the entry measured FA using an antibody against the scaffold focal adhesion protein vinculin in DU145 and RWPE-1 cells overexpressing miR-183, employing identical conditions as those of the experiments shown in Figure 2. Indeed, a decrease was found in the number of FA per cell in cells overexpressing miR-183 relative to those overexpressing the control RNA (Figure 4B,C). This observation suggests that miR-183-mediated reduction of cell adhesion could be due to a reduction of the focal adhesions, which is consistent with a downregulation of ITGB1.

6. Conclusions

The entry have confirmed the oncogenic expression pattern of miR-183 in the largest PrCa cohorts publicly available (and in South American patients), and found positive associations with clinical parameters that were not yet reported (PSA prior to radical prostatectomy, shorter time until recurrence, biochemical recurrence, clinical T stage and pathologic N status). Therein, a positive association was also found between miR-183 expression and PSA at diagnosis and biopsy, pathologic Gleason Score and pathological T stage, that has been reported before  [3][4]. Cell attachment, spreading assays and focal adhesion quantification of miR-183-overexpressing cells confirmed the predicted reduction in cell adhesion. ITGB1 was validated as a major target of repression by miR-183 as well as a mediator of cell adhesion in response to miR-183. The reporter gene assay and PAR-CLIP read mapping suggest that ITGB1 may be a direct target of miR-183. The negative correlation between miR-183 and ITGB1 expression in prostate cancer cohorts supports their interaction in the clinical set. Overall, cell adhesion was uncovered as a major pathway controlled by miR-183 in prostate cancer, and ITGB1 was identified as a relevant mediator of this effect.

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Subjects: Biochemistry & Molecular Biology
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