The Role of Gene Expression in Stress Urinary Incontinence: An Integrative Review of Evidence
Abstract
:1. Introduction
2. Materials and Methods
2.1. Study Design
2.2. Eligibility Criteria
- Gene expression analysis of SUI women relative to healthy women;
- Experiments on samples from human tissue;
- Gene expression detection and quantification using molecular techniques of polymerase chain reaction (PCR), immunohistochemistry, Western blot, and immunofluorescence staining;
- Articles written in the English language.
2.3. Information Sources and Search Strategies
2.4. Study Selection and Data Extraction
2.5. Data Items
2.6. Risk of Bias in Individual Studies
3. Results
3.1. Study Selection
3.2. Study Characteristics and Results of Individual Studies
Author, Year | Study Design | Study Population | Tissue Analyzed | Analytical Methods Used | Results Summary |
---|---|---|---|---|---|
Chen, 2006 | Case control | n = 26 women; 14 cases and 12 controls | Vaginal wall | Immunofluorescence cell staining, microarray data analysis, PCR, Western blot | SKALP, KRT16, COL17A1, PKP1 were perpetually classified as upregulated genes by both MAS 5.0 and RMA when assessed through analytical methods and as discussed in the study. |
Wen, 2007 | Case control | n = 62 women; 31 cases and 31 controls | Vaginal wall | Immunofluorescence cell staining, PCR, Western blot | BGN, DCN, and FMOD were found to be placed in vaginal tissue along with connective matter (via immunofluorescence cell staining). DCN mRNA was 3-fold higher in the case group in the proliferative phase and 8 times higher in the secretory phase. FMOD mRNA was 2.5 times lower in the case group in the proliferative phase. BGN showed no difference in both phases. Via Western blot: BGN and DCN showed higher density in the case group in the secretory phase, while FMOD showed lower density in the case group in the secretory phase. |
Tong, 2010 | Case control | n = 17 women; 9 cases and 8 controls | Vaginal wall | Microarray data analysis, PCR, Western blot | The four most relevant pathways identified were: SNARE containing STX10, GOSR1 genes Nerve degenerating pathway via GRB2, APOE genes Inositol functioning including GBA gene (APOE, GRB2, GOSR1, and GBA were selected) |
Liu, 2014 | Case control | n = 26 women; 13 cases and 13 controls | Vaginal wall | miRNA microarray data analysis, PCR, Western blot | 12 miRNAs were differentially expressed (p < 0.05) (5 upregulated, 7 downregulated). The differential expression of these 12 miRNAs predicated 3 miRNA-mRNA pairs for BICD2, GRB2, and STAT3 genes |
Chen, 2020 | Case control | N/A; Samples were obtained from prostate hyperplasia surgeries in men and bladder outlet obstruction and bladder neck sclerosis surgeries in women. | Urethra | Immunofluorescence cell staining, PCR, Western blot | The upregulation of ANO1 in urethral smooth muscle cells results in doubling the expression in women and female mice compared to cells from men and male mice. |
Cartwright, 2021 | Case control | n = 8979 women; genome-wide association study in 3 independent discovery cohorts of European women. | Urinary bladder | Microarray analysis, RT-PCR | The authors classified two genetic variants associated with SUI. The first, rs138724718, is located near MARCO, functioning as a host protection. The second, rs34998271, is positioned near EDN1, a major smooth muscle contractor. |
Full Name | Gene Symbol | Functions |
---|---|---|
Anoctamin 1 | ANO1 |
|
Apolipoprotein E | APOE |
|
Biglycan | BGN |
|
Protein bicaudal D homolog 2 | BICD2 |
|
Collagen type XVII alpha 1 chain | COL17A1 |
|
Decorin | DCN |
|
Endothelin 1 | EDN1 |
|
Fibromodulin | FMOD |
|
Glucosylceramidase beta | GBA |
|
Golgi SNAP receptor complex member 1 | GOSR1 |
|
Growth-factor-receptor-bound protein 2 | GRB2 |
|
Keratin 16 | KRT16 |
|
Macrophage receptor with collagenous structure | MARCO |
|
Plakophilin 1 | PKP1 |
|
Skin-derived, protease inhibitor 3 (peptidase inhibitor 3) | SKALP (PI3) |
|
Signal transducer and activator of transcription 3 | STAT3 |
|
Syntaxin 10 | STX10 |
|
3.3. Upregulated Genes
3.3.1. Anoctamin 1 (ANO1)
3.3.2. Apolipoprotein E (APOE)
3.3.3. Biglycan (BGN)
3.3.4. Protein Bicaudal D Homolog 2 (BICD2)
3.3.5. Collagen Type XVII Alpha 1 Chain (COL17A1)
3.3.6. Decorin (DCN)
3.3.7. Endothelin 1 (EDN1)
3.3.8. Golgi SNAP Receptor Complex Member 1 (GOSR1)
3.3.9. Growth-Factor-Receptor-Bound Protein 2 (GRB2)
3.3.10. Keratin 16 (KRT16)
3.3.11. Macrophage Receptor with Collagenous Structure (MARCO)
3.3.12. Plakophilin 1 (PKP1)
3.3.13. Skin-Derived Antileukoproteinase (SKALP/PI3)
3.3.14. Signal Transducer and Activator of Transcription 3 (STAT3)
3.3.15. Syntaxin 10 (STX10)
3.4. Downregulated Genes
3.4.1. Fibromodulin (FMOD)
3.4.2. Glucosylceramidase Beta (GBA)
4. Discussion
5. Conclusions
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Conflicts of Interest
References
- Abrams, P.; Cardozo, L.; Fall, M.; Griffiths, D.; Rosier, P.; Ulmsten, U.; Van Kerrebroeck, P.; Victor, A.; Wein, A. The Standardisation of Terminology in Lower Urinary Tract Function: Report from the Standardisation Sub-Committee of the International Continence Society. Urology 2003, 61, 37–49. [Google Scholar] [CrossRef]
- Nie, X.-F.; Ouyang, Y.-Q.; Wang, L.; Redding, S.R. A Meta-Analysis of Pelvic Floor Muscle Training for the Treatment of Urinary Incontinence. Int. J. Gynecol. Obstet. 2017, 138, 250–255. [Google Scholar] [CrossRef]
- Nyström, E.; Sjöström, M.; Stenlund, H.; Samuelsson, E. ICIQ Symptom and Quality of Life Instruments Measure Clinically Relevant Improvements in Women with Stress Urinary Incontinence: ICIQ-UI SF and ICIQ-LUTSqol Correlation to PGI-I. Neurourol. Urodynam. 2015, 34, 747–751. [Google Scholar] [CrossRef] [Green Version]
- Fjerbæk, A.; Søndergaard, L.; Andreasen, J.; Glavind, K. Treatment of Urinary Incontinence in Overweight Women by a Multidisciplinary Lifestyle Intervention. Arch. Gynecol. Obstet. 2020, 301, 525–532. [Google Scholar] [CrossRef] [PubMed]
- Hunskaar, S.; Lose, G.; Sykes, D.; Voss, S. The Prevalence of Urinary Incontinence in Women in Four European Countries. BJU Int. 2004, 93, 324–330. [Google Scholar] [CrossRef] [PubMed]
- Lim, R.; Liong, M.L.; Leong, W.S.; Khan, N.A.K.; Yuen, K.H. Magnetic Stimulation for Stress Urinary Incontinence: Study Protocol for a Randomized Controlled Trial. Trials 2015, 16, 279. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Peng, L.; Zeng, X.; Shen, H.; Luo, D. Magnetic Stimulation for Female Patients with Stress Urinary Incontinence, a Meta-Analysis of Studies with Short-Term Follow-Up. Medicine 2019, 98, e15572. [Google Scholar] [CrossRef]
- Papanicolaou, S.; Pons, M.E.; Hampel, C.; Monz, B.; Quail, D.; von der Schulenburg, M.G.; Wagg, A.; Sykes, D. Medical Resource Utilisation and Cost of Care for Women Seeking Treatment for Urinary Incontinence in an Outpatient Setting. Maturitas 2005, 52, 35–47. [Google Scholar] [CrossRef]
- DeLancey, J.O.L. Structural Support of the Urethra as It Relates to Stress Urinary Incontinence: The Hammock Hypothesis. Am. J. Obstet. Gynecol. 1994, 170, 1713–1723. [Google Scholar] [CrossRef]
- Hannestad, Y.S.; Rortveit, G.; Daltveit, A.K.; Hunskaar, S. Are Smoking and Other Lifestyle Factors Associated with Female Urinary Incontinence? The Norwegian EPINCONT Study. BJOG 2003, 110, 247–254. [Google Scholar] [CrossRef]
- Diokno, A.C.; Brock, B.M.; Herzog, A.R.; Bromberg, J. Medical Correlates of Urinary Incontinence in the Elderly. Urology 1990, 36, 129–138. [Google Scholar] [CrossRef] [PubMed]
- Hannestad, Y.S.; Lie, R.T.; Rortveit, G.; Hunskaar, S. Familial Risk of Urinary Incontinence in Women: Population Based Cross Sectional Study. BMJ 2004, 329, 889–891. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Mushkat, Y.; Bukovsky, I.; Langer, R. Female Urinary Stress Incontinence--Does It Have Familial Prevalence? Am. J. Obstet. Gynecol. 1996, 174, 617–619. [Google Scholar] [CrossRef] [PubMed]
- Elia, G.; Bergman, J.; Dye, T.D. Familial Incidence of Urinary Incontinence. Am. J. Obstet. Gynecol. 2002, 187, 53–55. [Google Scholar] [CrossRef]
- Altman, D.; Forsman, M.; Falconer, C.; Lichtenstein, P. Genetic Influence on Stress Urinary Incontinence and Pelvic Organ Prolapse. Eur. Urol. 2008, 54, 918–922. [Google Scholar] [CrossRef] [PubMed]
- McKenzie, P.; Rohozinski, J.; Badlani, G. Genetic Influences on Stress Urinary Incontinence. Curr. Opin. Urol. 2010, 20, 291–295. [Google Scholar] [CrossRef]
- Tong, J.; Lang, J.; Zhu, L. Microarray Analysis of Differentially Expressed Genes in Vaginal Tissues in Postmenopausal Women. The Role of Stress Urinary Incontinence. Int. Urogynecol J. 2010, 21, 1545–1551. [Google Scholar] [CrossRef]
- Page, M.J.; McKenzie, J.E.; Bossuyt, P.M.; Boutron, I.; Hoffmann, T.C.; Mulrow, C.D.; Shamseer, L.; Tetzlaff, J.M.; Akl, E.A.; Brennan, S.E.; et al. The PRISMA 2020 Statement: An Updated Guideline for Reporting Systematic Reviews. BMJ 2021, 372, n71. [Google Scholar] [CrossRef]
- Lo, C.K.-L.; Mertz, D.; Loeb, M. Newcastle-Ottawa Scale: Comparing Reviewers’ to Authors’ Assessments. BMC Med. Res. Methodol. 2014, 14, 45. [Google Scholar] [CrossRef] [Green Version]
- Chen, B.; Wen, Y.; Zhang, Z.; Guo, Y.; Warrington, J.A.; Polan, M.L. Microarray Analysis of Differentially Expressed Genes in Vaginal Tissues from Women with Stress Urinary Incontinence Compared with Asymptomatic Women. Hum. Reprod. 2006, 21, 22–29. [Google Scholar] [CrossRef] [Green Version]
- Wen, Y.; Zhao, Y.Y.; Li, S.; Polan, M.L.; Chen, B.H. Differences in MRNA and Protein Expression of Small Proteoglycans in Vaginal Wall Tissue from Women with and without Stress Urinary Incontinence. Hum. Reprod. 2007, 22, 1718–1724. [Google Scholar] [CrossRef] [Green Version]
- Liu, X.; Lang, J.; Wu, S.; Cheng, L.; Wang, W.; Zhu, L. Differential Expression of MicroRNAs in Periurethral Vaginal Wall Tissues of Postmenopausal Women with and without Stress Urinary Incontinence. Menopause 2014, 21, 1122–1128. [Google Scholar] [CrossRef] [PubMed]
- Chen, D.; Meng, W.; Shu, L.; Liu, S.; Gu, Y.; Wang, X.; Feng, M. ANO1 in Urethral SMCs Contributes to Sex Differences in Urethral Spontaneous Tone. Am. J. Physiol. Ren. Physiol. 2020, 319, F394–F402. [Google Scholar] [CrossRef] [PubMed]
- Cartwright, R.; Franklin, L.; Tikkinen, K.A.O.; Kalliala, I.; Miotla, P.; Rechberger, T.; Offiah, I.; McMahon, S.; O’Reilly, B.; Lince, S.; et al. Genome-Wide Association Study Identifies Two Novel Loci Associated with Female Stress and Urgency Urinary Incontinence. J. Urol. 2021, 206, 679–687. [Google Scholar] [CrossRef] [PubMed]
- Hunziker, M.; O’Donnell, A.-M.; Gosemann, J.; Alvarez, L.A.; Puri, P. Altered Anoctamin-1 and Tyrosine Phosphorylation in Congenital Ureteropelvic Junction Obstruction. J. Pediatr. Surg. 2020, 55, 1621–1625. [Google Scholar] [CrossRef]
- Marais, A.D. Apolipoprotein E in Lipoprotein Metabolism, Health and Cardiovascular Disease. Pathology 2019, 51, 165–176. [Google Scholar] [CrossRef]
- Yang, X.; Chen, S.; Shao, Z.; Li, Y.; Wu, H.; Li, X.; Mao, L.; Zhou, Z.; Bai, L.; Mei, X.; et al. Apolipoprotein E Deficiency Exacerbates Spinal Cord Injury in Mice: Inflammatory Response and Oxidative Stress Mediated by NF-ΚB Signaling Pathway. Front. Cell. Neurosci. 2018, 12, 142. [Google Scholar] [CrossRef] [PubMed]
- Roedig, H.; Nastase, M.V.; Wygrecka, M.; Schaefer, L. Breaking down Chronic Inflammatory Diseases: The Role of Biglycan in Promoting a Switch between Inflammation and Autophagy. FEBS J. 2019, 286, 2965–2979. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Miguez, P.A. Evidence of Biglycan Structure-Function in Bone Homeostasis and Aging. Connect. Tissue Res. 2020, 61, 19–33. [Google Scholar] [CrossRef]
- Oates, E.C.; Rossor, A.M.; Hafezparast, M.; Gonzalez, M.; Speziani, F.; MacArthur, D.G.; Lek, M.; Cottenie, E.; Scoto, M.; Foley, A.R.; et al. Mutations in BICD2 Cause Dominant Congenital Spinal Muscular Atrophy and Hereditary Spastic Paraplegia. Am. J. Human. Genet. 2013, 92, 965–973. [Google Scholar] [CrossRef] [Green Version]
- Huang, X.; Fan, D. A Novel Mutation of BICD2 Gene Associated with Juvenile Amyotrophic Lateral Sclerosis. Amyotroph. Lateral Scler. Front. Degener. 2017, 18, 454–456. [Google Scholar] [CrossRef] [PubMed]
- Jonsson, F.; Byström, B.; Davidson, A.E.; Backman, L.J.; Kellgren, T.G.; Tuft, S.J.; Koskela, T.; Rydén, P.; Sandgren, O.; Danielson, P.; et al. Mutations in Collagen, Type XVII, Alpha 1 (COL17A1) Cause Epithelial Recurrent Erosion Dystrophy (ERED). Hum. Mutat. 2015, 36, 463–473. [Google Scholar] [CrossRef]
- Mao, F.; Li, D.; Xin, Z.; Du, Y.; Wang, X.; Xu, P.; Li, Z.; Qian, J.; Yao, J. High Expression of COL17A1 Predicts Poor Prognosis and Promotes the Tumor Progression via NF-ΚB Pathway in Pancreatic Adenocarcinoma. J. Oncol. 2020, 2020, 8868245. [Google Scholar] [CrossRef] [PubMed]
- Buraschi, S.; Neill, T.; Iozzo, R.V. Decorin Is a Devouring Proteoglycan: Remodeling of Intracellular Catabolism via Autophagy and Mitophagy. Matrix Biol. 2019, 75–76, 260–270. [Google Scholar] [CrossRef] [PubMed]
- Seidler, D.G. The Galactosaminoglycan-Containing Decorin and Its Impact on Diseases. Curr. Opin. Struct. Biol. 2012, 22, 578–582. [Google Scholar] [CrossRef]
- Tanfin, Z.; Leiber, D.; Robin, P.; Oyeniran, C.; Breuiller-Fouché, M. Endothelin-1: Physiological and Pathological Roles in Myometrium. Int. J. Biochem. Cell Biol. 2011, 43, 299–302. [Google Scholar] [CrossRef]
- Bagnato, A.; Rosanò, L. The Endothelin Axis in Cancer. Int. J. Biochem. Cell Biol. 2008, 40, 1443–1451. [Google Scholar] [CrossRef]
- Andersson, K.E.; Michel, M.C. (Eds.) Urinary Tract. In Handbook of Experimental Pharmacology; Springer: Heidelberg, Germany; New York, NY, USA, 2011; ISBN 978-3-642-16498-9. [Google Scholar]
- Khan, M.A.; Dashwood, M.R.; Thompson, C.S.; Mumtaz, F.H.; Mikhailidis, D.P.; Morgan, R.J. Up-Regulation of Endothelin-B (ETB) Receptors and ETB Receptor-Mediated Rabbit Detrusor Contraction in Partial Bladder Outlet Obstruction: PARTIAL BLADDER OUTLET OBSTRUCTION. BJU Int. 2001, 84, 714–719. [Google Scholar] [CrossRef]
- Ukai, M.; Yuyama, H.; Fujimori, A.; Koakutsu, A.; Sanagi, M.; Ohtake, A.; Sato, S.; Sudoh, K.; Sasamata, M.; Miyata, K. In Vitro and in Vivo Effects of Endothelin-1 and YM598, a Selective Endothelin ETA Receptor Antagonist, on the Lower Urinary Tract. Eur. J. Pharmacol. 2008, 580, 394–400. [Google Scholar] [CrossRef]
- Ogawa, T.; Sasatomi, K.; Hiragata, S.; Seki, S.; Nishizawa, O.; Chermansky, C.J.; Pflug, B.R.; Nelson, J.B.; Chancellor, M.B.; Yoshimura, N. Therapeutic Effects of Endothelin-A Receptor Antagonist on Bladder Overactivity in Rats with Chronic Spinal Cord Injury. Urology 2008, 71, 341–345. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hay, J.C.; Chao, D.S.; Kuo, C.S.; Scheller, R.H. Protein Interactions Regulating Vesicle Transport between the Endoplasmic Reticulum and Golgi Apparatus in Mammalian Cells. Cell 1997, 89, 149–158. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Lewis, T.R.; Smith, J.; Griffin, K.; Aguiar, S.; Rueb, K.F.; Holmberg-Douglas, N.; Sampson, E.M.; Tomasetti, S.; Rodriguez, S.; Stachura, D.L.; et al. NHD2-15, a Novel Antagonist of Growth Factor Receptor-Bound Protein-2 (GRB2), Inhibits Leukemic Proliferation. PLoS ONE 2020, 15, e0236839. [Google Scholar] [CrossRef]
- Roy, K.; Chakrabarti, O.; Mukhopadhyay, D. Interaction of Grb2 SH3 Domain with UVRAG in an Alzheimer’s Disease–like Scenario. Biochem. Cell Biol. 2014, 92, 219–225. [Google Scholar] [CrossRef]
- Zhang, X.; Yin, M.; Zhang, L. Keratin 6, 16 and 17—Critical Barrier Alarmin Molecules in Skin Wounds and Psoriasis. Cells 2019, 8, 807. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Wong, P.; Colucci-Guyon, E.; Takahashi, K.; Gu, C.; Babinet, C.; Coulombe, P.A. Introducing a Null Mutation in the Mouse K6α and K6β Genes Reveals Their Essential Structural Role in the Oral Mucosa. J. Cell Biol. 2000, 150, 921–928. [Google Scholar] [CrossRef] [PubMed] [Green Version]
- Hirano, S.; Kanno, S. Macrophage Receptor with Collagenous Structure (MARCO) Is Processed by Either Macropinocytosis or Endocytosis-Autophagy Pathway. PLoS ONE 2015, 10, e0142062. [Google Scholar] [CrossRef]
- Savino, F.; Pellegrino, F.; Daprà, V.; Calvi, C.; Alliaudi, C.; Montanari, P.; Galliano, I.; Bergallo, M. Macrophage Receptor With Collagenous Structure Polymorphism and Recurrent Respiratory Infections and Wheezing During Infancy: A 5-Years Follow-Up Study. Front. Pediatr. 2021, 9, 666423. [Google Scholar] [CrossRef]
- Fuchs, M.; Foresti, M.; Radeva, M.Y.; Kugelmann, D.; Keil, R.; Hatzfeld, M.; Spindler, V.; Waschke, J.; Vielmuth, F. Plakophilin 1 but not plakophilin 3 regulates desmoglein clustering. Cell Mol. Life Sci. 2019, 76, 3465–3476. [Google Scholar] [CrossRef]
- South, A.P. Plakophilin 1: An important stabilizer of desmosomes. Clin. Exp. Dermatol. 2004, 29, 161–167. [Google Scholar] [CrossRef]
- Isali, I.; Mahran, A.; Khalifa, A.O.; Sheyn, D.; Neudecker, M.; Qureshi, A.; Conroy, B.; Schumacher, F.R.; Hijaz, A.K.; El-Nashar, S.A. Gene expression in stress urinary incontinence: A systematic review. Int. Urogynecol. J. 2020, 31, 1–14. [Google Scholar] [CrossRef]
- Yang, C.; Fischer-Keso, R.; Schlechter, T.; Strobel, P.; Marx, A.; Hofmann, I. Plakophilin 1-deficient cells upregulate SPOCK1: Implications for prostate cancer progression. Tumor Biol. 2015, 36, 9567–9577. [Google Scholar] [CrossRef]
- Kuijpers, A.L.; Pfundt, R.; Zeeuwen, P.L.; Molhuizen, H.O.; Mariman, E.C.; van de Kerkhof, P.C.; Schalkwijk, J. SKALP/elafin gene polymorphisms are not associated with pustular forms of psoriasis. Clin. Genet. 1998, 54, 96–101. [Google Scholar] [CrossRef]
- Vandermeeren, M.; Daneels, G.; Bergers, M.; Van Vlijmen-Willems, I.; Pol, A.; Geysen, J.; Schalkwijk, J. Development and application of monoclonal antibodies against SKALP/elafin and other trappin family members. Arch Derm. Res. 2001, 293, 343–349. [Google Scholar] [CrossRef] [PubMed]
- Zou, S.; Tong, Q.; Liu, B.; Huang, W.; Tian, Y.; Fu, X. Targeting STAT3 in Cancer Immunotherapy. Mol. Cancer 2020, 19, 145. [Google Scholar] [CrossRef] [PubMed]
- Hruska, K.S.; LaMarca, M.E.; Scott, C.R.; Sidransky, E. Gaucher disease: Mutation and polymorphism spectrum in the glucocerebrosidase gene (GBA). Hum. Mutat. 2008, 29, 567–583. [Google Scholar] [CrossRef] [PubMed]
Disclaimer/Publisher’s Note: The statements, opinions and data contained in all publications are solely those of the individual author(s) and contributor(s) and not of MDPI and/or the editor(s). MDPI and/or the editor(s) disclaim responsibility for any injury to people or property resulting from any ideas, methods, instructions or products referred to in the content. |
© 2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
Share and Cite
Miličić, I.; Mikuš, M.; Vrbanić, A.; Kalafatić, D. The Role of Gene Expression in Stress Urinary Incontinence: An Integrative Review of Evidence. Medicina 2023, 59, 700. https://doi.org/10.3390/medicina59040700
Miličić I, Mikuš M, Vrbanić A, Kalafatić D. The Role of Gene Expression in Stress Urinary Incontinence: An Integrative Review of Evidence. Medicina. 2023; 59(4):700. https://doi.org/10.3390/medicina59040700
Chicago/Turabian StyleMiličić, Iva, Mislav Mikuš, Adam Vrbanić, and Držislav Kalafatić. 2023. "The Role of Gene Expression in Stress Urinary Incontinence: An Integrative Review of Evidence" Medicina 59, no. 4: 700. https://doi.org/10.3390/medicina59040700