Genes responsible for vaginal extracellular matrix metabolism are modulated by women's reproductive cycle and menopause

Shynlova, Oksana; Bortolini, Maria Augusta Tezelli; Alarab, May

doi:10.1590/s1677-5538.ibju.2013.02.15

Cited by 37 publications

(29 citation statements)

References 29 publications

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“…There is, however, correlative data in an array of tissues suggesting that TIMP4 restricts ECM proteolysis in the developing lung [63], female reproductive tract [64], eyes [65], and transplanted tissues [66].…”

Section: Timp4 Direct Inhibition Of Ecm Proteolysis By Timp4mentioning

confidence: 99%

“…Pelvic organ prolapse (POP) is thought to be dependent on a lack of ECM deposition and increased ECM destruction leading to a weakening of the pelvic floor [64]. Timp4 expression is significantly lower in patients suffering from POP, which supports a role for TIMP4 in protection of the ECM from increased proteolysis [64].…”

Section: Timp4 Direct Inhibition Of Ecm Proteolysis By Timp4mentioning

confidence: 99%

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The role of TIMPs in regulation of extracellular matrix proteolysis

2015

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Tissue inhibitors of metalloproteinases (TIMPs), which inhibit matrix metalloproteinases (MMPs) as well as the closely related, a disintegrin and metalloproteinases (ADAMs) and ADAMs with thrombospondin motifs (ADAMTSs), were traditionally thought to control extracellular matrix (ECM) proteolysis through direct inhibition of MMP-dependent ECM proteolysis. This classical role for TIMPs suggests that increased TIMP levels results in ECM accumulation (or fibrosis), whereas loss of TIMPs leads to enhanced matrix proteolysis. Mice lacking TIMP family members have provided support for such a role; however, studies with these TIMP deficient mice have also demonstrated that loss of TIMPs can often be associated with an accumulation of ECM. Collectively, these studies suggest that the divergent roles of TIMPs in matrix accumulation and proteolysis, which together can be referred to as ECM turnover, are dependent on the TIMP, specific tissue, and local tissue environment (i.e. health vs. injury/disease). Ultimately, these combined factors dictate the specific metalloproteinases being regulated by a given TIMP, and it is likely the diversity of metalloproteinases and their physiological substrates that determines whether TIMPs inhibit matrix proteolysis or accumulation. In this review, we discuss the evidence for the dichotomous roles of TIMPs in ECM turnover highlighting some of the common findings between different TIMP family members. Importantly, while we now have a better understanding of the role of TIMPs in regulating ECM turnover, much remains to be determined. Data on the specific metalloproteinases inhibited by different TIMPs in vivo remains limited and must be the focus of future studies.

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Section: Timp4 Direct Inhibition Of Ecm Proteolysis By Timp4mentioning

confidence: 99%

Section: Timp4 Direct Inhibition Of Ecm Proteolysis By Timp4mentioning

confidence: 99%

The role of TIMPs in regulation of extracellular matrix proteolysis

2015

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“…This result contradicts results from other studies, like the one conducted by M. Bortolini et al, where PCP reaction was stronger in the control group [21,22,26]. Nevertheless the menopausal status alone could explain the overall reduction of PCP expression, as M. Bortolini et al, conclude [22,26,27].…”

Section: Discussionmentioning

confidence: 56%

Distribution and immunoexpression of LOX, PCP and Myofi broblasts in Vaginal Tissue of Postmenopausal Women with and without Pelvic Organ Prolapse

Kleanthis¹,

Kondi-Pafiti²,

Liapis³

et al. 2017

J Gynecol Res Obstet

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Aim: of the study was to investigate the difference of distribution and expression of the lysyl oxidase enzymes (LOX), the pro-collagen C proteinase (PCP) and the myofi broblasts in the vaginal tissue of postmenopausal women, with and without prolapse. Materials and Methods:This was a prospective closely matched controlled clinicopathological study. Samples were obtained from the anterior vaginal wall of postmenopausal patients that underwent hysterectomy for benign conditions. The immunohistochemical study of the samples was performed on paraffi n embedded specimens with the semi-automatic Ventana method according to the manufacturer's instructions. We have also examined the correlation between prolapse and parity, age and body weight in the same population. Results:We have examined vaginal tissue from 44 postmenopausal patients: 21 with prolapse and 23 without (control group). LOX enzymes were observed in all samples, but they were strongly expressed only in the control group (P<0.005). Similarly PCP and myofi broblasts were positive in all tissues but no statistically important difference in their expression was observed between the two groups. Linear correlation between older age and higher parity with prolapse, was observed. There was no correlation between prolapse and body weight. Conclusion:LOX enzymes are strongly expressed in the vaginal tissue of postmenopausal women without prolapse and may play an important role in the pathophysiology of POP. There is no statististical difference in the expression of PCP and fi broblasts between the control group and the patients with prolapse. Higher parity and older age are associated with prolapse, but the same doesn't apply for higher body weight.

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“…The tissue biopsy technique was reported in previous publication. 17 Briefly, after removal of the uterus or pelvic floor repair, vaginal tissue specimen (at least 1 cm 2 ) was obtained by sharp dissection down to the avascular space of loose areolar connective tissue of the vagina. The site of tissue collection was standardized at the anterior middle portion of the vaginal vault.…”

Section: Tissue Collectionmentioning

confidence: 99%