Collagen metabolism and turnover in women with stress urinary incontinence and pelvic prolapse

Int Urogynecol J Pelvic Floor Dysfunct. 2002;13(2):80-7; discussion 87. doi: 10.1007/s001920200020.

Abstract

The aim of this study was to investigate quantitative mRNA expression of matrix metalloproteinases MMP-1, MMP-2, MMP-9, and their inhibitors, the tissue inhibitors of metalloproteinases TIMP-1, TIMP-2 and TIMP-3, in vaginal wall tissue from women with stress urinary incontinence compared to continent controls. Vaginal wall tissues were obtained from 7 women with stress urinary incontinence/severe pelvic prolapse and 15 continent controls. RNA was then extracted and quantified. Quantitative competitive reverse transcription (QC-RT-PCR) was carried out with oligonucleotide primers to quantify MMP-1, MMP-2, MMP-9, TIMP-1, TIMP-2 and TIMP-3 mRNA expression. Stress continent women demonstrated a significant decrease in TIMP-1 and mRNA expression (P = 0.03). There was no difference in TIMP-2, TIMP-3, MMP-2 or MMP-9 mRNA expression between stress incontinent women and controls. However, MMP-1 mRNA expression was significantly increased (P = 0.05) in the incontinent group and the MMP-1/TIMP-1 ratio (P = 0.04) was consistent with increased collagen degradation in the stress incontinence. Stress incontinent women demonstrated an increase in MMP-1 mRNA expression and a decrease in the inhibitor TIMP-1 mRNA expression. Both these findings are consistent with increased collagen breakdown as a pathologic etiology of incontinence.

MeSH terms

  • Amino Acids / metabolism
  • Case-Control Studies
  • Collagen / metabolism*
  • Female
  • Humans
  • Matrix Metalloproteinases / metabolism*
  • Middle Aged
  • RNA, Messenger / genetics
  • Reverse Transcriptase Polymerase Chain Reaction
  • Tissue Inhibitor of Metalloproteinases / metabolism*
  • Urinary Incontinence, Stress / metabolism*
  • Uterine Prolapse / metabolism*
  • Vagina / metabolism

Substances

  • Amino Acids
  • RNA, Messenger
  • Tissue Inhibitor of Metalloproteinases
  • pyridinoline
  • Collagen
  • Matrix Metalloproteinases