Matrix metalloproteinase (MMP-1) and tissue inhibitor of MMP in peritoneal fluids and sera and correlation with peritoneal adhesions

Chegini, Nasser; Kotseos, Kristina; Bennett, Barbara B.; Diamond, Michael P.; Holmdahl, Lena; Burns, James W.

doi:10.1016/s0015-0282(01)02874-6

Cited by 29 publications

(19 citation statements)

References 29 publications

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“…In subject with adhesion, the peritoneal fluids had a lower level of MMP‐3 than in the serum, values that did not reach statistical significance or did not reflect the extent of the adhesions. However, the results suggest a local, rather than systemic, alteration in subjects with adhesions, a condition that is also found for TIMP‐1 in these subjects 11,39 . Because the proteolytic activity of MMPs is locally controlled by TIMPs, their differential expression may not only alter the proteolytic activity of MMPs in adhesions, but may also regulate cell proliferation, migration and angiogenesis that are critical in peritoneal wound healing and adhesion development 14,23,25,28,40 .…”

Section: Discussionmentioning

confidence: 74%

Differential expression of matrix metalloproteinase and tissue inhibitor of MMP in serosal tissue of intraperitoneal organs and adhesions

Chegini¹,

Zhao²,

Kotseos³

et al. 2002

BJOG

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Objective To comparatively analyse the expression of matrix metalloproteinase (MMP‐3) and tissue inhibitor of MMP (TIMP‐2) in serosal tissue of intraperitoneal organs and adhesions, as well as peritoneal fluid and serum of subjects with and without adhesions. Design Cross sectional study. Setting Academic research centres. Sample Patients undergoing abdominal/pelvic surgery. Methods Messenger ribonucleic acid (mRNA) and protein expression using quantitative reverse transcription polymerase chain reaction (Q‐RT‐PCR), ELISA and immunohistochemistry. Results All the tissues examined express MMP‐3 and TIMP‐2 mRNA and protein at consistently varying levels ranging from 100‐ to 1000‐fold and 2‐ to 10‐fold mRNA and protein, respectively. Serosa of uterine, fallopian tube, ovary and partial peritoneum express a higher MMP‐3 mRNA compared with small and large bowels and omentum, while TIMP‐2 expression was less variable with the highest level found in uterine serosa (P < 0.05). The expression of MMP‐3 and TIMP‐2 mRNA in adhesions was not significantly different compared with parietal peritoneum. MMP‐3 and TIMP‐2 protein content in tissue extracts, peritoneal fluids and serum also varied with higher TIMP‐2 than MMP‐3 (P < 0.05). TIMP‐2 levels were lower in serum of subjects with moderate/extensive adhesions compared with subjects without adhesions. Immunoreactive MMP‐3 and TIMP‐2 proteins were detected in various cell types in these tissues. There was no correlation between MMP‐3 and TIMP‐2 expression, and age, gender or menstrual status of subjects with or without adhesions. Conclusion MMP‐3 and TIMP‐2 are expressed at varying levels in serosal tissues of peritoneal organs and adhesions, with higher TIMP‐2 than MMP‐3. Based on the knowledge that tissue injury alters the expression of MMPs and TIMPs, such variations may predispose an organ to develop more adhesions than others. In addition, the results suggest that serum level of TIMP‐2 may represent a marker for subjects who will form adhesions with greater severity.

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Section: Discussionmentioning

confidence: 74%

Differential expression of matrix metalloproteinase and tissue inhibitor of MMP in serosal tissue of intraperitoneal organs and adhesions

Chegini¹,

Zhao²,

Kotseos³

et al. 2002

BJOG

Self Cite

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show abstract

“…Moreover, TGF-␤1 decreases the expression of matrix metalloproteinases (MMPs) and increases the expression of tissue inhibitors of MMPs (TIMP) [34]. A decreased MMP-1 and an increased TIMP-1 expression has been found to correlate with the presence of severe adhesions in humans [35,36]. Furthermore, peritoneal mesothelial hypoxia, which can be induced by microvascular damage associated with surgery, has been suggested to correlate with adhesion formation [37], likely through the activation of hypoxia inducible factor 1 (HIF-1).…”

Section: Discussionmentioning

confidence: 99%

RNA Interference Targeting Hypoxia Inducible Factor 1α Reduces Post-Operative Adhesions in Rats

Segura

Schmökel

Hubbell

2007

Journal of Surgical Research

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“…Several studies have demonstrated postoperative shifts in the ratio of various MMPs to their antagonists, the tissue inhibitors of matrix metalloproteinases (TIMPs) [57][58][59]. The alterations in the MMP/ TIMP ratio demonstrate a decrease in enzymatic activity during the immediate postoperative period and a maintenance of this suppression in adhesion tissue itself [57,59,60]. This suggests that the proteolytic activity of various MMPs may be important in adhesion prevention via either the degradation of matrix components, the activation of growth factors, or the facilitation of cellular migration and activity.…”

Section: Matrix Deposition-ongoing During the First Weekmentioning

confidence: 99%

Formation and Prevention of Postoperative Abdominal Adhesions

Boland

Weigel

2006

Journal of Surgical Research

192

172

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Matrix metalloproteinase (MMP-1) and tissue inhibitor of MMP in peritoneal fluids and sera and correlation with peritoneal adhesions

Cited by 29 publications

References 29 publications

Differential expression of matrix metalloproteinase and tissue inhibitor of MMP in serosal tissue of intraperitoneal organs and adhesions

Differential expression of matrix metalloproteinase and tissue inhibitor of MMP in serosal tissue of intraperitoneal organs and adhesions

RNA Interference Targeting Hypoxia Inducible Factor 1α Reduces Post-Operative Adhesions in Rats

Formation and Prevention of Postoperative Abdominal Adhesions

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