Expression of matrix metalloproteinase (MMP-1) and tissue inhibitor of MMP in serosal tissue of intraperitoneal organs and adhesions.
OBJECTIVE
To compare expression of matrix metalloproteinase (MMP-1) and tissue inhibitor of MMP (TIMP-1) in serosal tissue of intraperitoneal organs and adhesions.


METHODS
Prospective and cross-sectional study.


METHODS
Academic research centers.


METHODS
Patients undergoing abdominal or pelvic surgery.


METHODS
MMP-1 and TIMP-1 expression.


METHODS
Expression of messenger ribonucleic acid (mRNA) and protein was measured by using quantitative reverse transcription polymerase chain reaction (RT-PCR) and enzyme-linked immunosorbent assay.


RESULTS
Serosal tissue of intraperitoneal organs and adhesions express MMP-1 and TIMP-1 mRNA and protein at levels that are consistently varied with 10- to 10,000-fold and 2- to 10-fold higher TIMP, mRNA and protein, respectively. Parietal peritoneum, fallopian tubes and ovaries express higher MMP-1 mRNA levels compared with uterus and adhesions; the lowest expression is found in small and large bowels, subcutaneous tissue. and omentum. Expression of TIMP-1 mRNA was less variable; the highest level was found in the uterus and the lowest in subcutaneous tissue and small bowels. There was less variability in MMP-1 and TIMP-1 protein content than mRNA expression; ovaries and adhesions contained the highest MMP-1 and TIMP-1 levels, respectively, and peritoneum contained the lowest. The MMP-1 and TIMP-1 content and ratios further indicate limited MMP-1 proteolytic activity. Although tissues from premenopausal women express more MMP-1 and TIMP-1, expression did not differ by sex or age.


CONCLUSIONS
Because MMP-1 and TIMP-1 expression varies consistently among the serosal tissues of peritoneal organs and adhesions, and because tissue injury alters their expression, site-specific variations in expression of these substances may predispose a particular organ to develop more adhesions.
Chegini
N
N
Department of Obstetrics and Gynecology, Institute for Wound Research, University of Florida, Gainesville, Florida 32610-0294, USA. cheginin@obgyn.ufl.edu
Kotseos
K
K
Zhao
Y
Y
Ma
C
C
McLean
F
F
Diamond
M P
MP
Holmdahl
L
L
Burns
J
J
D000005:Abdomen / Q000601:surgery; D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D003430:Cross-Sectional Studies; D018076:DNA, Complementary / Q000737:chemistry; D004797:Enzyme-Linked Immunosorbent Assay; D005260:Female; D006801:Humans; D008297:Male; D020781:Matrix Metalloproteinase 1 / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D008875:Middle Aged; D010532:Peritoneal Diseases / Q000201:enzymology* / Q000473:pathology; D010537:Peritoneum / Q000201:enzymology* / Q000473:pathology; D011446:Prospective Studies; D012313:RNA / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D020133:Reverse Transcriptase Polymerase Chain Reaction; D018709:Statistics, Nonparametric; D000267:Tissue Adhesions / Q000201:enzymology* / Q000473:pathology; D019715:Tissue Inhibitor of Metalloproteinase-1 / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics
D018076:DNA, Complementary; D019715:Tissue Inhibitor of Metalloproteinase-1; D012313:RNA; D020781:Matrix Metalloproteinase 1