OBJECTIVETo examine the expression of matrix metalloproteinases (MMP)-2, -9, tissue inhibitor of matrix metalloproteinase (TIMP)-1 and hs-CRP, and their relationship with coronary artery in children with Kawasaki disease.

METHODSOne hundred and fifty-one children with Kawasaki disease (111 cases with coronary artery damage and 40 cases without) and 60 healthy children were enrolled. The expression of MMP-2, MMP-9 and TIMP-1 was detected using ELISA, and the hs-CRP concentration was measured using the endpoint nephelometry.

RESULTSThere were significant differences in the level of MMP-2, MMP-9 and hs-CRP between the patients with or without coronary artery damage and the healthy children (p<0.05). The levels of MMP-2, MMP-9 and hs-CRP were the highest in the cardiovascular damage group (p<0.05). There were positive correlations between MMP-2, MMP-9 and TIMP-1 in children with Kawasaki disease.

CONCLUSIONSMMP-2, MMP-9, TIMP-1 and hs-CRP may play important roles in the development of Kawasaki disease. The combined measurement of MMP-2, MMP-9 and hs-CRP may be useful in the evaluation of the severity in children with Kawasaki disease.

C-Reactive Protein ; analysis ; Child ; Child, Preschool ; Female ; Humans ; Infant ; Male ; Matrix Metalloproteinase 2 ; blood ; Matrix Metalloproteinase 9 ; blood ; Mucocutaneous Lymph Node Syndrome ; blood ; etiology ; Tissue Inhibitor of Metalloproteinase-1 ; blood

DNA, Complementary ; chemistry ; Humans ; Leukocytes ; enzymology ; Lung Neoplasms ; enzymology ; pathology ; Matrix Metalloproteinase 2 ; blood ; genetics ; Matrix Metalloproteinase 9 ; blood ; genetics ; Neoplasm Invasiveness ; Neoplasm Metastasis ; RNA, Messenger ; analysis ; Tissue Inhibitor of Metalloproteinase-1 ; blood ; genetics

The levels of tartrate resistant acid phosphatase (TRAP), matrix metalloproteinase-2 (MMP-2), and tissue inhibitor of matrix metalloproteinase-2 (TIMP-2) in synovial fluid (SF) and serum in cases of canine osteoarthritis (OA) were measured. OA was induced by a surgically-created medial patellar luxation in the left stifle of 24 dogs. SF and blood samples were collected at 1.5- and 3-month intervals, respectively. Every 3 months, one dog was euthanatized to collect tissue samples from both stifles. TRAP levels in SF and serum were measured using a spectrophotometer, and TRAP-positive cells in joint tissues were identified by enzyme histochemistry. MMP-2 and TIMP-2 in SF and serum were detected by Western blotting and ELISA, respectively. TRAP in SF from the stifles and serum was significantly increased (p < 0.05) after 3 months. TIMP-2 in SF and serum was significantly decreased (p < 0.05), whereas MMP-2 in SF was significantly increased (p < 0.05) during the progression of OA. Histochemistry revealed an increased number of TRAP-positive cells in tissues from OA-affected joints. Assays measuring TRAP, MMP-2, and TIMP-2 in SF and serum, and methods that detect increased numbers of TRAP-positive cells in the joint tissues can play an important role in identifying the early phases of degenerative changes in canine joint components.
Acid Phosphatase/analysis/blood ; Animals ; Arthritis, Experimental/enzymology/etiology/veterinary ; Biological Markers/*analysis/*blood ; Blotting, Western/veterinary ; Dislocations/complications/*veterinary ; Dog Diseases/*enzymology/etiology ; Dogs ; Enzyme-Linked Immunosorbent Assay/veterinary ; Female ; Isoenzymes/analysis/blood ; Male ; Matrix Metalloproteinase 2/analysis/blood ; Osteoarthritis/enzymology/etiology/*veterinary ; Spectrophotometry/veterinary ; Stifle/physiopathology ; Synovial Fluid/*enzymology ; Tissue Inhibitor of Metalloproteinase-2/analysis/blood

BACKGROUND AND OBJECTIVES: Hypertension develops as a result of cardiac hypertrophy and fibrosis or as a result of exchange of the extracellular matrix. In particular, matrix metalloproteinase (MMP)-3 is a major enzyme involved in the reconstruction of the arterial intima through activation of other MMPs. We analyzed MMP-3 genotypes in hypertensive and normotensive adolescents and sought to determine if a particular genotype is a predictor of cardiovascular complications. SUBJECTS AND METHODS: Forty-four hypertensive adolescents and 59 healthy adolescents were included in this study. Serum aldosterone, renin, insulin, angiotensin converting enzyme (ACE), insulin, homocysteine, vitamin B12, folate, MMP-1, MMP-2, MMP-3, MMP-9, tissue inhibitors of matrix metalloproteinases (TIMP)-1, and TIMP-2 were measured. MMP-3 genotypes were analyzed using a polymerase chain reaction (PCR) primer. The carotid intima media thickness (IMT), diameter, and brachial ankle pulse wave velocity (baPWV) were evaluated using ultrasound. RESULTS: In hypertensive adolescents, blood pressure, anthropometric data, carotid IMT, baPWV, serum pro-MMP-1, MMP-2, MMP-9, TIMP-1, and TIMP-2 were no different between the 6A/6A group and the 5A/6A group. Serum MMP-9 was higher in the 5A/6A group than in the control group. Aldosterone, insulin, and homocysteine were higher in the 6A/6A group than in the control group, and vitamin B12 and folate were lower in the 6A/6A group than in the control group. CONCLUSION: In conclusion, serum MMP-3 levels were not significantly different in different MMP-3 genotypes in hypertensive adolescents. However, few patients were included in this study. Further investigation is necessary to clarify the relationship between MMP-3 genotype and cardiovascular risk.
Adolescent ; Aldosterone ; Animals ; Ankle ; Blood Pressure ; Cardiomegaly ; Carotid Intima-Media Thickness ; Extracellular Matrix ; Fibrosis ; Folic Acid ; Genotype ; Homocysteine ; Humans ; Hypertension ; Insulin ; Matrix Metalloproteinases ; Peptidyl-Dipeptidase A ; Polymerase Chain Reaction ; Pulse Wave Analysis ; Renin ; Tissue Inhibitor of Metalloproteinase-1 ; Tissue Inhibitor of Metalloproteinase-2 ; Tunica Intima ; Vitamin B 12

BACKGROUNDExcessive deposition of extracellular matrix (ECM) in the kidney is the hallmark of diabetic nephropathy. Increased matrix synthesis has been well documented but the effects of diabetes on degradative pathways, particularly in the in vivo setting. The renal protective effect of these pathways on matrix accumulation has not been fully elucidated. The present study was undertaken to investigate the activity of matrix metalloproteinase-2 (MMP-2), the expression of MMP-2 and tissue inhibitor of metalloproteinase-2 (TIMP-2) in kidney tissues of diabetic rats, and to explore the degradative pathway of type IV collagen (IV-C) and the renal protective effects of ACE inhibition-benazepril.

METHODSTwenty-four healthy male Wistar rats were divided randomly into normal control group (NC group), untreated diabetes mellitus group (DM group), and diabetes mellitus group treated with benazepril (DL group). The rat model of diabetes mellitus was induced by intraperitoneal injection of streptozocin (60 mg/kg). After the establishment of DM model, benazepril (10 mg.kg(-1).d(-1)) was given to the DL group for 12 weeks, and the same volume of water was given to the other two groups. At the end of 12 weeks, renal function was evaluated with 24-hour urinary protein (Upro), clearance of creatinine (Ccr), and blood urea nitrogen (BUN). MMP-2 activity was determined by gelatin zymography. The levels of MMP-2, TIMP-2 and collagen IV (IV-C) protein in the kidney tissue were assessed by immunohistochemistry. The gene expression of MMP-2 and TIMP-2 was measured by reverse transcription polymerase chain reaction (RT-PCR).

RESULTSThe levels of BUN, Upro and Ccr in the DM group were higher than those in the NC group. In the DM group, the mRNA, enzymatic activity and proteins of MMP-2 decreased, but the expressions of IV-C and TIMP-2 increased. All diabetes-associated changes in renal function and MMP/TIMP were attenuated after benazepril treatment with reduced IV-C accumulation.

CONCLUSIONSThe changes of MMP-2 and TIMP-2 expressions in kidney tissues of diabetes rats may contribute to the occurrence and progression of diabetic nephropathy. Benazepril could exert protective effects on diabetic nephropathy, owing to the upregulation of MMP-2 and downregulation of TIMP-2 expressions, which further inhibits the excessive deposition of extracellular matrix in the glomerulus.

Angiotensin-Converting Enzyme Inhibitors ; pharmacology ; Animals ; Benzazepines ; pharmacology ; Blood Glucose ; analysis ; Body Weight ; Collagen Type IV ; metabolism ; Diabetes Mellitus, Experimental ; metabolism ; pathology ; Diabetic Nephropathies ; prevention & control ; Kidney ; drug effects ; metabolism ; Kidney Glomerulus ; pathology ; Male ; Matrix Metalloproteinase 2 ; analysis ; genetics ; Organ Size ; Rats ; Rats, Wistar ; Streptozocin ; Tissue Inhibitor of Metalloproteinase-2 ; analysis ; genetics