Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.3 (collagenase)
 18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the fetal membranes that have ruptured 12 hours before onset of the labour the tissue collagen content was lower than in control accompanying by similar local collagenase and elastase activity. These results excluded the inflammatory process as the main cause of prelabour preterm rupture of membranes (PPROM). The analysis of the collagen fractions taken from the site of rupture and the location close to umbilical cord indicates that in PPROM there are changes in posttranslational collagen molecule modification.
Ginekol Pol 1996 Mar
PMID:[Biochemical changes in extracellular matrix components of the amniotic sac during its premature rupture]. 864 3

It was found that amniotic fluid (38-42 Hbd) contains hydroxyproline in concentration about 10 micrograms/ml. Gel filtration and dialysis demonstrated that most of hydroxyproline exists in a form of low molecular weight products. Furthermore, it was found that amniotic fluid contains a protein which eluates during gel filtration in void volume of the column. It gives a positive reaction for hydroxyproline but the absorption spectrum of such product is not characteristic for this amino acid. Furthermore, it is not digested by bacterial collagenase. It allows to conclude that amniotic fluid (38-42 Hbd) does not contain collagenous proteins. Only low molecular weight degradation products were found. Only part of them is susceptible on the action of bacterial collagenase.
Ginekol Pol 1996 Sep
PMID:[Collagen degradation products in amniotic fluid]. 928 60

In 30% cases nephrotic syndrome is due to membranous glomerulonephritis (MG). Fifty percent of patients reveal end stage renal disease in 15 years follow-up. The another 50% gain persistent remission. The pathogenesis of disease is not known. Protein accumulation in glomeruli leads to progressive loss of kidney structure and function in MG. Also the role of tissue proteolytic systems and growth factors in this process is not known. We aimed to estimate urine cathepsin B, collagenase activity and urine excretion of TGF-beta 1 and fibronectin in MG. MG patients revealed increased urine cathepsin B activity (10.58 +/- 8.73 pmol AMC/mg creatinine/min. vs. control 7.11 +/- 2.05 pmol AMC/mg creatinine/min. [p < 0.05]), urine collagenase activity (8.59 +/- 4.26 pmol AMC/mg creatinine/min. vs. control 3.84 +/- 2.09 pmol AMC/mg creatinine/min. [p > 0.02]) and increased urine excretion of fibronectin (214 +/- 335 ng/mg creatinine vs. control 12.7 +/- 6.7 ng/mg creatinine [p < 0.05]) and increased urine excretion of TGF-beta 1 (283.55 +/- 248.13 pg/ml vs. control 36.11 +/- 48.01 pg/ml [p < 0.05]). The results indicates on glomerular overproduction of TGF-beta 1 and urinary leak of proteolytic enzymes which may exacerbate glomerular proteolytic activity in MG. This may lead to glomerular protein accumulation and progressive loss of kidney function and structure in MG. Increased urine fibronectin excretion in MG patients seems to confirm the hypothesis.
Pol Arch Med Wewn 1997 Sep
PMID:[Activity of cathepsin B and collagenase in urine and excretion of fibronectin and TGF-beta 1 in urine of patients with membranous glomerulonephritis]. 955 72

The amniotic fluid (AF) was fractionated by dialysis, gel filtration and SDS/PAGE, and submitted to the assay of collagenous constituents. The collagenous character of peptides and proteins of amniotic fluid was confirmed by hydroxyproline (Hyp) assay and treatment with bacterial collagenase followed by electrophoresis and gel filtration of the digestion products. It was found that AF contains collagen degradation products but the classical method of Hyp determination described by Woessner (Arch. Biochem. Biophys., 1961, 93, 440-447) gives overestimated values due to the interference with other AF components. Fractionation of AF on Sephadex G-100 column allowed to remove the interfering material and to estimate the actual Hyp content which equals to approx. 6.2 microg/ml. About 70% of Hyp was found in low molecular dialyzable products and the rest (about 30%) appears to be a constituent of nondialyzable collagenous polypeptides of the molecular mass of about 7.9-26.3 kDa. It is suggested that such collagenous polypeptides may be the products of proteolytic conversion of collagen precursor (procollagen) into the monomeric form of this protein. No high molecular forms of collagen, corresponding to alpha-subunits, were found.
Acta Biochim Pol 1998
PMID:Collagenous constituents of amniotic fluid. 1039 50

A simple method of whole intestinal crypts isolation from rat's colonic tissue has been developed. Culture of viable epithelial cells (colonocytes) was obtained from intact crypts using method providing colonocytes for apoptosis. Satisfactory results have been obtained if the crypts were isolated using collagenase I. Under conditions applied, spontaneous release of the colonocytes took place. Liberated cells underwent almost immediate adhesion to microcarrier surface. The primary culture of normal colonocytes indicating metabolic activity for long time (> 10 days) has been obtained.
Acta Pol Pharm 2000 Nov
PMID:Normal colonocytes in primary culture--an experimental model for molecular pharmacology and biology of large intestine. 1129 54

Lesions of articular cartilage are a common problem and concern millions of people world-wide. A decrease in physical activity and pain symptoms among patients resulting from damage to articular cartilage have prompted research concerning new methods allowing cartilage regeneration. State-of-the-art treatment of articular damage depends very much on genetic engineering techniques. The aim of this paper was to determine the authors' own way of isolation, proliferation and storage of chondrocytes of articular cartilage. The material consisted of 30 rabbits, from which fragments of articular cartilage were taken. The study consisted of the following stages: isolation, chondrocyte proliferation, cell and matrix identification, storage and MTT tests. Matrix digestion was achieved using the following solutions: 0.1% type IA collagenase; 0.025% trypsin, a mixture of collagenase and trypsin. The greatest amount of cells were found after digestion of the basic matter of cartilage by 0.1% solution of type IA collagenase. When ascorbic acid was added to the medium, a 25% increase in cellularity was observed. A cumulation of procollagen mRNA was noted in the isolated cells. After about 21 days the isolated cells formed a multilayer structure, with the space between the cells filled with a substance that showed typical traits for cartilage matrix. Storing the isolated cells for less than 48 hours at room temperature gave a 90% survival rate. Most cells died after less than 12 hours when stored at 4 degrees C. The described method of chondrocyte isolation proved to be effective in preparing material for treatment of articular cartilage lesion.
Chir Narzadow Ruchu Ortop Pol 2000
PMID:[The possibility of isolation, culture and storage of articular cartilage cells]. 1138 13

Rapid resynthesis of the adenylate pool in cardiac myocytes is important for recovery of contractility and normal function of regulatory mechanisms in the heart. Adenosine and adenine are thought to be the most effective substrates for nucleotide synthesis, but the possibility of using other compounds has been studied very little in cardiomyocytes. In the present study, the effect of S-adenosyl-L-methionine (SAM) on the adenylate pool of isolated cardiomyocytes was investigated and compared to the effect of adenine and adenosine. Adult rat cardiomyocytes were isolated using the collagenase perfusion technique. The cells were incubated in the presence of adenine derivatives for 90 min followed by nucleotide determination by HPLC. The concentrations of adenine nucleotides expressed in nmol/mg of cell protein were initially 22.1 +/- 1.4, 4.0 +/- 0.3 and 0.70 +/- 0.08 for ATP, ADP and AMP, respectively (n = 10, +/- S.E.M.), and the total adenylate pool was 26.8 +/- 1.6. In the presence of 1.25 mM SAM in the medium, the adenylate pool increased by 5.2 +/- 0.4 nmol/mg of cell protein, but only if 1 mM ribose was additionally present in the medium. No changes were observed with SAM alone. A similar increase (by 4.9 +/- 0.6 nmol/mg protein) was observed after incubation with 1.25 mM adenine plus 1 mM ribose, but no increase was observed if ribose was omitted. Adenosine at 0.1 or 1.25 mM concentrations also caused an increase in the adenylate pool (by 5.2 +/- 1.0 and 5.2 +/- 0.9 nmol/mg protein, respectively), which in contrast to the SAM or adenine was independent of the additional presence of ribose. Thus, S-adenosyl-L-methionine could be used as a precursor of the adenylate pool in cardiomyocytes, which is as efficient in increasing the adenylate pool after 90 min of incubation as adenosine or adenine. Nucleotide synthesis from SAM involves the formation of adenine as an intermediate with its subsequent incorporation by adenine phosphoribosyltransferase.
Acta Biochim Pol 2000
PMID:Elevation of the adenylate pool in rat cardiomyocytes by S-adenosyl-L-methionine. 1199 6

Studies on type I procollagen produced by skin fibroblasts cultured from twins with lethal type II of osteogenesis imperfecta (OI) showed that biosynthesis of collagen (measured by L-[5-(3)H]proline incorporation into proteins susceptible to the action of bacterial collagenase) was slightly increased as compared to the control healthy infant. SDS/PAGE showed that the fibroblasts synthesized and secreted only normal type I procollagen. Electrophoretic analysis of collagen chains and CNBr peptides showed the same pattern of electrophoretic migration as in the controls. The lack of posttranslational overmodification of the collagen molecule suggested a molecular defect near the amino terminus of the collagen helix. Digestion of OI type I collagen with trypsin at 30 degrees C for 5 min generated a shorter than normal alpha2 chain which melted at 36 degrees C. Direct sequencing of an asymmetric PCR product revealed a heterozygous single nucleotide change C-->G causing a substitution of histidine by aspartic acid in the alpha2 chain at position 92. Pericellular processing of type I procollagen by the twin's fibroblasts yielded a later appearance of the intermediate pC-alpha1(I) form as compared with control cells.
Acta Biochim Pol 2003
PMID:Studies on type I collagen in skin fibroblasts cultured from twins with lethal osteogenesis imperfecta. 1283 72

We explored whether the serum concentration of interleukin 6 (IL-6) is associated with matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) in rheumatoid arthritis (RA) patients. Serum levels of IL-6, interstitial collagenase (MMP-1), stromelysin-1 (MMP-3), gelatinase B (MMP-9), TIMP-1 and TIMP-2 were assessed with an ELISA technique in 30 RA patients. We observed the association between IL-6 and MMP-1 (p < 0.001), MMP-3 (p < 0.05), MMP-9 (p < 0.001), TIMP-1 (p < 0.01) and TIMP-2 (p < 0.05). Additionally, serum IL-6, measured MMPs and TIMP-1 correlated with the erythrocyte sedimentation rate, C reactive protein plasma level and the number of swollen joints. We suggest that assessing the serum IL-6, MMP-1, MMP-3, MMP-9 and TIMP-1 levels may be helpful in the prediction of the RA activity.
Pol Arch Med Wewn 2003 Feb
PMID:[Serum interleukin 6 (il-6A) concentration correlates with matrix metalloproteinases and their tissue inhibitors in rheumatoid arthritis]. 1287 74

Tumour necrosis factor alpha (TNF-alpha) and matrix metalloproteinases (MMPs) play an important role in the pathogenesis of rheumatoid arthritis (RA). The present study was conducted to investigate whether the serum level of TNF-alpha is correlated with MMPs and tissue inhibitors of metalloproteinases (TIMPs) in RA patients. Serum concentrations of TNF-alpha, interstitial collagenase (MMP-1), stromelysin-1 (MMP-3), gelatinase B (MMP-9), TIMP-1 and TIMP-2 were measured by ELISA in 34 patients with RA. We found the TNF-alpha to correlate with MMP-1, MMP-3, MMP-9 and total measured MMPs serum concentrations (p < 0.05 for all comparisons). Furthermore, serum TNF-alpha, MMP-1 MMP-3, MMP-9 and TIMP-1 levels correlated with markers of disease activity such as the erythrocyte sedimentation rate, C reactive protein level and the number of swollen joints. No associations were observed between TNF-alpha and TIMPs serum concentrations. Our results support the concept of the regulation of the MMPs synthesis by cytokines such as TNF-alpha. We conclude that the measurement of the serum TNF-alpha, MMPs and TIMP-1 concentrations may be useful in the assessment of RA activity.
Pol Merkur Lekarski 2003 May
PMID:[Correlation between tumor necrosis factor alpha and matrix metalloproteinases levels in serum of patients with rheumatic arthritis]. 1293 14


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