Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

A number of soluble proteins contained in human aortic intimal tissue was extracted into buffered saline (pH 7.4) and identified and quantitated by immunoelectrophoresis and immunodiffusion. The proteins included IgA, IgG, IgM, B1C (C3), alpha 1-antitrypsin, alpha 2-macroglobulin, fibrinogen, albumin, LDL, HDL, alpha 1-acid glycoprotein, beta 2-glycoprotein, transferrin and ceruloplasmin. The concentration of soluble proteins was significantly higher in the atherosclerotic intima than in the normal intima. The diseased intima also contained a small amount of tissue-bound IgG, IgA and B1C which was extractable with citrate buffer at pH 3.2. The vascular band IgG, and B1C were shown by enzymatic and immunohistochemical studies to be closely associated with the collagenous tissue of the plaque. The Ig contained in the atherosclerotic plaque may be derived in part from the biosynthesis of Ig by the artery, since the incorporation of 14C-labeled leucine into IgG by the atheromatous plaque was demonstrable by radioimmunoelectrophoresis. In contrast to the diseased artery, the normal artery did not synthesize IgG and did not contain vascular bound IgG or complement. However, the normal artery was capable of fixing IgG and B1C eluted from the diseased artery. The present studies suggested that the IgG contained and synthesized by the plaque might represent an immune response to an endogenous or exogenous antigen closely associated with plaque collagen. IgG and B1C either alone or in the form of an immune complex also may play an important role in phagocytosis in the plaque and thereby influence the course of atherosclerosis. The proteolytic inhibitors, alpha 1-antitrypsin and alpha 2-macroglobulin, found in relatively high concentrations in the plaque, could enhance fibrosis of the lesion because of thier known inhibitory effects on collagenase and elastase.
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PMID:Soluble proteins in the human atherosclerotic plaque. With spectral reference to immunoglobulins, C3-complement component, alpha 1-antitrypsin and alpha 2-macroglobulin. 9 93

Previous studies from this laboratory have shown that pigeon embryo fibroblasts in culture, derived from embryo explants, do not express LDL receptors. In contrast, pigeon peritoneal macrophages and pigeon hepatocytes in culture express LDL receptors. The presence of an active LDL receptor pathway in pigeons has been further confirmed by in vivo studies which showed that receptor-mediated mechanisms were responsible for greater than 80 percent of whole body LDL clearance. The purpose of the present study was to determine the factors responsible for the failure of explant-derived pigeon embryo cells to express LDL receptors. To address this problem, both chicken and pigeon embryo cells were studied. Primary pigeon and chicken embryo cells isolated by collagenase digestion expressed high levels of LDL receptor activity using 125I-labelled pigeon LDL as the ligand. Cells isolated from chicken embryo by enzyme digestion expressed an approximately 10-fold greater LDL receptor activity than cells derived from explants. Pigeon LDL and beta-VLDL, but not methyl-LDL, HDL or mammalian LDL, bound to a limited number of receptors on pigeon embryo cells with specificity and high affinity. Other properties of the pigeon LDL receptor were similar to the mammalian LDL receptor with the exception that the pigeon LDL receptor was resistant to the proteolytic enzyme, pronase. In both pigeon and chicken embryo cells LDL receptor activity was lost with subsequent passage in culture. As a result, the failure of explant derived pigeon cells to express LDL receptors appears to be the result of two factors, the use of explant rather than enzyme-isolated cells and the loss of any remaining LDL receptor activity as a result of passage in culture. Whether this difference between pigeon and mammalian cells with respect to LDL receptor activity is the result of differences in the molecular structure of the pigeon LDL receptor remains to be determined.
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PMID:The method of isolation of primary cells and their subculture influences the expression of LDL receptors on pigeon and chicken embryo cells in culture. 166 57

High density lipoprotein (HDL3) binds with high affinity to many types of cells, but controversy exists concerning the nature and biological significance of the binding. We have recently demonstrated that HDL and apoproteins (apo)-AI, -AII, and -CI stimulate a specific and dose-dependent increase in placental lactogen (hPL) release from human trophoblast cells. To examine the possible relationship between HDL3 binding and stimulation of hPL release, we have characterized the binding of [125I]HDL3 to an enriched fraction of hPL-producing trophoblast cells. Binding studies were performed on trophoblast cells isolated by isopycnic centrifugation of collagenase/hyaluronidase-dispersed placental tissue and apo-E free-HDL3 (density, 1.125-1.215 g/ml). Scatchard analysis of binding studies performed at 37 C for 2 h revealed two classes of binding sites: 1) high affinity binding sites with a Kd of 9.7 +/- 2.2 micrograms/ml (1.3 x 10(-7) M) and 9.8 +/- 3.2 x 10(5) binding sites/trophoblast cell, and 2) low affinity binding sites with a Kd of 172.8 +/- 64.8 micrograms/ml (2.3 x 10(-6) M) and an estimated 3.2 x 10(6) sites/cell. As has been found in hepatocytes and other cells, the number of HDL3-binding sites per trophoblast cell (but not the binding affinity) decreased at lower incubation temperatures. In addition, HDL3 binding to trophoblasts cells did not require calcium and was not affected by prior treatment of the cells with pronase or trypsin. HDL3-binding sites on trophoblast cells, however, were not specific for HDL3. Low density lipoprotein (density, 1.063-1.055 g/ml), which does not stimulate hPL release, was nearly as potent on a molar basis as HDL3 in binding to the high and low affinity binding sites on trophoblast cells. Furthermore, nitrated HDL3, which does not compete for high affinity binding to trophoblast cells, stimulated hPL release. Although the characteristics of HDL3 binding to trophoblast cells are similar to those of other cells, these results strongly suggest that the binding of HDL3 to high affinity binding sites is not essential for HDL-mediated hPL release.
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PMID:High density lipoprotein3 binding and biological action: high affinity binding is not necessary for stimulation of placental lactogen release from trophoblast cells. 258 47

A total of 46 patients, aged 39-71 years (mean 57.7), were studied. Forty-eight percent of the patients were hyperlipidemic and 63% had earlier suffered a myocardial infarction. Biopsies from aorta were obtained during coronary bypass surgery. Apo B was extracted from the intima by incubation of the tissue in buffer, followed by collagenase digestion. Intimal apo B was quantified in an immunoradiometric assay. There were significant correlations between total or collagenase-extractable apo B and serum cholesterol (rs = 0.39, P less than 0.01), serum triglycerides (rs = 0.33, P less than 0.05), LDL cholesterol (rs = 0.33, P less than 0.05) and serum apo B (rs = 0.37, P less than 0.05). The correlations were strongest for the collagenase-extractable apo B, while no correlations were observed for the buffer-extractable intimal apo B. No significant correlations were found between intimal apo B and serum HDL, apo A-I, smoking habits, history of hypertension or sustained myocardial infarction. Follow-up data were available for 42 of the patients, with a mean follow-up period of 35.1 months. The patients were classified according to symptoms of angina pectoris at the time of follow-up. There were significantly lower levels of serum apo A-I in the patients with poorer clinical prognosis. In a linear multiple stepwise regression analysis, apo A-I and serum LDL were significantly and independently related to clinical prognosis (R2 = 0.31).
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PMID:Apolipoprotein B in human aortic biopsies in relation to serum lipids and lipoproteins. 278 44

The plasma clearance rate of high density lipoprotein is reduced in the hypothyroid rat. Because the liver is an important site of HDL-cholesterol catabolism, the present study was undertaken to investigate whether thyroid hormone deficiency affects binding of HDL to liver cells. Male Wistar rats were made hypothyroid by feeding propylthiouracil (0.1% w/w). Liver cells were isolated by in situ perfusion of the liver with a buffered collagenase solution. 125I-labelled rat HDL binding to isolated liver cells was carried out at low temperature on ice. For both control and hypothyroid rat liver cells, 125I-HDL binding was significantly inhibited by excess unlabelled rat HDL and also by human HDL3 and human LDL but was unaffected by the addition of 10 mM EDTA. From Scatchard analysis of dose-response studies, hypothyroid cells displayed a lower HDL binding capacity (P less than 0.01) and a higher binding affinity (P less than 0.025) compared to control cells. These results suggest that thyroid hormone affects the expression of the HDL binding site in liver cells which may contribute to the reduced HDL clearance in the hypothyroid animal.
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PMID:Hypothyroidism reduces HDL binding to rat liver cells. 280 42

A collagenase dispersed cell suspension from PMSG-hCG primed immature rats responded to exogenously added hCG, cholera enteroxin, prolactin, and 8-Bromocyclic-AMP with increase in progesterone production in a dose dependent manner, and this stimulation was augmented by the plasma lipoprotein fractions hHDL and hLDL. The responsiveness to low doses of prolactin was not apparent when lipoprotein fractions were not included in the assay mixture. When the incubation mixture contained either LDL or HDL, the stimulatory effect of prolactin on progesterone production was evident at 5 and 10 micrograms prolactin/ml of the incubation mixture. Progesterone production, both basal and hormone stimulated, was maximum on day 7 of pseudopregnancy. Although the extent of hCG and prolactin stimulation of progesterone production and its potentiation by lipoprotein fractions was observed to be higher on days 3 and 5 than that seen on day 7, the net amount of progesterone produced was highest on day 7. The basal as well as hormone and lipoprotein stimulated progesterone production started to decline after day 7, reaching a nadir on day 14. These experiments show that prolactin is effective in stimulating progesterone production by rat luteal cells in vitro and that lipoprotein fractions, LDL and HDL further potentiate this response. This study further suggests that it is important to include LDL or HDL as a source of cholesterol for in vitro experiments in which the steroidogenic response of luteal cells to exogenous stimuli is tested.
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PMID:Lipoprotein augmentation of human chorionic gonadotropin and prolactin stimulated progesterone synthesis by rat luteal cells. 397 30

Utilization of lipoproteins by cells prepared by collagenase dispersion of ovaries of immature gonadotropin-primed rats was studied. Human and rat HDL increased basal progestin secretion and incorporation of [14C]oleate into cellular sterol esters 2-fold during a 2 h incubation, with maximal stimulation occurring at a lipoprotein sterol concentration of 125 micrograms/ml. This concentration of HDL cholesterol also increased progestin production by cells stimulated with dibutyryl cyclic AMP. Human LDL or cholesterol-rich lipid dispersions had little effect upon either progestin secretion or sterol esterification at similar sterol concentrations. However, addition of delipidated human HDL apolipoproteins to the cholesterol-rich lipid dispersions markedly enhanced progestin production. Incubation of the dispersed cells in the presence of 25 micro M ML-236B, which blocked cellular de novo sterol synthesis by over 90%, had no effect upon progestin secretion. Specific uptake of human 125I-labeled HDL by the dispersed cells was observed. Analysis fo 125I-labeled HDL uptake as a function of lipoprotein concentration indicated that the uptake process was saturated at HDL levels of 200-400 micrograms protein/ml. The amount of HDL specifically associated with the cells at saturating levels after 1 h of incubation was sufficient to account for the increased progestin synthesis and sterol ester storage observed during this time. During the incubations cell-specific degradation of the 125I-labeled HDL apolipoprotein appeared to be minimal. We conclude that lipoprotein-carried cholesterol is an important substrate for rat luteal cells and that these cells possess a specific mechanism for the uptake of HDL.
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PMID:High density lipoprotein utilization by dispersed rat luteal cells. 626 77

Bovine aortic endothelial cells (BAEC), detached with collagenase, have been studied morphologically after administration, in vitro, of human lipoprotein fractions (200 micrograms/ml of LDL, 200 micrograms/ml of HDL), 24 h before the confluence. One day after the treated cells and the control one were detached with trypsine and prepared for freeze-etching examination. The plasma-membrane has revealed, in the lipoprotein treated cells (HDL or LDL) an increased average value of the number of "pits" present upon a surface unit (P less than 0,05). Moreover, in the HDL-treated cells, the "pits", sometimes, have appeared with a different morphological evidence, similar to the aspects of exocytosis as seen e.g. in platelets or in Langerhans isle cells.
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PMID:[Effects of high density lipoproteins (HDL) and low density lipoproteins (LDL) on cultured bovine aorta endothelial cells. Preliminary observations on ultrastructural morphology of the plasma membrane by freeze-fracturing]. 715 31

In the present study, hypertriglyceridemia was induced by feeding S. D. rats with high carbohydrate diet (carbohydrate accounting for 80% of total calorie) for 5 days. Rat liver parenchymal cells (PC) and non-parenchymal cells (NPC) were prepared by collagenase method. Human plasma LDL, VLDL and HDL were isolated by density gradient ultracentrifugation method. 125I-LDL was labelled by ICI method. 125I-LDL binding to rat liver PC and NPC were measured by Goldstein and Brown's method. The results showed that both rat liver PC and NPC had LDL receptors to bind, uptake and degradate 125I labelled human plasma LDL. The Bmax of 125I-LDL binding to NPC was 7-fold higher than that of PC (P < 0.01), but the Kd values remained unchanged. The Bmax of 125I-LDL binding to liver NPC from hypertriglyceridemic rats was significantly higher than that of NPC from the normal diet (carbohydrate accounting for 60% of total calorie) rats (435.4 + 100.0 vs 307.1 +/- 76.8 ng/mg cell protein, n = 6, P > 0.05), but there was no difference in Kd between the HTG rats and normal rats (18.1 +/- 4.1 vs 17.2 +/- 4.0 micrograms/ml n = 6, P > 0.05). These results suggest that the increase in fractional catabolic rate of LDL in patients with hypertriglyceridemia reported by Vega and Grundy might be induced by the increase in number of LDL receptor on liver non-parenchymal cells.
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PMID:[Study on LDL receptors of liver non-parenchymal cells in hypertriglyceridemic rats induced by high carbohydrate diet]. 858 86

Cortisol-cortisone interconversion is catalyzed by the NADP/NADPH-dependent oxido-reductase, 11beta-hydroxysteroid dehydrogenase-1 (11betaHSD-1) and the NAD-dependent oxidase, 11betaHSD-2. Because of the importance of placental corticosteroid metabolism in dictating the amount of cortisol arriving in the fetus to regulate fetal pituitary-adrenocortical function, the present study determined whether there was a developmental change in the expression of 11betaHSD-1 and/or -2 in placental syncytiotrophoblast, the site of maternal:fetal exchange. A syncytiotrophoblast-enriched (>95%) cell fraction was isolated from baboon placentas obtained at early (day 60), mid (day 100), and late (day 165) gestation (term = day 184), and 11betaHSD-1 and -2 messenger RNA (mRNA) and protein levels were determined by Northern and Western blots. The levels (mean +/- SE) of the single 1.6-kilobase (kb) mRNA for 11betaHSD-1, expressed as a ratio to beta-actin, increased (P < 0.05) between early (0.36 +/- 0.16; n = 4) and mid (0.95 +/- 0.21; n = 11) gestation and further increased (P < 0.05) by late gestation (1.82 +/- 0.29; n = 13). Similarly, the levels of the single 1.9-kb mRNA for 11betaHSD-2 in late gestation (2.46 +/- 0.35; n = 8) were greater (P < 0.05) than respective values at mid (1.36 +/- 0.22; n = 8) and early (0.64; n = 2) gestation. The levels of 11betaHSD-1 (arbitrary densitometric units), detected as a dominant band of 34 kDa, were greater (P < 0.05) in late gestation (2.6 +/- 0.2; n = 4) than at early (1.2 +/- 0.1; n = 4) or mid (1.9 +/- 0.3; n = 4) gestation. In contrast, 11betaHSD-2 was not detected by Western blot in syncytiotrophoblast isolated by collagenase dispersion. However, immunocytochemistry revealed that 11betaHSD-2 was present in and localized to the syncytiotrophoblast layer of the baboon placenta and that expression in late gestation (n = 4) appeared to exceed that in placentas of early (n = 4) and mid (n = 4) gestation. These results indicate that both 11betaHSD-1 and 11betaHSD-2 were expressed in syncytiotrophoblasts of the baboon placenta and that the mRNA and protein levels of these two 11betaHSD enzymes increased with advancing gestation. However, because 11betaHSD-2 was not detected in syncytiotrophoblast isolated by collagenase dispersion, we suggest that the 11betaHSD-1 and -2 reside in different membrane fractions of the syncytiotrophoblast. Consequently, the estrogen-regulated change in transplacental cortisol metabolism with advancing gestation may result in a developmental change in the expression and location of the two 11betaHSD enzymes controlling cortisol-cortisone metabolism and transfer into the fetus, resulting in activation of the fetal pituitary adrenocortical system.
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PMID:Developmental increase in expression of the messenger ribonucleic acid and protein levels of 11beta-hydroxysteroid dehydrogenase types 1 and 2 in the baboon placenta. 894 Mar 99


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