Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Partially purified beta cell monolayer cultures were prepared from the pancrease of neonatal Wistar rats by dissociating the cells with a trypsin-collagenase solution. The cultures were grown in medium 199 containing a 10% fetal calf serum and 100 or 300 mg/100 ml glucose. Insulin release from the primary cultures during 12 days was 15 to 20 microunit/culture/day when the cells were grown in the medium containing 300 mg/100 ml glucose. When glucose concentration in the medium was decreased from 300 to 100 mg/ml insulin release fell to 2--5 microunit/culture/day. Theophylline stimulated insulin release in a short-time experiment. Transplantation of a 6--8-day culture in diabetic rats reduced the blood glucose concentration for 1 to 2 days.
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PMID:[Monolayer culture of pancreatic beta cells of newborn rats: Insulin secretion in vitro and attempt at beta-cell transplantation in experimental diabetes]. 15 May 94

A method for primary culture of ovine myometrial cells is described. After dissection, myometrium of ewe uteri was digested in trypsin and collagenase. The cells were preplated for 1 h at 37 degrees C. The non-attached cells were grown in appropriate medium supplemented with 2% fetal calf serum. They had a doubling time of 3 days, reached confluency at 10 days and did not exhibit contact inhibition. Cultures were maintained up to 22 days. Characterization of the cells was achieved by electron microscopy, analysis of myosin in cell extracts and assessment of hormone sensitivity. The cells were found to contain myofilaments, characteristic of smooth muscle. A high content of myosin (6--13%) was demonstrated on SDS-polyacrylamide gel electrophoresis: this was confirmed by ATPase activity assay. Cells responded to estradiol stimulation by increased protein synthesis, and bound [3H]estradiol in a specific and saturable way. These results suggest that myometrial cells grown in primary culture should provide a useful model for studying the hormonal control of contractile protein synthesis.
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PMID:Myometrial cells in primary culture: characterization and hormonal profile. 15 21

A cell suspension was prepared from immature rat ovaries by treatment with trypsin and collagenase. The isolated cells were capable of converting [8-14-C]adenine to cyclic [-14-C]AMP and the rate of this conversion was stimulated in vitro by luteinizing hormone and human chorionic gonadotropine, but not by prolactin, norepinephrine, dopamine or albumin. The accumulation of progesterone was also measured in these cells by radioimmunoassay. In vitro addition of luteinizing hormone and human chorionic gonadotropine, but not by prolactin, norepinephrine, dopamine or albumin. The accumulation of progesterone was also measured in these cells by radioimmunoassay. In vitro addition of luteinizing hormone stimulated the accumulation of radioimmuno-assayable progesterone. The conversion of [8-14-C]adenine to cyclic [-14-C]AMP showed a rapid increase during the first 30 min of the incubation period when luteinizing hormone was added to the incubation medium. Progesterone accumulation in response to the same dose of luteinizing hormone showed a lag period for the first 30 min of incubation after which there was an increase up to 2 h. The luteinizing hormone-induced progesterone accumulation was sensitive to puromycin, but there was no effect on the luteinizing hormone-induced increase in cyclic [-14-C]AMP formation from [8-14-C]-adenine. Actinomycin D also inhibited the luteinizing hormone-induced progesterone accumulation in rat ovarian interstitial cell suspension is preceded by an increased accumulation of cyclic AMP and that the accumulation of steroid under the influence of luteinizing hormone involve processes sensitive to puromycin and antinomycin D.
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PMID:Stimulatory effect of gonadotropins on the synthesis of adenosine 3': 5'-cyclic monophosphate and progesterone by suspensions of rat ovarian interstitial cells. 16 26

By treatment of chorioallantoic membranes from embryonated eggs with collagenase and hyaluronidase before the conventional application of trypsin cells could be grown in culture which supported growth of a large variety of myxoviruses, herpesviruses, avian reoviruses and the infectious bronchitis virus of chickens. The cultures could be used for sensitive plaque assays and neutralization tests.
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PMID:In vitro cultivation of cells from the chorioallantoic membrane of chick embryos. 16 93

Transformation of the chick fibroblast surface has been studied in cells infected with Schmidt-Ruppin Rous sarcoma virus and the temperature-sensitive mutant of this virus, TS-68. Major findings following transformation induced by a shift from nonpermissive (41 C.) to permissive (36 C.) temperature in TS-68 infected cells were: (1) rapid cessation or slowing of the synthesis of a protein, M.W. 100-200,000, localization uncertain; (2) cessation or slowing of the synthesis of a plasma membrane protein, M.W. 45,000, within 2-4 hours; (3) cessation or slowing of the synthesis of a large trypsin- and collagenase- sensitive protein (M.W. greater than 200,000) only after an extended period of morphologic transformation. In addition, increased quantities of type-specific viral antigen in the membranes of infected cells were observed in TS-68-infected cells at 41 compared with 36 C.
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PMID:Comparisons of major cell-surface proteins of normal and transformed cells. 16 7

To obtain pure culture of epidermal cells from small human biopsies, two different techniques were tested and compared, i.e. separation of epidermis from corium before cultivation by trypsin and suction, and after cultivation by trypsin and collagenase. The most active growth of epidermal cells was obtained by the third technique, since short-term trypsin treatment released only fibroblasts from the culture. Crude collagenase (type I) was less effective than trypsin. Collagenase type II, III and IV had no effect on fibroblast release. Neither trypsin nor collagenases dispersed epidermal cells.
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PMID:Separation of human epidermal cells from fibroblasts in primary skin culture. 16 87

Endothelial cells from porcine aorta and inferior vena cava have been harvested, using trypsin, EDTA or collagenase, and grown in tissue culture. Growth-behaviour, cytology, scanning and electronmicroscopy findings are reported. It is hoped that this technique will prove useful in the investigation of atherosclerosis.
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PMID:The porcine endothelial cell in tissue culture. 16 26

A new method for the preparation of cell suspensions from human newborn kidneys is described. It involves the use of a mixture of trypsin-ethylenediaminetetraacetic acid and collagenase. The cell yields obtained after tissue dispersion by this method were significantly greater than those obtained after dispersion with either trypsin or ethylenediaminetetraacetic acid alone or in combination. When kidneys were removed 12 h or more postmortem from refrigerated cadavers, higher cell yields were obtained from renal tissue stored overnight at 4 to 6 C in CMRL ATM (Healy and Parker, 1966), as compared to cell yields obtained from kidneys processed immediately upon removal. This observation was confirmed by controlled experiments performed with rabbit kidneys.
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PMID:Dispersion and cultivation of renal cells after short-term storage of kidneys. 17 Mar 18

Latent collagenase, subject to activation by trypsin, was found in culture fluids of cells and tissues from several mammalian sources. The activation requires exposure to enzymatically active trypsin and cannot be achieved by inhibited or by heat-inactivated trypsin.
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PMID:Trypsin activation of latent collagenase from several mammalian sources. 17 Jun 66

1. An activator catalysing specifically conversion of latent forms of human leucocyte collagenase and gelatin-specific protease into the active forms, has been isolated from rheumatoid synovial fluid and purified 55-fold with a yield of 16%. 2. Molecular weight of the activator is about 35 000. 3. The activator is thermolabile, and is irreversibly inactivated at pH below 5.5 or in the presence of low concentrations of trypsin or papain; it is resistant to the action of lysozyme, hyaluronidase, diisopropylfluorophosphate, soybean trypsin inhibitor, p-chloromercuribenzoate, iodoacetamide and dithiothreitol. 4. The activator did not show any activity towards collagen, gelatin, casein, haemoglobin, histones, elastin or p-phenylazobenzyloxycarbonyl-peptide.
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PMID:Isolation, purification and properties of a factor from rheumatoid synovial fluid activating the latent forms of collagenolytic enzymes. 17 Jul 64


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