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)

To determine the effects of relaxin, oxytocin, and prostaglandin F2 alpha on progesterone secretion, bovine luteal cells from different stages of gestation were dispersed in Medium 199 with 200 units/ml penicillin, 1.0% kanamycin, 0.5% bovine serum albumin, and 400 units/ml collagenase. Cells (10(5) were cultured in 400 microliters of Dulbecco's modified Eagle's medium and Ham's F-12 medium containing fetal bovine serum and antibiotics, in Falcon multiwell plates, in a humidified environment of 95% O2 and 5% CO2 at 37 degrees C. Cells were cultured for 24 hr without treatment and thereafter with medium-hormone replacement every 24 hr. Progesterone was quantified from unextracted media by radioimmunoassay. Basal progesterone secretion after 24 hr was 1.81 +/- 0.14, 1.76 +/- 0.17, 0.54 +/- 0.49, and 0.57 +/- 0.21 pg/ml per viable luteal cell from 145-, 165-, 185-, and 240-day-old corpora lutea, respectively. Basal progesterone secretion increased (P less than 0.05) with time in culture. Relaxin induced a dose-dependent (greater than 100 ng/ml) increase in progesterone release, compared with the controls. Oxytocin and prostaglandin F2 alpha induced greater release (P less than 0.05) of progesterone than relaxin at all stages of gestation, but progesterone release was dependent on the stage of gestation and the duration in culture. Luteinizing hormone (100 ng/ml) stimulated whereas 17 beta-estradiol (50 ng/ml) inhibited progesterone secretion by luteal cells at all stages of gestation examined. Relaxin obliterated the prostaglandin- and oxytocin-induced progesterone secretion by bovine luteal cells from 145 to 214 days of gestation. Thus, relaxin, cloprostenol, and oxytocin regulate progesterone production by cultured bovine luteal cells, but hormone secretion was dependent on the stage of gestation.
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PMID:Relaxin, oxytocin, and prostaglandin effects on progesterone secretion from bovine luteal cells during different stages of gestation. 223 7

Epidermolysis bullosa is a group of disorders whose common primary feature is the formation of blisters following trivial trauma. Recessive dystrophic epidermolysis bullosa (RDEB), a subtype of epidermolysis bullosa, is frequently associated with growth retardation. This growth retardation has been reported to be caused by trophopathy following protein loss through skin lesions. Endocrine disorders as the cause of growth retardation in RDEB have not been clearly described. An 11-year-old female had a typical RDEB with dwarfism. Her height was 125 cm and weight was 21 kg, both of which were 2.5 SD below the average. The skin lesions were generalized and probably caused by undernourishment, infection, and blood loss through the skin. However, her serum albumin was at the lower normal limit, and the rapid turnover proteins were slightly decreased. Endocrinological examinations revealed that all the basal levels of pituitary, thyroid, and adrenal hormones were normal. Results of the exercise test, the insulin tolerance test, and the growth hormone-releasing factor test indicated the presence of hypothalamic disorder in secretion of growth hormone. This is the first report of RDEB in which hypothalamic disorder in growth hormone secretion was investigated. On the other hand, growth hormone is known to be involved in collagen metabolism, and a decrease in collagen fibrils and an increase in collagenase activities are found in the skin of RDEB. This implies that this hypothalamic disorder in growth hormone secretion may be involved in the pathophysiology of both dwarfism and the skin lesions in RDEB.
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PMID:[A case of recessive dystrophic epidermolysis bullosa associated with dwarfism with special reference to pathophysiological role of growth hormone]. 233 81

Cell subsets have been discriminated in cell suspensions derived from 37 human head and neck tumors by means of light scatter, DNA, and cytokeratin flow cytometry (FCM). Cell dispersion was performed overnight at 4 degrees C in two different enzyme mixtures, i.e., trypsin/dithioerythritol and collagenase/DNase, under slight agitation of sliced tumor tissue. Cells were examined before and after fractionation on a discontinuous low-density bovine serum albumin (BSA) gradient. Forward and right-angle light scatter FCM of 23 tumor specimens revealed four main subpopulations with different size and structure. Fractionation of primary cell suspensions on a BSA gradient at unit gravity separated debris, small cells and large cells. DNA FCM of the enriched populations demonstrated a relation between large cells and DNA aneuploidy. Epithelial cells, as recognized by cytokeratin antibodies, were also related with large cells. The results demonstrated the usefulness of light scatter, DNA, and cytokeratin analysis of crude and fractionated tumor cell suspensions for assessment of the efficacy of a particular dispersion technique and to obtain information of the cell subsets dispersed.
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PMID:Cell size, DNA, and cytokeratin analysis of human head and neck tumors by flow cytometry. 241 57

In order to study the influence of the colloid osmotic pressure on albumin and total liver protein synthesis, rat hepatocytes were isolated by collagenase perfusion and incubated in Krebs-Ringer-buffer for 4 h. The colloid osmotic pressure produced by different bovine serum albumin (BSA) or dextran 60 concentrations varied from 3 to 80 mm Hg. A physiological colloid osmotic pressure of 20 mm Hg was obtained with 5.7 g BSA or 3.7 g dextran 60 per 100 ml of buffer. Albumin synthesis was measured by Laurell rocket immunoelectrophoresis. Total liver protein and total secretory protein synthesis were determined by the measurement of 1-14C-leucine incorporation. Albumin synthesis was not primarily regulated by the colloid osmotic pressure as was demonstrated by a lack of inhibition after addition of BSA. There was no significant influence of the oncotic pressure on the incorporation of 14C-leucine into total liver proteins. The incorporation into total secretory proteins was inhibited by an increasing colloid osmotic pressure, mediated either by BSA or dextran, suggesting an inhibition of the secretion of plasma proteins other than albumin.
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PMID:Is albumin synthesis regulated by the colloid osmotic pressure? Effect of albumin and dextran on albumin and total protein synthesis in isolated rat hepatocytes. 241 34

We wished to determine whether the stimulation of protein synthesis by CCK8, carbachol, and insulin in isolated rat pancreatic acini resulted from translational or transcriptional induction of protein synthesis, and whether these hormones had similar or different effects on the rates of synthesis of individual enzymes. Isolated pancreatic acini were prepared from streptozocin-treated rats by collagenase digestion, mechanical dissociation, and centrifugation through a bovine serum albumin (BSA) cushion. Sixty-minute incubations, with maximally effective doses of CCK8, carbachol, and insulin, produced a 50, 90, and 100% increase, respectively, in the rate of protein synthesis. After inhibition of transcription with actinomycin D, the hormones still produced a 23, 50, and 61% increase, respectively, in the rate of protein synthesis. The study of the effect of the three hormones and the combination of CCK8 and insulin on the rate of synthesis of trypsinogen, chymotrypsinogen, lipase, and amylase, purified by isoelectric focusing, demonstrated that the hormones induced similar effects on the pattern of enzyme synthesis, and that they all induced the rate of synthesis of chymotrypsinogen slightly more than that of the other enzymes studied. We conclude that the hormones studied exert similar posttranscriptional influences in the regulation of protein synthesis in the pancreatic acinar cell.
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PMID:Translational control of protein synthesis in isolated pancreatic acini: role of CCK8, carbachol, and insulin. 243 15

There is an increasing interest in culturing of insect cells, which are host for arthropod-born (Arbo) viruses. The potential applications of Arbo viruses are in the following two main fields: 1. Medical applications (e.g. preparation of viral vaccines and viral antigens for diagnostic purposes). 2. As bioinsecticides in pest control in horticulture, agriculture and forestry. One of the potential cell substrates for these applications is an anchorage-dependent-mosquito cell line established from embryonic tissues of Aedes aegypti (AA). The following areas were investigated in the reported research with the AA cell line: The AA cells were successfully propagated in microcarrier (MC)-culturing-systems. Of the tested MC's the cellulose-based microgranular MC (DE-53 of Whatman, having an exchange capacity of 2 meq/g) was found to be the best MC. Cells grew in MCs-cells aggregates in submerged spinner culture. The AA-MC's culture was successfully scaled-up to 8 litre culture volume. "Trypsinization" of the AA cells from the MC surface is successfully done by RDB, a dispersion agent from a plant origin (produced and marketed at the author's Institute). Other known dispersion agents (trypsin, collagenase, pronase) failed to disperse the AA cells from the MC. A serum-free medium was developed for culturing the AA cells on the DE-53 MC's. Bovine serum albumin was the main serum substituant in the developed medium. Arboviruses, from the Toga group, were grown in the AA-MC culture. Sindbis virus (from alpha-group) and West Nile virus (from the Flavi group), chronically infected the AA cells, which continuously produce and liberate these two viruses.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Microcarriers as a culturing system of insect cells and insect viruses. 243 74

The labeling pattern of mouse embryonic eye frozen sections incubated with radioiodinated brain acidic and basic fibroblasts growth factors (aFGF and bFGF) was investigated by autoradiography. Both growth factors bind to basement membranes in a dose-dependent way, with a higher affinity for bFGF. Similar data were obtained with eye-derived growth factors (EDGF), the retinal forms of FGF. There was a heterogeneity in the affinity of the various basement membranes toward these growth factors. The inner limiting membrane of the retina and the posterior part of the lens capsule have a higher binding capacity than the posterior part of the Bruch's membrane. The specificity of the growth factor-basement membrane interaction was demonstrated by the following experiments: (i) an excess of unlabeled growth factor displaced the labeling; (ii) unrelated proteins with different isoelectric points--gelatin, serum albumin, histones--did not modify the labeling; and (iii) iodinated EGF or PDGF did not label basement membrane. In order to get a better understanding of the nature of this binding, we performed the incubation of the frozen sections with iodinated FGFs preincubated with various compounds: (i) heparin which is known to have a strong affinity for aFGF and bFGF partially decreases the labeling, and (ii) chondroitin sulfate B and dextran sulfate at high concentrations were also partially effective. In addition, enzymatic treatment of the sections reveals that only heparitinase, not collagenase or chondroitinase ABC, completely prevents the labeling without destroying the overall structure of the basement membrane. An antibody against the proteic part of EHS mouse proteoheparan sulfate does not affect the signal. Esterification of the acidic groups cancelled the binding. These results demonstrate that FGFs bind specifically to basement membranes, probably on the polysaccharidic part of the proteoheparan sulfate, and suggest that this type of interaction may be a general feature of the mechanism of action of these growth factors.
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PMID:Specific fixation of bovine brain and retinal acidic and basic fibroblast growth factors to mouse embryonic eye basement membranes. 244 16

The tissue sites of monomeric IgA (mIgA) catabolism were determined in a BALB/c mouse model. Mouse mIgA myeloma proteins were labeled either by direct iodination or by coupling the residualizing label, dilactitol-125I-tyramine (125I-DLT) to the proteins; catabolites from protein labeled with 125I-DLT accumulate at the site of protein degradation, allowing identification of the tissue and cellular sites involved in catabolism of the protein. The circulating half-lives of 125I- and 125I-DLT-mIgA were the same. The distribution of radioactivity in tissues was measured at 1, 3, 24, and 96 h after iv. injection of 125I-DLT-labeled mIgA, dimeric IgA (dIgA), IgG, or mouse serum albumin. The greatest uptake of 125I-DLT-mIgA was attributable to the liver. This organ accounted for more internal catabolism of mIgA than all other tissues combined. In contrast, 125I-DLT-IgG was catabolized equally in skin, muscle, and liver. These data indicate that, in mice, the liver is the major site of mIgA catabolism. To determine the cell types involved, collagenase digestion was used to isolate parenchymal and non-parenchymal cells from perfused liver of animals injected with 125-DLT-mIgA. Most of the radioactivity was associated with the hepatocyte fraction, even though both cell types showed uptake of 125I-DLT-mIgA. Inhibition studies, with asialofetuin and mouse IgA demonstrated that the uptake of mIgA by liver cells was mediated primarily by the asialoglycoprotein receptor.
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PMID:The sites of catabolism of murine monomeric IgA. 245 58

Longitudinal muscle strips adhered with myenteric plexus were subjected to enzyme digestion under controlled conditions in a Krebs-bicarbonate buffer solution containing a mixture of collagenase, deoxyribonuclease, protease, choline chloride, and bovine serum albumin for 30 min at 37 degrees C. Myenteric ganglia, singly or in multiple aggregates, were harvested with micropipette and labeled with [3H]choline for [3H]acetylcholine (ACh) release studies. When examined by light or electron (transmission or scanning) microscopy, the ganglia exhibited their normal structural characteristics with axon bundles, dendrites, cell bodies, and vesiculated processes. Depolarization with elevated potassium or veratrine hydrochloride significantly elevated the efflux of [3H] ACh. Perfusion with tachykinins (substance P and substance K), vasoactive intestinal peptide, forskolin, or serotonin also significantly increased the release of [3H]ACh. This study demonstrated that enzyme-dissociated myenteric ganglia, notably free of muscle or connective tissue components, were structurally well preserved and were amenable to functional studies targeted specifically for the enteric plexus neurons.
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PMID:Characterization of acetylcholine release from enzyme-dissociated myenteric ganglia. 253 38

Isolation of islets of Langerhans from the pancreas by action of collagenase, a major breakthrough for physiological studies in vitro, has long appeared empirical, and the results were sometimes unpredictable. Isolation yields (number of islets obtained per pancreas) and their reproducibility, purification from exocrine remnants and vitality of the islets obtained, can improve owing to precise techniques, adapted to the architecture of collagen in the pancreas. We have tested four isolation-purification techniques in the rat pancreas. The best results were obtained by combining intra-ductal collagenase injection, with complete but moderate distension of the gland, avoiding leakage, multistep digestion (in situ and then in vitro), followed by purification on a discontinuous bovine serum albumin (BSA) gradient. Average yields were 670 +/- 40 islets per pancreas (range 570-800), versus 170 +/- 9 (range 40-350) with the technique used initially. The use of BSA discontinuous gradient improved the purification yield: 90-96% of islets obtained were concentrated in the 26/29% BSA interface. Furthermore, this technique shortened the duration of purification step: 1 hr (centrifugation gradient) vs 3 hrs (handpicked). It was verified that islets were morphologically free of exocrine tissue. Islet structure was well preserved either in conventional histology or insulin and glucagon immunoperoxidase staining. Islet vitality, as assessed by trypan blue exclusion test, was 100% of freshly isolated islets, and 89% after 24 hrs culture. Insulin secretory responses to a given stimulus were stronger than in the case of islets isolated by former techniques: 10-12 times the basal release (vs 5 times) with clear dose-response proportionality.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Reproducible high yields of rat islets of Langerhans. 254 70


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