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:3.2.1.36 (hyaluronidase)
4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Previous studies have shown that bovine retinas incubated with [3H]galactose incorporated it, unmodified, into large molecules. Light and electron microscope autoradiography showed a significant proportion of the label to be in cone inner segments, and pulse-chase studies showed it was subsequently transported to the synaptic pedicles. In this report, evidence is presented to show that the galactose-labelled macromolecules are resistant to hydrolysis by proteolytic enzymes, testicular hyaluronidase, chondroitinase ABC, beta-glucosidase and beta-glucuronidase, but are readily degraded by alpha-amylase and beta-galactosidase, and to a lesser extent by beta-amylase. Treatment with alpha-amylase also leads to specific removal of radioactivity from cone inner segments and pedicles, as judged by light-microscopic autoradiography. These studies appear to indicate that the cone-specific galactose label is in glycogen or glycogen-like molecules.
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PMID:D-[3H]galactose incorporation into glycogen in retinal cone cells. 231 72

Tissue culture conditions can modulate apparent levels of incorporation of the radiolabeled precursor [3H]glucosamine into hyaluronic acid in cells. A careful study was made on the effects of culture conditions on human skin fibroblasts. A newly described technique to measure hyaluronic acid was utilized based on incorporation of [3H]glucosamine into cetylpyridinium chloride-precipitable hyaluronidase-digestible material. The precipitate was collected on glass fiber filters using a manifold suction apparatus. A six-fold greater level of incorporation occurred in rapidly growing preconfluent than in confluent fibroblasts. Ascorbic acid stimulated incorporation with a maximum at 25 micrograms/ml. The same ascorbic acid optimum was observed for collagen prolylhydroxylation. When beta-hydroxybutyrate was used as an energy source instead of D-glucose, a 3.5-fold increase in levels was observed. All tissue-culture media examined supported comparable levels of incorporation, except for Roswell Park Memorial Institute Media-1640, in which cells had only half the level. Fetal calf serum supported high levels of incorporation in a dose-dependent manner, while newborn calf and calf sera supported much lower levels of incorporation. Under serum-free conditions, lactalbumin hydrolysate was best able to support incorporation of hyaluronic acid. In the search for mechanisms that modulate hyaluronic acid, it is critical to consider the tissue culture conditions under which incorporation of radiolabeled precursors are being examined.
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PMID:Levels of [3H]glucosamine incorporation into hyaluronic acid by fibroblasts is modulated by culture conditions. 237 20

Fifty-eight consecutive patients with advanced cancer who required parenteral hydration were treated with hypodermoclysis. A solution of two-thirds 5% dextrose and one-third saline was used in all cases at a rate of 20-100 cc/hr, with 750 units of hyaluronidase per liter, and 20-40 mEq KCl/L were administered in all patients. In 38 patients, morphine (21 cases) or hydromorphone (17 cases) were added. The mean duration of infusion and volume were 14 +/- 9 days and 1.3 +/- 0.8 L/day, respectively (range, 0.5-3 L/day). Mean dose of KCl was 25 +/- 8 mEq/L. The reason for discontinuation was death in 43 cases, oral hydration in 12 cases, and need for fluid restriction in 3 cases. Toxicity consisted in local infection in two cases and bruising in two cases. We conclude that hypodermoclysis is a safe and effective method of hydration in patients with advanced cancer.
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PMID:Hypodermoclysis for the administration of fluids and narcotic analgesics in patients with advanced cancer. 238

The choice of which neurotransmitters will be produced by a developing neuron is influenced by the microenvironment of the neuron. In this study we show that neuronal contact with membrane-associated molecules promotes expression of peptidergic and cholinergic traits. Treatment of cultured neonatal rat sympathetic neurons with plasma membranes derived from adult rat spinal cord or sympathetic ganglia induced expression of the peptide transmitter substance P and increased levels of the cholinergic biosynthetic enzyme choline acetyltransferase. The transmitter-stimulating activity could be solubilized from spinal cord membranes by the detergent octyl glucoside but not by Triton X-100. The choline acetyltransferase- and substance P-stimulating activity also could be extracted from spinal cord membranes by 4 M sodium chloride, suggesting that the active material is membrane associated rather than an intrinsic structural membrane molecule. Trypsin or heat treatment of the extract destroyed the transmitter-stimulating activity, indicating that the factor contains a protein. Activity also was destroyed by hyaluronidase treatment, suggesting that the active material may contain a glycosaminoglycan. The choline acetyltransferase-stimulating activity in the 4 M NaCl extract was eluted in a single peak from a calibrated Sephadex G-75 column with a retention time slightly less than that of a 25-kDa standard. NaDodSO4/polyacrylamide gel electrophoresis of the active peak revealed a predominant band at 29 kDa. Thus, contact-mediated stimulation of substance P and choline acetyltransferase activity in sympathetic neurons results from neuronal exposure to a 29-kDa membrane-associated factor.
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PMID:Solubilization of a membrane factor that stimulates levels of substance P and choline acetyltransferase in sympathetic neurons. 244 32

Colon cancer cells in culture synthesize and secrete mucin glycoproteins, which carry a number of cancer-associated antigens. However, the structures and mechanisms of biosynthetic processing are not well understood. Mucins synthesized and secreted by LS174T human colon cancer cells were compared to those in LS174T xenografts in athymic mice. Mucins radiolabeled with glucosamine or sulfate were purified by gel filtration and cesium chloride density gradient centrifugation. The mucins were of high molecular weight and were resistant to chondroitinase ABC, hyaluronidase and HNO2 treatment. They were, however, susceptible to pronase digestion and mild alkaline treatment. Using radiochemical precursors, the cellular mucin was shown to contain fucose, galactose, N-acetylgalactosamine, N-acetylglucosamine, N-acetylneuraminic acid, and sulfate. Oligosaccharides released by beta-elimination had N-acetylgalactosaminitol as the reduced amino sugar and also unreduced galactosamine, indicating that there is N-acetyl-galactosamine O-glycosidically attached to protein core and also peripheral N-acetyl-galactosamine not directly linked to protein. DEAE-cellulose chromatography of mucins showed two major peaks with both intracellular and secreted mucins, but xenograft mucins also had more acidic components. Sulfate-labeled mucins were shifted to less acidic peaks by neuraminidase digestion, which indicates that the same mucin molecules are both sialylated and sulfated. We conclude that the intracellular mucins of cultured colon cancer cells, those secreted into the medium, and those in nude mouse xenografts are chemically similar, but differ in sialic acid and sulfate content. This experimental model system, LS174T cells maintained in culture and as nude mouse xenografts, may be useful for further biosynthetic and structural studies of colon cancer mucin.
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PMID:Comparison of metabolically labeled mucins of LS174T human colon cancer cells in tissue culture and xenograft. 273 49

A high-performance liquid chromatographic method for the separation and analysis of the unsaturated tetrasaccharide and hexasaccharide from Streptomyces hyaluronidase (S.HAase) enzyme digestion products of hyaluronic acid (HA) and standard unsaturated disaccharides 2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-D-galactose (delta Di-0S), 2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose (delta Di-4S) and 2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-6-O-sulfo-D-galactose (delta Di-6S) is described. An amino phase chemically bonded to silica with a particle diameter of 6 micron was used as the column. The composition and the pH of the mobile phase were systematically varied to determine the optimal chromatographic conditions for separation and analysis of the compounds. For HA, a complete separation was accomplished in less than 12 min with a practical detection limit of 100 ng. Separation of the disaccharides also required less than 15 min with detection limits of 10 ng for delta Di-0S and 25 ng each for delta Di-4S and delta Di-6S. This chromatographic method represents a significant improvement over existing methods. It allows the simultaneous separation and analysis of HA and chondroitin sulfate isomers (after digestion of the latter with chondroitinase) at a higher speed, and with more sensitivity and efficiency.
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PMID:Rapid and sensitive method for measurement of hyaluronic acid and isomeric chondroitin sulfates using high-performance liquid chromatography. 310 83

The effects of steroid hormones on the synthesis of lactosaminoglycan (LAG)-containing oligosaccharides by mouse uteri are reported. The uterine LAG-containing oligosaccharides were degraded partially by Pseudomonas endo-beta-galactosidase, releasing an oligosaccharide of the apparent structure: Gal beta----N-acetylglucosaminyl(----N-acetylgalactosaminyl)beta 1,3----galactose. A larger fraction of the LAG-containing oligosaccharides bound to pokeweed mitogen than to Datura stramonium lectin, suggesting the presence of highly branched structures. LAG-containing oligosaccharides were resistant to sequential digestion with Pronase, nitrous acid, hyaluronidase, and chondroitinase ABC. These polysaccharides exhibited a Gal:GlcNAc:GalNAc ratio of approximately 1.0:1.0:0.3 and were not fucosylated. The ion-exchange behavior of the LAG-containing oligosaccharides before and after mild acid hydrolysis indicated the presence of sialic acid residues. The LAG-containing glycopeptides were highly resistant to beta-elimination but were released quantitatively by hydrazinolysis, demonstrating an N-linkage to protein. Binding to pokeweed mitogen was markedly enhanced following release of these oligosaccharides from peptides by hydrazinolysis, suggesting that peptide-bound oligosaccharides were partially inaccessible to the lectin. Molecular exclusion chromatography of the oligosaccharides released by hydrazinolysis revealed a broad distribution ranging from Mr 4,000 to 15,000 with a median Mr of approximately 8,000. We extended the above observations by determining how the steroid hormones 17-beta-estradiol (E2) and progesterone affected synthesis of the LAG-containing oligosaccharides in ovariectomized mice. Generally, E2 and a number of E2 agonists stimulated glycoconjugate synthesis; however, chronic E2 treatment or combined treatment with E2 plus progesterone caused the synthesis of most glycosaminoglycans to return to basal levels. In contrast, E2 either alone or in combination with progesterone stimulated synthesis of LAG-containing oligosaccharides in preference not only to glycosaminoglycans but also to other classes of N-linked oligosaccharides. This effect was apparent during both priming and nidatory E2 treatments. Collectively, these data provide the first demonstration of LAG-containing oligosaccharides in uteri and for the hormonally regulated synthesis of lactosaminoglycans. In addition, this is the first demonstration of the ability of steroid hormones to induce the synthesis of certain types of N-linked oligosaccharides in preference to others in the same tissue.
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PMID:Estrogen preferentially stimulates lactosaminoglycan-containing oligosaccharide synthesis in mouse uteri. 312 90

Rat renal papillary collecting duct (PCD) cells were isolated using collagenase and hyaluronidase digestion and a three-step low-speed centrifugation. As assessed by binding of the lectin Dolichos biflorus and determination of vasopressin-sensitive adenylate cyclase and Na+-K+-ATPase, the enrichment of PCD cells over a crude papillary cell preparation was 1.8, 2.4, and 1.4, respectively. Microscopic evaluation indicated that the preparation was greater than 90% pure PCD cells. The isolated cells were viable as evident from the high K/Na ratio of intracellular electrolytes measured by electron probe analysis (5.3), from the high ATP/ADP ratio (2.15), and the metabolic response to alterations in Na transport. Exposure to 2 mM ouabain or removal of Na reduced O2 consumption by 25-35%; the uncoupler carboxylcyanide-m-chlorophenylhydrazone more than doubled O2 consumption. In the presence of 14 mM glucose and at a PO2 of 100 Torr the cells produced substantial quantities of lactate. This aerobic glycolysis may account for greater than 20% of the ATP production. In the presence of rotenone, glycolysis increased by 56% and was able to maintain the cellular ATP level at 65% of control. In the absence of any exogenous substrate PCD cells respired normally and had a close to normal ATP content, but lactate production was markedly decreased. These results demonstrate that viable PCD cells can be isolated from rat kidney. At normal PO2 and in the presence of D-glucose the cells show a substantial amount of aerobic glycolysis, although their mitochondrial respiration is not rate limiting. In the absence of glucose the cells derive the majority of their energy from an as yet unidentified endogenous substrate.
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PMID:Purification of rat papillary collecting duct cells: functional and metabolic assessment. 330 74

Mesenchymal cell aggregates, termed blastema in vivo, precede cartilage differentiation in vivo and in high-density cell cultures. The galactose specific lectin, peanut agglutinin (PNA), has been shown to be blastema specific (B. Zimmermann and M. Thies, 1984, Histochemistry 81, 353-361). PNA appears to be a marker for precartilage cellular aggregates both in vivo and in vitro. Frozen sections of stage 24 chick wing buds were double stained with PNA-rhodamine and by indirect immunofluorescence with antibody directed against type II collagen. The PNA stained the humeral blastema intensely and extended distal to the level of type II collagen. High-density cultures of stage 24 chick wing buds were also evaluated for the distribution of PNA binding. Sixteen-hour cultures showed the earliest consistent appearance of PNA binding. The PNA-stained areas coincided with hematoxylin-stained cell aggregates. PNA staining was inhibited by 50 mM D(+)-galactose and was not sensitive to 1% testicular hyaluronidase pretreatment. No Alcian blue-staining nodules were present yet at 16 hr. The presence of a precartilage, blastema-specific marker in situ, as well as in precartilage aggregates in cultures, suggests the similarities in chondrogenesis between these two conditions. Stage 19 limb bud cultures did not form nodules but did form aggregates that were PNA positive. Furthermore, single cells that differentiated into chondrocytes on collagen gels or after cytochalasin D treatment lacked PNA-binding material. These results suggest that this material is specific to precartilage aggregates. The PNA-positive material was extracellular in distribution and was removed after brief extraction with 0.5 M guanidine hydrochloride.
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PMID:The detection of a precartilage, blastema-specific marker. 355 59

In the distal hypertrophic zone of growth-plate cartilage, the pericellular matrix surrounding individual chondrocytes and the territorial matrix uniting chondrocytes into columnar groups are invaded by metaphyseal endothelial cells prior to osteogenesis. In the present study, lectin-binding glycoconjugates were analyzed in these two matrix compartments of growth-plate cartilage from Yucatan swine. Nine lectin-fluorescein conjugates were tested by a postembedment method on 1-micron-thick, nondecalcified, Epon-embedded sections. Chondrocytes in all cellular zones were surrounded by a pericellular matrix which showed positive binding for peanut agglutinin (PNA), ricin agglutinin (RCA-I), and soybean agglutinin (SBA). Binding by these lectins was sensitive to digestion with hyaluronidase, chondroitinase, and trypsin. Pericellular glyconconjugtes that bind RCA-I and concanvalin A (CONA) after periodic acid oxidation, and which were sensitive to trypsin but not to chondroitinase or hyaluronidase, were present in the hypertrophic cell zone. Within the territorial matrix, binding of lectins specific for galactose, N-acetylgalactosamine, and fucose showed gradients of intensity which became maximal at the last transverse septum. Lectin-binding histochemistry more precisely differentiated the microheterogeneity of glycoconjugate distribution within these two matrix compartments than has been possible with other histochemical techniques. Lectin-binding affinity is a potentially useful technique by which to isolate cartilage matrix macromolecules unique to specific cellular zones of the growth plate.
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PMID:In situ localization of lectin-binding glycoconjugates in the matrix of growth-plate cartilage. 372 44


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