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)

Many skin lesions are specific for diabetes mellitus. Necrobiosis lipoidica, lipoatrophy and idiopathic bullae (bullosis diabeticorum) are usually associated with diabetes. However, diabetic scleredema has not been noticed by internists, although dermatologists have paid attention to such a cutaneous manifestation. We reported a clinical case of a female diabetic patient aged 15 who had been afflicted with diabetic scleredema. She had been treated with insulin since 5 years of age. She noticed stiffness of the skin in April 1980. Skin biopsy showed thickness of the dermis and accumulation of acid mucopolysaccharide. After control of blood glucose with continuous subcutaneous insulin infusion (CSII) and administration of tocopherol acetate and hyaluronidase, the skin lesion improved. Etiology of diabetic scleredema is unknown. Such skin lesion which is observed frequently in insulin dependent obese patients is different from a category of scleredema of Buschke.
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PMID:Diabetic scleredema. 667 Jan 1

We aimed to identified cervical ripening at term pregnancy by measuring acid glycosaminoglycans (aGAG) in nonpregnant and immediately postpartum rabbits cervix and body. aGAG was extracted from the uterine tissues by the modified method of K. Anno (1964) and determined by the carbazole method (Bitter, 1962). Components of aGAG were separated by two dimensional electrophoresis (0.1M pyridine-0.47M formic acid in the first and 0.1M calcium acetate buffer in the second) using acetate cellulose strips. aGAG were separated five spots that were identified hyaluronic acid, heparan sulfate, chondroitin sulfate A, dermatan sulfate and chondroitin sulfate C. These results were confirmed by method of hyaluronidase, chondroitinase AC and ABC digestion test.
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PMID:[Studies on acid glycosaminoglycans in rabbit uterine cervix and body (author's transl)]. 706 98

A beta-N-acetylhexosaminidase [EC 3.2.1.30] was isolated from internal organs of the sea-squirt, Styela plicata. The enzyme was purified 1,560-fold in 5% yield. The preparation was fairly homogeneous as examined by disc and SDS polyacrylamide gel electrophoresis and Sephadex G-200 chromatography. The molecular weight of the enzyme was estimated to be 132,000 by gel chromatography and 66,000 by SDS polyacrylamide gel electrophoresis. Therefore, this beta-N-acetylhexosaminidase was considered to be a dimer. The optimum pH for activity was 4.0 but the enzyme was stable in the pH range from 5 to 6. The isoelectric point was 4.99. This enzyme was inhibited by Fe2+, Hg2+, Ag+, and PCMB but not by acetate. The isolated enzyme hydrolyzed both p-nitrophenyl-N-acetyl-beta-D-glucosaminide and p-nitrophenyl-N-acetyl-beta-D-galactosaminide. The hydrolysis rate of p-nitrophenyl-N-acetyl-beta-D-galactosaminide was 43% of that of p-nitrophenyl-N-acetyl-beta-D-glucosaminide. The enzyme liberated N-acetylhexosamine from asialodegalactosyl ovomucoid glycopeptide, asialodegalactosyl fetuin glycopeptide and the fragment of hyaluronic acid prepared by hyaluronidase treatment.
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PMID:Purification and characterization of a beta-N-acetylhexosaminidase of sea-squirt. 711 68

Because the dermis of myxedematous humans is known to accumulate increased amounts of glycosaminoglycan (GAG), we were prompted to study the effects of thyroid hormone depletion in vitro. Human skin fibroblasts were grown to confluence in medium containing 10% fetal calf serum (FCS). Some cultures were shifted to a medium containing FCS depleted of thyroid hormone (D-FCS) or to a D-FCS medium to which 10(-7) M triiodothyronine (T3) was added (D-FCS + T3). Cultures were then labeled for 16 h with [3H]-acetate, harvested and combined with the media. After pronase digestion, the non-trichloroacetic acid precipitable, non-dialysable material was digested with streptomyces hyaluronidase followed by chondroitinase ABC. Digestable material was separated by G-50 Sephadex column chromatography. The cultures incubated in media containing D-FCS accumulated 2.8-fold more hyaluronic acid and 2.1-fold more chondroitin sulfate than did sister cultures incubated in the presence of D-FCS + T3. The addition of T3 to the D-FCS reduced the amounts of GAG accumulated nearly to the levels observed in cultures grown in FCS. The data indicate that thyroid hormone exerts an inhibitory effect on GAG accumulation in human skin fibroblasts. This model offers the opportunity to study thyroid hormone action in vitro using an easily accessible human tissue.
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PMID:The effect of thyroid hormone on glycosaminoglycan accumulation in human skin fibroblasts. 722 12

Retinal microvessels were isolated from bovine eyes and the basement membranes were purified either directly or after incubation with [35S]sulfate and [14C]glucosamine. The basement membranes, which were purified by osmotic lysis and sequential treatment with detergents, had the general compositional features associated with basement membrane collagens, including high levels of hydroxyproline and hydroxylysine and the presence of 3-hydroxyproline and cystine. After pronase digestion, cellulose acetate electrophoresis of glycosaminoglycans from retinal microvessel basement membrane revealed material comigrating with heparan sulfate that was insensitive to digestion with Streptomyces hyaluronidase ad chondroitinase ABC. Retinal microvessels also incorporated [35S]- and [14C]glucosamine into glycosaminoglycans that were isolated following pronase digestion of the retinal microvessel basement membrane purified from these incubations. The findings provide the first demonstration that glycosaminoglycans are integral components of the retinal microvascular basement membrane and suggest that heparan sulfate is the major glycosaminoglycan species in this basement membrane.
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PMID:Presence of glycosaminoglycans in retinal capillary basement membrane. 723 37

Isolated rat jejunal villus and crypt cells prepared by differential scraping and hyaluronidase dispersion were used in the presence of 8 mM sodium taurocholate to study the incorporation of sn-[3H]glycerol-2-monooleate, [1-14C]palmitate, [1-14C]acetate, L-[4,5(n)-3H]leucine and D-[1-14C]glucosamine into cellular and medium lipids and proteins, respectively. The villus cells were capable of an apparently normal biosynthesis of triacylglycerols and phospholipids, as well as of proteins and glycoproteins despite an altered dye permeability and increased release of cytosolic and membrane enzymes. About 20-30% of the newly formed triacylglycerols and about 35% of the newly formed phospholipids were secreted into the medium and were recovered as triacylglycerol-rich particles. Labelled proteins and glycoproteins were also recovered from this fraction. The crypt cells synthesized about one-half as much triacylglycerol and phospholipid as did the villus cells, but secreted little or no labelled lipid into the postincubation medium. The release into the medium of triacylglycerols synthesized by the villus cells was blocked by a pretreatment of the isolated cells with the microtubule disruptors, nocodazole, colchicine and colcemid; by the amino sugar, D-galactosamine; by the inhibitors of protein synthesis, puromycin and cycloheximide, and by the inhibitor of the biosynthesis of phosphatidylcholine, chlorocholine. These results indicate that the secretion of labelled lipids, proteins and glycoproteins by the upper villus enterocytes in the presence of sodium taurocholate is not entirely due to cell breakage and spillage of contents. It is concluded that incubations of isolated villus cells of rat jejunum with mixed micellar solutions containing 8 mM taurocholate are compatible with an apparently normal biosynthesis and secretion of triacylglycerol-rich particles.
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PMID:Synthesis and release of lipids and lipoproteins by isolated rat jejunal enterocytes in the presence of sodium taurocholate. 728 26

Non-pregnant and pregnant rats of known gestational age were killed at intervals and their uterine cervices were excised and digested with papain. Glycosaminoglycans thus extracted were separated by cellulose acetate electrophoresis and stained with Alcian Blue. Glycosaminoglycans were identified by comparison with standards and by serial degradation with chondroitin ABC lyase, butyl nitrite and leech hyaluronidase. Dermatan sulphate, hyaluronic acid and heparan sulphate were identified and quantitative determined by densitometry. The overall concentration of glycosaminoglycans changed little during pregnancy. A 3-fold total increase in uronic acid paralleled the increase in cervical weight. Hyaluronate content, however, increased 17-fold, and rose from 6% of total glycosaminoglycans in the non-pregnant state to 33% at term. Furthermore, the ratio of hyaluronate to hydroxyproline increased 10-fold. These changes are consistent with an accumulation of hyaluronate in the interstices between collagen fibres, resulting in the softening of this tissue that is seen in late pregnancy.
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PMID:Pregnancy-related changes in rat cervical glycosaminoglycans. 730 89

Synovial fluid (SF) of 16 adult patients with rheumatoid arthritis (RA) and 9 children with juvenile rheumatoid arthritis (JRA) was investigated for the presence of hidden 19S IgM rheumatoid factor (RF). SF was incubated with 500 IU hyaluronidase/g of SF, dialyzed against acetate buffers at decreasing pH, centrifuged and subjected to chromatography on a Sephadex G-200 column. The resulting IgM-containing fraction of SF from 5 seropositive patients (3 adult RA, 2 JRA patients) demonstrated RF activity by the complement-dependent hemolytic assay. Hidden 19S IgM RF was not found in the IgM-containing fractions of SF from 13 adult seronegative RA patients. Hidden 19S IgM RF was shown in the IgM-containing fraction of SF in 4 of 7 children with seronegative JRA.
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PMID:Hidden 19S IgM rheumatoid factor in synovial fluid. 731 Jul 76

The biosynthesis of glycosaminoglycans (GAG) by cultivated rat glomerular epithelial and mesangial cells was studied by incorporation of [35S]sulfate or [14C]glucosamine for 48 h. After dialysis, the incubation medium was subjected to digestion with papain. Labeled GAG were isolated from the digests by precipitation with cetylpyridinium chloride and ethanol. Results of cellulose acetate electrophoresis of the isolated 'epithelial' GAG fraction revealed the presence of two [14C] spots and one [35S] spot. The [35S] spot was identified as heparan sulfate, because it comigrated with the heparan sulfate standard and it was insensitive to testicular hyaluronidase. One [14C] spot comigrated with the [35S] spot and with the heparan sulfate standard. This GAG fraction did not contain galactosamine. The second [14C] spot was identified as hyaluronic acid, since it comigrated with the hyaluronic acid standard and since it was sensitive to testicular hyaluronidase. Results of cellulose acetate electrophoresis of the isolated 'mesangial' GAG fraction revealed the presence of one [14C] spot only. No [35S] spot was detectable. The [14C] spot comigrated with the hyaluronic acid standard and was sensitive to hyaluronidase. The data therefore suggest that the glomerular epithelial cells synthesize and secret both sulfated GAG (heparan sulfate) and nonsulfated GAG (hyaluronic acid) into the culture medium, whereas the glomerular mesangial cells synthesize and secrete nonsulfated GAG (hyaluronic acid) only into the culture medium.
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PMID:Tissue culture of normal rat glomeruli: glycosaminoglycan biosynthesis by homogeneous epithelial and mesangial cell populations. 732 11

The preparation of a proteoglycan (PG) from human aortic intima-media is described. The PG was obtained from intima-media homogenates by differential centrifugation, exclusion chromatography and preparative agarose electrophoresis. Crude or purified preparations of the proteoglycan are capable of forming specific insoluble complexes with LDL, purified or in serum. This product has been labelled lipoprotein-complexing proteoglycan (LCP-3). On agarose and cellulose acetate electrophoresis LCP-3 appears as a single band. However, its glycosaminoglycan (GAG) moiety shows a composition and chromatographic behaviour compatible with hybrid or mixed chains of chondroitin-6-so4, dermatan sulfate and heparin and/or heparan sulfate. The specificity of LCP-3 for LDL disappears when it is treated with testicular hyaluronidase or proteolytic enzymes. Ionic strength, pH, Ca++ and Mg++ modulate the amount of LDL insolubilized. The amino acid composition of the protein from LCP-3 is that of a basic protein(s), perhaps bound covalently through xylose--serine residues to the GAG's. The estimated molecular weight of LCP-3 is 1 to 5 x 10(6) daltons. The presence of LCP-3 to intima-media and its specificity for interacting with LDL at conditions near to physiological ones are suggestive of the role that this type of structure may play in the association of the atherogenic lipoproteins with components of the arterial intima-media.
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PMID:Characterization and properties of a lipoprotein-complexing proteoglycan from human aorta. 736 2


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