Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Streptococcus equi was found to adhere to tongue, cheek and nasal epithelial cells of ponies, in vitro. Maximum adherence was observed at pH 7.5 after one hour of incubation of bacteria with epithelial cells. This adherence was more on epithelial cells from adult animals than from foals. Streptococci exposed to heat (60 degrees C for 10 min) or treated with pepsin or trypsin showed a reduced adherence, whereas an increase occurred on treatment with hyaluronidase. Antibodies against whole S. equi cells or M-like protein blocked the adherence, whereas antibodies against group-specific carbohydrate or lipoteichoic acids did not. Pretreatment of epithelial cells with either the M-like protein or crude extract of S. equi lowered the adherence, whereas an extract of S. zooepidemicus did not. Adherence of S. equi to the epithelial cells was considered to be mediated by structures specific to S. equi.
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PMID:Adherence of Streptococcus equi on tongue, cheek and nasal epithelial cells of ponies. 664 8

Studies were conducted of the content of ferments with which metacercariae of trematodes of the genus Diplostomum affect the tissues of the host's crystalline lens. The following ferments were found in exudates of metacercariae: pepsin, cathepsin, hyaluronidase and lipase. Their activity depends to a great extent on temperature. Considerable changes in the biochemical content of crystalline lens infected with the parasites were found. The character and force of pathogenic effect of diplostomatids on fishes depend on the factors associated with activation and inhibition of ferments of metacercariae, temperature and the presence of ions-inhibitors in particular.
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PMID:[Enzyme activity of metacercariae in the genus Diplostomum (Trematoda, Diplostomidae)]. 673 24

Culture-produced subendothelium (SE) has been prepared from cultured porcine aortic endothelial cells (ECs) by a rapid freeze-thaw, ice-shearing method. En face preparations of this in situ SE material are essentially free of intact or damaged cells and cell debris and consisted of an extensive meshwork of microfibrillar and amorphous material. Washed porcine platelets reacted extensively with this SE material and were associated with the SE as single adherent platelets, single spread platelets, and varying-sized platelet aggregates or 'microthrombi'. Platelet aggregates were associated only with the damaged or frayed edges of the SE, and the platelets had undergone extensive SE-induced contraction and degranulation, as indicated by transmission electron microscopy. Platelet-SE interaction was affected by pH, calcium, platelet concentration, rapid shaking and exposure time. Platelet-SE interaction was significantly enhanced by the addition of 0.1-1% citrated plasma or purified porcine F.VIIIR:WF. Pretreatment of the SE with thrombin, elastase, neuraminidase or hyaluronidase had no effect on platelet-SE interaction, whereas pretreatment with pepsin, plasmin, trypsin, alpha-chymotrypsin or collagenase decreased or completely abolished all platelet-SE interaction. Extraction of the SE with various solutions (high salt, detergents, etc.) had no effect on platelet-SE interaction, only solutions containing sodium dodecyl sulfate completely abolished all platelet-SE interaction.
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PMID:Culture-produced subendothelium. I. Platelet interaction and properties. 680 25

Collagen was isolated from human placenta by pepsin digestion and salt precipitation. This collagen was similar in its electrophoretic mobility and immunological reactivity with monoclonal antibody to form B of type VI collagen in the literature (Trueb B, Schreier T, Bruckner P and Winterhalter K. 1987. Eur. J. Biochem. 166: 699-703). We prepared polyclonal rabbit antiserum against alpha 2 chain of type VI collagen and performed an immunohistochemical study using this polyclonal antibody. It reacted in fat tissue and around vessels and peripheral nerves in normal human skin. To confirm the presence of type VI collagen in fat tissue, we isolated collagen from human subcutaneous tissue. This collagen showed a similar pattern in polyacrylamide gel electrophoresis with that from human placenta and cross-reacted with monoclonal or polyclonal antibody against type VI collagen. By immunohistochemical staining, abundant type VI collagen was observed in the septum of subcutaneous fat tissue in morphea or systemic sclerosis. In the mild hyalinizing areas or after treatment with 6M urea or hyaluronidase in highly hyalinized areas, the staining of type VI collagen increased. These data suggest that the amount of type VI collagen in subcutaneous tissue is involved in the early phases of these fibrosing disorders and that type VI collagen accumulates even more in hyalinizing tissue in late phases of these diseases.
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PMID:Human type VI collagen: purification from human subcutaneous fat tissue and an immunohistochemical study of morphea and systemic sclerosis. 756 Apr 37

This study demonstrated that semenogelin I and II, the predominant and the major basic human seminal coagulum proteins respectively were shown to be potent activators of sperm hyaluronidase. These proteins stimulated the activity of bovine testicular hyaluronidase, goal cauda sperm hyaluronidase and human ejaculated sperm hyaluronidase. Human seminal plasma protein, which predominantly contains the basic degradation residues of the basic coagulum proteins and albumin (pI 4.7) and which is also basic at the assay pH 3.8, also showed activation of bovine testicular hyaluronidase while acidic pepsin (pI < 1.0) exhibited no such activation. The findings may be utilized as an assay method for comparative evaluation of specific activation units of the purified basic seminal coagulum proteins or their cleavage products and for quantifying the total basic protein (pI > 3.8) units in human seminal plasma. One unit of the coagulum protein was defined as the amount of the activator that increases 1 mIU of hyaluronidase activity by 50%. The specific activity of the 57 kDa and 75-79 kDa coagulum proteins, and that of serum albumin against Sigma bovine testicular hyaluronidase (type IV), were 11,447, 8600 and 6252 units per mg protein respectively. It was speculated that human seminal coagulum proteins may have an activation effect on spermatozoal hyaluronidase activity in vivo.
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PMID:Sperm hyaluronidase activation by purified predominant and major basic human seminal coagulum proteins. 858 73

Structural and compositional variations are marked in tendon fibrocartilages, which appear at the insertion to bone and in areas subjected to compressive plus frictional loading regime. We are interested in characterizing the extracellular matrix adaptations in these areas, in an attempt to understand cellular responses to biomechanics. In this work, we have applied immunocytochemistry and an ATP treatment for the ultrastructural identification of type VI collagen, to tendons subjected to compressive forces in different species. Immunocytochemistry, after testicular hyaluronidase or pepsin digestion, revealed the presence of type VI collagen in tensional and compressive areas of the plantaris longus tendon of the bullfrog, in the deep flexor tendon of dogs and rabbits, in the calcanear tendon and the suprapatela of rats and in the gastrocnemius tendon of chickens. In each tendon, the tensional region showed a weak reaction, restricted to the collagen fiber surface. However, the compression region was especially rich in type VI collagen, which accumulates in the interfibrillar spaces and is concentrated around the fibrochondrocytes. Intense reaction was also found in the paratenon. The ATP treatment not only allowed for the detection of the typical ladder-like aggregates of type VI collagen in the same areas identified by immunocytochemistry, but also demonstrated that type VI collagen forms a microfibrillar network around the fibrochondrocytes. Besides the function of organizing groups of collagen fibrils, type VI collagen seems to assemble the pericellular matrix in tendon fibrocartilages, perhaps through physical interactions with the large proteoglycans that concentrate in the same area.
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PMID:Identification and distribution of type VI collagen in tendon fibrocartilages. 1045 5

This assay employs a biotinylated heparan sulfate glycosaminoglycan (HSGAG) substrate that is covalently linked to the surface of 96-well immunoassay plates. The ratio of biotin:HSGAG and the coating concentration of substrate bound to the wells have been optimized and allow removal of biotin HSGAG within 60 min of incubation at 37 degrees C in assay buffer with a standard dilution of bacterial heparitinase or platelet heparanase. Loss of biotin signal from the well surface is detected on incubation with peroxidase-streptavidin followed by color development using 3,3',5,5'-tetramethylbenzidine as the peroxidase substrate. The new assay allows specific detection of heparanase activity in multiple samples in a total time of 3 h including a 1-h substrate digestion step and is a significant improvement with regard to sensitivity, specificity, and ease of handling of multiple samples compared to other described assays. Heparanase specifically degrades the biotinylated HSGAG substrate, when used with an optimized assay buffer. A range of enzymes including collagenase, trypsin, plasmin, pepsin, chondroitinases, hyaluronidase, and neuraminidase show no effect on the substrate under optimized assay conditions. The covalent linkage of the substrate to the well prevents leaching of substrate and allows preparation and long-term storage of substrate-coated plates. The assay can be used to detect heparanase levels in clinical samples and cell culture supernatants and is ideal as a screening method for antagonists of enzyme activity.
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PMID:A multiwell format assay for heparanase. 1292 26

The aim of this study was to provide an effective procedure for immunohistochemistry (IHC) investigations of bone specimens. Samples from rat femoral and human vertebral bone were processed with a detailed and effective IHC protocol summarized here. First, a novel antigen retrieval (AR) method of hyaluronidase combined pepsin predigestion (H+P) was established and the optimal concentration and pH value for AR of bone specimens were determined. Second, the newly developed method was compared with existing AR methods (boiling in sodium citrate, hyaluronidase predigestion (H) and pepsin predigestion (P), with PBS only as the negative control) using two chromogenic detection systems (horseradish peroxidase (HRP) and alkaline phosphatase (AP)) to evaluate their efficacy in obtaining the best IHC results for bone samples. Considering the drawbacks of significant shrinking and detachment from slide for heat retrieval methods and the only moderate immunolabeling for H and P, H+P was the optimal AR method for IHC of bone specimens with the advantages of both good morphological preservation and strong immunoreactivity. Moreover, AP-mediated chromogenic detection was superior to HRP-labeled chromogenic detection due to significantly less non-specific staining. In conclusion, we presented an effective and practical IHC protocol for bone specimens characterized by H+P predigestion combined with AP-mediated chromogenic detection. Finally, a detailed troubleshooting guide was provided for common mistakes that occur during IHC processing of the bone tissue samples.
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PMID:An effective and practical immunohistochemical protocol for bone specimens characterized by hyaluronidase and pepsin predigestion combined with alkaline phosphatase-mediated chromogenic detection. 2527 39


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