Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Analysis of mouse serum hyaluronidase by polyacrylamide gel electrophoresis, with the substrate high-molecular-weight hyaluronan (hyaluronic acid) included in the gel performed in mice of two different strains, BALB/cBy and C57BL/6By, reveals a pattern of multiple enzyme forms specific for each genotype. In BALB/c serum, seven different forms are present, only one of which is found in C57BL/6 serum. Segregation analysis of the enzyme polymorphism in backcross progeny and in recombinant inbred and bilineal congenic lines shows that the difference is due to a single locus, which we have designated as Hyal-1. Hyal-1 is linked to the histocompatibility locus H-7, on chromosome 9.
Somat Cell Mol Genet 1989 Jan
PMID:Hyal-1, a locus determining serum hyaluronidase polymorphism, on chromosome 9 in mice. 291 64

The effect of gossypol on the activities of 10 acrosomal enzymes of the rabbit sperm was evaluated. Acrosin, Azocoll proteinase, neuraminidase, and arylsulfatase were significantly inhibited or completely inactivated by 12-76 microM gossypol. Hyaluronidase, beta-glucuronidase, and acid phosphatase were inhibited only at a higher concentration of gossypol (380 microM). Phospholipase C, alkaline phosphatase, and beta-N-Acetyl glucosaminidase were not inhibited even at 380 microM gossypol. Gossypol was found to be a noncompetitive inhibitor of arylsulfatase with a Ki of 120 microM. The inhibition was reversible and dose-dependent. As the acrosomal enzymes were more sensitive to the inhibition by gossypol compared to sperm enzymes involved in glycolysis or energy production, these assays may serve as a more reliable indicator for monitoring the occurrence of gossypol-induced sterility.
Mol Reprod Dev 1995 Feb
PMID:Inhibition of rabbit sperm acrosomal enzymes by gossypol. 776 16

A recombinant lambda phage was identified in a Clostridium perfringens genomic library by means of its ability to hydrolyse the fluorescent substrate 4-methyl-umbelliferyl-beta-D-glucosaminide, isolated and shown to encode an endo-beta-N-acetylglucosaminidase. This enzyme, NagH, is also known as hyaluronidase, or Mu toxin, a putative virulence factor which is likely to act on connective tissue during gas gangrene. Nucleotide sequence analysis allowed the primary structure to be deduced and showed hyaluronidase to be a large exported protein of 114,392 Daltons and an enzyme of this size, endowed with the corresponding activities, was partially purified from C. perfringens. Hyaluronidase seems to be organised into two domains, an N-terminal region comprising 700 amino acids bearing the active site and a 300-residue C-terminal segment, containing three copies of an extended motif. Two other reading frames, linked to nagH, also appear to encode proteins with sugar-binding motifs.
Mol Gen Genet 1994 Apr
PMID:Molecular genetic analysis of the nagH gene encoding a hyaluronidase of Clostridium perfringens. 817 18

Tissue kallikrein (TK) is secreted by serous cells of tracheobronchial submucosal glands and plays a role in allergic airway responses. To better understand the regulation of TK, we used primary cultures of submucosal gland cells that release TK upon stimulation. Media from cultures stimulated with chymase (10(-7) M) showed increased TK activity (0.50 +/- 0.22 mU/ml mean +/- standard error) in comparison with the control group (0.08 +/- 0.02 mU/ml). The increased TK activity was significantly correlated with increases in the levels of the serous cell marker, secretory leukoprotease inhibitor. Anion exchange chromatography of the conditioned culture media showed that TK activity eluted as a broad peak between 1.6 and 1.8 M NaCl, unlike the reported elution (0.3 to 0.6 M NaCl) of kallikreins from other tissues, suggesting that secreted bronchial TK was bound to a negatively charged molecule. Hyaluronidase digestion increased TK activity in both pre- and post-chymase-stimulated culture media, whereas no such change was seen after samples were digested with heparinase or chondroitinase ABC. Further, after hyaluronidase digestion of media, TK eluted from an anion exchange column between 0.3 and 0.6 M NaCl. Enzymatic detection of TK after nondenaturing gel electrophoresis showed that hyaluronidase digestion also reduced the electrophoretic heterogeneity of TK to a single band, whereas adding back hyaluronic acid (HA) to hyaluronidase-digested samples restored the original heterogeneity. Finally, TK activity bound to HA-Sepharose and could be eluted with HA. These studies show that primary cultures of ovine submucosal gland cells secrete TK in a regulated fashion, and that secreted TK binds to HA. This binding reduces TK enzymatic activity; therefore, factors that affect HA turnover could modify the TK activity in the airway lumen. These events could be important in the regulation of kinin-mediated airway inflammation.
Am J Respir Cell Mol Biol 1999 Dec
PMID:Bronchial tissue kallikrein activity is regulated by hyaluronic acid binding. 1057 63

We tested the hypothesis that matrix glycosaminoglycans contribute to lung tissue viscoelasticity. We exposed lung parenchymal strips to specific degradative enzymes (chondroitinase ABC, heparitinase I, and hyaluronidase) and determined whether the mechanical properties of the tissue were affected. Subpleural parenchymal strips were obtained from Sprague-Dawley rats and suspended in a Krebs-filled organ bath. One end of the strip was attached to a force transducer and the other to a servo-controlled lever arm that effected sinusoidal oscillations. Recordings of tension and length at different amplitudes and frequencies of oscillation were recorded before and after enzyme exposure. Resistance, dynamic elastance, and hysteresivity were estimated by fitting the equation of motion to changes in tension and length. Quasi-static stress-strain curves were also obtained. Exposure to chondroitinase and heparitinase I caused significant increases in hysteresivity, no decrement in resistance, and similar decreases in dynamic elastance relative to control strips exposed to Krebs solution only. Conversely, measures of static elastance were different in treated versus control strips. Hyaluronidase treatment did not alter any of the mechanical measures. These data demonstrate that digestion of chondroitin sulfate and heparan sulfate alters the mechanical behavior of lung parenchymal tissues.
Am J Physiol Lung Cell Mol Physiol 2001 Feb
PMID:Effect of glycosaminoglycan degradation on lung tissue viscoelasticity. 1115 10

This study investigates the effects of aestivation on body water content, body mass, acid mucopolysaccharide (AMPS) and some of its degrading enzymes in different tissues for some Australian desert frogs. The AMPS component of the liver, kidney, skin and cocoon alter during aestivation to help retain water, which is unchanged in most tissues of all frog species, and to protect the frogs from desiccation during extended periods of aestivation. Hepatic AMPS was unaltered in Cyclorana maini, C. platycephala and Neobatrachus sutor but increased significantly after 2 months of aestivation in C. australis. The level of AMPS in the kidney was elevated in all four frog species after 5 months of aestivation. Skin AMPS content in the skin of awake frogs decreases with aestivation period and increases in the cocoon. AMPS in the cocoon probably works as a cement between the cocoons' layers and its physical presence presumably contributes to preventing water flux. Changes in AMPS content in different tissues were accompanied by significant changes in both hyaluronidase and beta-glucuronidase activities, which play an important role in AMPS metabolism. Alcian blue staining of control and digested skin of C. australis and C. platycephala with testicular hyaluronidase indicated the presence of AMPS, concentrated in a thin layer (called ground substance, GS) located between stratum compactum and stratum spongiosum, and acid mucin concentrated in the mucous glands and in a 'tubular' structure which could be observed in the epidermal layer. Hyaluronidase digestion of the cocoon slightly changed the Alcian Blue colour, suggesting the presence of a large amount of acid mucin similar to that found in the skin mucous gland. The results of this study present data for the redistribution of AMPS, which may help in reducing water loss across the cocoon and reabsorption of water in the kidney during aestivation.
Comp Biochem Physiol A Mol Integr Physiol 2002 Apr
PMID:Water content, body weight and acid mucopolysaccharides, hyaluronidase and beta-glucuronidase in response to aestivation in Australian desert frogs. 1189 99

Hyaluronidase activity was detected and partially characterized in salivary gland extracts of females of six sand fly species. In Phlebotomus papatasi and Lutzomyia longipalpis the enzyme was active over a broad pH range; the pH optimum was 5.0. Besides high cleaving activity towards hyaluronic acid, it hydrolyzed chondroitin sulfates A and C. Hyaluronidases of various sand fly species differed in structure and sensitivity to reducing conditions. In the subgenera Phlebotomus (P. papatasi and P. duboscqi) and Adlerius (P. halepensis) the predominant active form of the enzyme was monomeric with the same apparent molecular weight under nonreducing and reducing conditions (around 65 kDa for P. papatasi and P. duboscqi and 110 kDa for P. halepensis). In P. sergenti the enzyme occurred as a putative homodimer but remained active under reducing conditions when separated into 60 kDa subunits. In L. longipalpis and P. perniciosus the activity was detectable under non-reducing conditions only. In P. duboscqi, low enzyme activity was found also in males. Salivary gland hyaluronidases of sand flies share characteristics with endo-N-acetyl-hexosaminidases of mammalian sperm cells and corresponding venom enzymes of Hymenoptera. Hypothetically, they facilitate blood meal acquisition but also may modulate immune reactions of the host and promote pathogen transmission.
Insect Biochem Mol Biol 2002 Dec
PMID:Salivary gland hyaluronidase in various species of phlebotomine sand flies (Diptera: psychodidae). 1242 21

Studies of the recent decade, including sequencing of numerous human genome regions, allowed a great progress in detection of new tumor suppressor genes (TSG) and development of new means of their identification and analysis. Effective methods of genome scanning and TSG identification combine DNA array techniques and subtraction hybridization. Alternative ways take advantage of new extrachromosomal vector systems (pETE, pETR) and the functional gene inactivation test. A breakthrough was made in localizing new TSG on the human chromosome 3 short arm, which harbors tumor-suppressing regions and is often rearranged in various tumors and in early carcinogenesis. On 3p, only three putative TSG were known five years ago, and at least ten were identified by the end of 2002. The role of new TSG in carcinogenesis is commonly inferred from a decrease in their transcription in tumor cell lines or primary tumors and from their ability to suppress the growth of these. Protein products of 3p TGS play an important part, constraining cell malignization. Some are directly involved in regulating the cell cycle and inducing apoptosis (RASSFIA), others suppress angiogenesis (Sema3B) or metastasis (Hyal-1). Numerous attempts to find mutations in exons of silent genes failed, and at least half of the new candidate genes (RASSFIA, CACNA2D2, BLU, HYAL1, SEMA3B, RAR-beta) proved to be inactivated by promoter methylation.
Mol Biol (Mosk)
PMID:[New tumor suppressor genes in hot spots of human chromosome 3: new methods of identification]. 1272 67

Sperm surface protein PH-20 expression was studied during spermatogenesis in pubertal and adult sheep, using molecular and histological methods. The effects of 24 hr of insulation raising scrotal temperatures to 39 degrees C on PH-20 expression in ejaculated sheep sperm were also determined. A 282 nt cDNA fragment of ovine PH-20 was identified in total RNA extracts of sheep testes, which exhibited 76% identity at the nucleotide level with the equivalent region of the human sequence. Ovine PH-20 mRNA and immunoreactivity were identified only in adult ram testis and not in peri-pubertal ram testis tubules lacking round spermatids, nor in adult sheep brain, pituitary, heart, spleen, lung, liver, kidney, epididymis, or ovary. Ovine PH-20 protein was distributed predominantly on the postacrosomal membrane and was also present on the anterior membrane of the sperm head in fresh, unheated sheep semen. Scrotal heating caused a significant, transient decrease in the percentage of PH-20 immunoreactive sperm, but did not change the pattern of PH-20 staining on the sperm head. The results strongly suggest that ovine PH-20 is postmeiotically expressed in haploid germ cells in sheep testis and is arrayed on the membrane of the mature ovine spermatozoon. Scrotal heating appears to have few effects on PH-20 expression and distribution on ejaculated sperm.
Mol Reprod Dev 2004 May
PMID:Effects of scrotal heating on sperm surface protein PH-20 expression in sheep. 1503 54

We have identified an 80 kDa protein in ejaculated bull spermatozoa (p80) which is found in acrosomal and post-acrosomal areas of the head. It has a hyaluronidase activity and shares homologies with PH-20, a sperm surface glycoprotein involved in sperm-egg interaction. The aim of the present study was to characterize bull sperm p80 protein at the nucleic and amino acid levels to determine whether it is the bovine PH-20 ortholog. The complete nucleotide sequence determined by RT-PCR, 3' and 5' RACE show that bull p80, displays identity with the PH-20 nucleotide and amino acid sequences. Messenger RNA and protein expressions determined by Northern blot and immunohistochemistry revealed that the protein is testicular (expressed in spermatocytes and spermatids). The localization of p80 on spermatozoa, determined by indirect immunofluorescence using a monoclonal antibody, shows the protein in acrosomal and post acrosomal areas of the head with an increase in the signal intensity as sperm progress through the epididymis. Post-translational modifications of the protein were investigated during the epididymal maturation by Western blot on protein extracts from sperm collected in the caput, corpus and cauda portions of bull epididymis. Glycolysation status of sperm p80 protein on proteins from ejaculated and epididymidal sperm was investigated. Result show that the glycosylation status is modified as spermatozoa migrate through the epididymis. Hyaluronidase activity evaluated in protein extracts from spermatozoa of the three different epididymal sections revealed that the activity is higher at pH 7 than 4 and is not affected by epididymal maturation. These data strongly suggest that p80 is the bovine PH-20.
Mol Reprod Dev 2005 Aug
PMID:Identification of the bull sperm p80 protein as a PH-20 ortholog and its modification during the epididymal transit. 1589 45


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