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)

In DNA preparations isolated from regenerating rat liver 22 hours after partial hepatectomy, i.e. at the period of the most intensive DNA synthesis a "Denaturating Protein Factor" (DPF) tightly bound to DNA was found. Isolated protein fraction with a molecular weight of 6500 dalton was found to be homogenous upon SDS-polyacrylamide electrophoresis. The degree of destabilisation of DNA was estimated by its reaction with water-soluble [14C]CME-carbodiimide which modifies selectively guanine and thymine residues only in the denatured DNA regions. Pronase treated DPF loses its DNA-denaturing capacity. Pronase treatment of DNA--DPF complex restores native DNA structure. DPF from rat liver was able to denature DNA from calf thymus and bacteriophage T7 DNA. A hypothesis is proposed that the DPF is responsible for the destabilization of DNA secondary structure in the process of replication.
Mol Biol (Mosk)
PMID:[Protein factor from regenerating rat liver destabilizing secondary DNA structure]. 75 92

The expression and ligand binding activity of Fc receptors for IgG (Fc gamma R) on guinea-pig peripheral blood polymorphonuclear leukocytes (blood PMN) have been compared with those on casein-elicited peritoneal PMN (exudate PMN). Both the PMN were found to express two distinct types of Fc gamma R, one specific for IgG1 and IgG2 (Fc gamma 1/gamma 2 R) and the other for IgG2 alone (Fc gamma 2 R), when evaluated by their reactivity to monoclonal antibodies (mAb) directed against each type of Fc gamma R. The surface density of Fc gamma 1/gamma 2 R was not significantly different between the two cell types, whereas exudate PMN expressed five times as many Fc gamma 2 R as blood PMN. Moreover, IgG immune complex (IC) binding activities of both the Fc gamma R on blood PMN were markedly low as compared with those on exudate PMN. In addition, blood PMN could not significantly generate superoxide anion (O2-) when exposed to IC. However, these lower activities were improved by protease treatment of the cells or by incubation with platelet activating factor (PAF). Fc gamma 2 R on blood PMN was found to be sensitive to pronase, whereas Fc gamma 1/gamma 2 R was resistant. Pronase-treated blood PMN showed a marked IC binding activity, though they lacked Fc gamma 2 R. This activity was completely blocked by anti-Fc gamma 1/gamma 2 R mAb, indicating that the proteolysis augments the ligand binding capacity of Fc gamma 1/gamma 2 R. In contrast, PAF was found to specifically modulate Fc gamma 2 R. The Fc gamma 2 R expression was significantly increased within 5 min incubation with PAF, whereas that of Fc gamma 1/gamma 2 R was not affected. The cells also exhibited enhanced IgG2-IC binding and subsequent O2- generating activities. These results indicate that both the Fc gamma R on blood PMN are functionally immature and are converted to exhibit intrinsic activities by proteases and PAF; such changes may occur in vivo during exudation and at inflammatory sites.
Mol Immunol 1992 May
PMID:Low ligand binding activities of two distinct types of Fc gamma receptor on guinea-pig peripheral blood polymorphonuclear leukocytes are differentially improved by proteolysis or platelet activating factor. 131 50

ZP3, a glycoprotein of the murine zona pellucida, functions both to bind acrosome intact sperm and to induce the acrosome reaction. Solubilized whole zonae as well as purified ZP3 are able to induce acrosome reactions in capacitated sperm. Pronase digests of whole zonae yield glycopeptides that bind to sperm but are unable to induce acrosome reactions. However, immunoaggregation of these glycopeptides results in the exocytosis of the acrosome in the majority of treated sperm. The data suggest that ZP3 triggers the acrosome reaction by the aggregation of ZP3 binding sites on the sperm head. If aggregation of ZP3 binding sites is important in the induction of the acrosome reaction, then it may be possible to induce the acrosome reaction in the absence of zona by immunoaggregation of the sites. This presentation deals with the immunoaggregation of a proteinase inhibitor of seminal vesicle origin (SVI) that binds to a site on the sperm head known to participate in zona binding. We show that capacitated murine sperm, pretreated with the SVI, will acrosome react, as determined by Coomassie brilliant blue staining, when incubated with rabbit antiinhibitor antiserum (anti-SVI). The percentage of SVI-treated sperm displaying an acrosome reaction is dependent on the concentration of the immune serum. Sperm stain positive for intact acrosomes when anti-SVI Fab fragments or normal rabbit serum is substituted for the immune serum. However, when capacitated sperm, treated with both SVI and anti-SVI Fab fragments, are incubated with goat antirabbit IgG, the majority of sperm acrosome react. The data suggest that the aggregation of SVI bound to the sperm surface, in the absence of zona glycoproteins, is sufficient to induce the acrosome reaction.
Mol Reprod Dev 1991 Nov
PMID:Acrosome reaction induced by immunoaggregation of a proteinase inhibitor bound to the murine sperm head. 172 79

The N-glycan-processing inhibitors swainsonine (Sw) and deoxymannojirimycin (dMM) were used to study the influence of N-glycans on iodide organification in cultured porcine thyroid cells. Incubations with [125I]NaI were followed by determination of labeled trichloroacetic acid-insoluble material in culture media, follicular contents and cells. In controls, most of this material was in the follicular contents. With Sw and dMM, total acid-insoluble material was less than 10% of control. Iodide uptake was slightly inhibited and hydrogen peroxide release was not affected by inhibitors. Cell-surface thyroid peroxidase (TPO) activity, assayed by its ability to iodinate bovine serum albumin, was strongly inhibited. Pronase glycopeptide analysis indicated that with drugs the content in complex-type N-glycans was strongly decreased while that in hybrid or oligomannosidic type was increased. In conclusion, inhibition of N-glycan processing prevents iodide organification in cultured porcine thyroid cells by decreasing the recovery of cell-surface TPO activity.
Mol Cell Endocrinol 1990 Oct 22
PMID:Inhibition of N-glycan processing affects iodide organification in porcine thyroid cells. 214 33

gamma-Hydroxybutyric acid (GHB) is a natural compound of mammalian brain synthesized from GABA. The characteristics of its synthesis, transport, release, distribution and turnover, in addition to the presence of a high affinity binding site for this substance in brain are in favor of a modulator role for GHB. The effects of hydrolytic enzymes on the specific binding capacity of GHB have been studied in the present work. Phospholipases A2 and C, neuraminidase and Pronase markedly decrease GHB binding to crude synaptosomal membranes from rat brain. This effect is time and enzyme concentration dependent. Trypsin, under the conditions employed, is less active. The inhibitory effects of phospholipases is correlated with phospholipid hydrolysis. Lysophospholipids, in the absence of bovine fatty acid free serum albumin partially inhibit GHB binding. The action of neuraminidase has been followed by sialic acid release and modifications of the ganglioside profile. The effects of phospholipase C and of neuraminidase are completely different to those on GABA binding sites. These results represent further data concerning the molecular existence of specific GHB binding sites on rat brain membranes.
Mol Cell Biochem 1990 Mar 05
PMID:Effects of phospholipases, proteases and neuraminidase on gamma-hydroxybutyrate binding sites. 218 47

Hoechst 33258 fluorescence of single stranded DNA has been used to perform alkaline elution with unlabeled DNA. The high background fluorescence of "standard" elution solutions has prompted others to use EDTA but the elution characteristics of DNA in EDTA-containing solutions and the comparability of results with those using "standard" tetrapropyl ammonium hydroxide solutions have not previously been examined. We report here the elution characteristics of DNA in EDTA and the relevant parameters for the successful use of EDTA as an elution solution. An increase in elution pH to 12.4 is required but elution solutions of higher pH cause alkaline hydrolysis of undamaged DNA. Drug-treated DNA from which DNA-protein crosslinks have been removed can be completely removed from the filters at the end of the elution by a Pronase filter digestion. The simplest and most efficient removal of DNA-protein crosslinks is through the inclusion of proteinase-K in an SDS containing lysis solution. EDTA elution can measure interstrand crosslinks and single strand breaks as easily as is performed using radiolabeled DNA under "standard" elution conditions and requires only 1.5-2 x 10(6) cells per elution filter. DNA-protein crosslinking measurements were unsatisfactory, however, since even the Pronase digestion failed to completely remove protein-crosslinked DNA from the elution filters.
Environ Mol Mutagen 1988
PMID:EDTA alkaline elution characteristics and measurement of DNA damage in unlabeled DNA using Hoechst 33258 fluorescence. 245 57

The properties of the antigen recognized by monoclonal antibody FH6 have been analyzed. FH6 was originally generated against a glycolipid, i.e. a difucoganglioside isolated from human colonic adenocarcinoma, and specifically reacts with sialyl Lex-i determinant. Several culture supernatants of human carcinoma cell line cells were found to have high levels of FH6-reactive antigen, and PC-9, a human lung carcinoma cell line was used for the analysis. A solid-phase sandwich radioimmunoassay was performed to detect the antigen. The antigenic activity was extractable in 0.6 M PCA or 7% TCA, and was sensitive to mild alkaline treatment and to Pronase digestion. Most of the antigen was eluted in the void volume of a Sepharose CL-2B column, which indicates that its molecular weight is greater than several million. It was eluted from a DEAE-cellulose column at a NaCl concentration in the range of 0.2-0.25 M. The immunoaffinity-purified antigen has a high carbohydrate content of more than 80%. These data indicate that the antigen recognized by FH6 in the culture supernatant of PC-9 is not a glycolipid, but a high molecular weight glycoprotein which could be referred to as a mucin, or a proteoglycan, which contains keratan-sulfate like glycosaminoglycan chains, as judged from the results of the glycosidase treatments.
J Mol Recognit 1988 Jun
PMID:Glycolipid-directed FH6 monoclonal antibody recognizes high molecular weight glycoprotein antigen carrying sialyl Lex-i determinant in the culture supernatant of PC-9 cells. 290 4

Previous work has shown that when a large number of Plasmodium falciparum isolates are examined by two dimensional electrophoresis, over 100 different proteins can be detected, 15 of which show polymorphism in electrophoretic characters. Eight of these proteins have now been subjected to limited proteolysis. Two methods of digestion were used: enzymic, with Streptomyces griseus Pronase E and chemical, using N-chlorosuccinimide to break proteins at tryptophan residues. When different forms of each variable protein were analysed most were found to exhibit similar peptide profiles, a finding indicating that they were determined by alleles of genes at single loci. Two of the proteins, A and K, exhibited higher degrees of polymorphism than the other variable proteins. The possible reasons for this are discussed.
Mol Biochem Parasitol 1987 May
PMID:Peptide digest studies of polymorphic proteins of Plasmodium falciparum. 330 1

This report describes the structures of the high-mannose-type N-linked oligosaccharides in glycoproteins synthesized by Schistosoma mansoni adult male worms. Adult male schistosomes were incubated in vitro in media containing either [2-3H]mannose, [6-3H]glucosamine or [6-3H]galactose to allow metabolic radiolabeling of the oligosaccharide moieties of newly synthesized glycoproteins. Glycopeptides were prepared from the radiolabeled glycoproteins by digestion with Pronase and fractionation by chromatography on concanavalin A-Sepharose. Eleven percent of [3H]mannose incorporated into the schistosome glycopeptides was recovered in high mannose-type Asn-linked oligosaccharides which bound to the immobilized lectin. Upon treatment of [3H]mannose-labeled glycopeptide with endo-beta-N-acetylglucosaminidase H, the high mannose-type chains were released and their structures were determined by high performance liquid chromatography, methylation analysis, acetolysis and exoglycosidase digestion. The major species of high mannose-type chains synthesized by S. mansoni adult males have the composition Man7GlcNAc2, Man8GlcNac2 and Man9GlcNA2. Structural analyses indicate that these oligosaccharides are similar to high mannose-type chains synthesized by mammalian cells.
Mol Biochem Parasitol 1988 Apr
PMID:Characterization of the high mannose asparagine-linked oligosaccharides synthesized by Schistosoma mansoni adult male worms. 338 83

Demembranized sperm and somatic nuclei of mammalian origin were extracted with high salt/urea/2-mercaptoethanol, treated with detergents and purified in CsCl density gradients to isolate DNA. Under these conditions a protein component still remained bound to DNA. This stable DNA-protein complex could be reduced to an oligodeoxynucleotide-peptide complex by extensive sequential digestions with DNase I and Pronase E. Chemical and enzymatic treatments of this complex indicated the presence of a phosphoester bond between DNA and a hydroxyamino acid. Two-dimensional tryptic peptide mapping revealed a remarkable similarity among the covalently linked protein components in all types of chromatin studied. These maps differed from the maps of mammalian topoisomerases I and II.
J Mol Biol 1987 Jul 20
PMID:Stable DNA-protein complexes in eukaryotic chromatin. 365 55


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