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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of 9 monosaccharides which constitute cell surface carbohydrates on the infection of bovine embryonic skin and muscle (BESM) cells by Trypanosoma cruzi trypomastigotes and Toxoplasma gondii tachyzoites was assayed. Most of the monosaccharides tested stimulated the infection of BESM cells by T. gondii; none of the monosaccharides were inhibitory. In contrast (at a concentration of 50 mM or greater) the monosaccharides inhibited non-specifically the infection of BESM cells by T. cruzi trypomastigotes whereas the other 8 monosaccharides were ineffective. The inhibition was due to an effect on the trypomastigotes and not on the vertebrate cells. It is proposed that there is a wheat-germ agglutinin-like lectin on the T. cruzi trypomastigote surface which recognizes and attaches to an N-acetylglucosamine-containing receptor on the vertebrate cell surface prior to infection. Infection of vertebrate cells by T. gondii tachyzoites appears to be mediated by other cell surface components. If monosaccharides are involved in infection by tachyzoites, they are ones not commonly found on animal cell surfaces. Alternatively, infection of vertebrate cells by T. cruzi and T. gondii is effected by different mechanisms.
Mol Biochem Parasitol 1982 May
PMID:Influence of monosaccharides on the infection of vertebrate cells by Trypanosoma cruzi and Toxoplasma gondii. 704 90

Establishment of Trichinella spiralis infective larvae is blocked to a large degree in the immune rat as compared with the nonimmune host. The rapidity with which this response occurs indicates that most worms are either prevented from penetrating the intestinal epithelium or are rejected immediately after cell entry. It is proposed that interference with larval infectivity is due to alterations in the epithelial cell apical or brush border membrane. Alterations may result from prior infection or may reflect an acute change induced by challenge infection. In either case the establishment of normal populations of larvae in the mucosa is disturbed. Lectin binding capacity of brush border membranes was used to assess possible membrane alterations. This parameter in uninfected (control) rats was compared with that in infected rats, which acquire resistance to subsequent challenge, and in infected rats immediately after a challenge inoculum. Enriched brush border membrane preparations were characterized for their binding of wheat germ agglutinin, which attaches specifically to the carbohydrate, N-acetylglucosamine. Maximum specific binding of 125I-labeled wheat germ agglutinin occurred within 20 min. The spontaneous rate of dissociation was negligible for 90 min. Highest specific binding resulted at 24 degrees C, pH 6.0 and with 75 micrograms brush border membrane protein per assay tube. Results suggested the existence of multiple binding sites. 1 mg of membrane protein from uninfected rats and rats immunized by primary infection maximally bound 9.8 X 10(10) and 4.3 X 10(10) molecules of wheat germ agglutinin, respectively. Binding for the 'immune' brush border membrane, as compared with the 'uninfected' brush border membrane was reduced during the first 3 weeks of infection and remained low for at least 3 months. No further reduction in binding was observed for brush border membrane isolated within minutes after a secondary infection. These results reveal the induction by a primary infection of changes in brush border membrane structure and the persistence of these changes in the immune host. In view of the rapid turnover time of epithelial tissue the mechanism by which this change is perpetuated speculatively involves immune elements in the lamina propria.
Mol Biochem Parasitol 1982 Sep
PMID:Intestinal epithelial membrane changes in rats immune to Trichinella spiralis. 713 53

The major polypeptides composing hepatitis B surface antigen (HBsAg) particles are P-I and P-II. P-II shares the same amino acid sequence as P-I and contains an additional carbohydrate moiety of mol. wt approximately 5000. When a purified preparation of P-II was digested with Nagarse and then with Pronase P, it gave rise to a glycopeptide containing 15 amino acid residues and the carbohydrate moiety of P-II. The N-terminal amino acid sequence of the glycopeptide was determined to be Lys-Pro-Thr-Asp-Gly-Asn-. The polysaccharide moiety contained 5 moles of N-acetylglucosamine and was connected with Asn at the sixth position from the N-terminus. When mice were immunized against this HBsAg glycopeptide, they raised humoral antibodies which bound to each of three preparations of P-I derived from HGsAg particles of subtypes adw, adr and ayw, thereby indicating that the sequence of 15 amino acids in the glycopeptide would constitute a common antigenic structure of HBsAg.
Mol Immunol 1982 Sep
PMID:A glycopeptide containing 15 amino acid residues derived from hepatitis B surface antigen particles: demonstration of immunogenicity to raise anti-HBs in mice. 714 54

Microsome enriched Ceratitis capitata extracts synthesized a glucosylated lipid linked oligosaccharide. Its properties were closely related to those of the previously described insect mannosylated dolichyl diphosphate oligosaccharides and almost the same as those of the rat liver dolichyl-diphosphate-(GlcNAc)2-(Man)9-(Glc)1-3. The saccharide moiety of the latter was transferred to an unknown endogenous protein-like acceptor by the fly extracts. These represent the first evidence of a protein glycosylation in a pluricellular invertebrate through dolichyl derivatives.
Mol Cell Biochem 1980 Dec 16
PMID:The biosynthesis of glucose containing insect lipid linked oligosaccharide and its possible role in glycoprotein assembly. 746 28

Rabbit tears were found to contain two lysozymes which differed in their electrophoretic mobility and were designated tear lysozymes 1 and 2. Rabbit tear lysozyme 1 was purified to homogeneity by conventional purification methods. It was found to be distinct from other known mammalian c-type lysozymes, rabbit tear lysozyme 2 and the major rabbit gastrointestinal lysozyme. The activity profile is centered around the neutral region with an optimum of 7 which is slightly lower than that for chicken lysozyme. The thermal stability as well as inhibition profiles by the substrate analogues, N-acetylglucosamine (NAG) and chitotetraose (NAG)4 are comparable to those of chicken lysozyme. Based on its molecular weight and catalytic properties this isozyme is classified as a c-type lysozyme.
Comp Biochem Physiol B Biochem Mol Biol 1995 Sep
PMID:Electrophoretic polymorphism in rabbit tear lysozyme. 758 45

To define carbohydrate specificity of Ricinus communis agglutinin (RCA1), the combining site of RCA1 was further characterized by quantitative precipitin (QPA) and precipitin-inhibition assays (QPIA). Among the oligosaccharides tested for QPIA, Gal beta 1-->4GlcNAc (II, human blood group type II precursor sequence) was found to be 7.1 times more active than Gal beta 1-->3GalNAc (T, Thomsen-Friedenreich sequence) and about 1.7 times more active than the other three disaccharides tested--Gal beta 1-->4Man, Gal beta 1-->3DAra and Gal beta 1-->6GalNAc. Gal alpha 1-->4Gal, the receptor of the uropathogenic E. coli ligand was 3.6 times less active than the II sequence. These results indicate that the beta 1-->4 linkage of the terminal Gal to subterminal GlcNAc is important as this beta 1-->4GlcNAc sequence is at least 1.6 times more active than other types of disaccharides. Among the glycoproteins examined for QPA, native and desialized bovine submandibular glycoproteins, native and desialized human plasma alpha 1-acid glycoproteins, as well as crude hog stomach mucin and its three mild acid hydrolyzed products reacted well with the lectin. These glycoproteins precipitated over 75% of the lectin nitrogen added indicating that RCA1 has the ability to recognize Gal beta 1-->4/3GlcNAc and/or the related residues at the non-reducing ends and at positions in the interior of the chains. However, Tn (GalNAc alpha 1-->Ser/Thr sequence) rich glycoproteins such as desialized ovine submandibular glycoprotein and desialized armadillo salivary glycoprotein, in which over 90% of the carbohydrate side chains are Tn determinants with none or only a trace of I/II or T determinants, precipitated poorly with RCA1. From the present and previous results obtained, the carbohydrate specificity of RCA1 can be constructed and summarized in decreasing order by lectin determinants as follows: II (Gal beta 1-->4GlcNAc) > I (Gal beta 1-->3GlcNAc) > E (Gal alpha 1-->4Gal) and B (Gal alpha 1-->3Gal) > T (Gal beta 1-->3GalNAc), while Tn (GalNAc alpha 1-->Ser/Thr) is a poor inhibitor.
Mol Immunol 1993 Mar
PMID:Defining carbohydrate specificity of Ricinus communis agglutinin as Gal beta 1-->4GlcNAc (II) > Gal beta 1-->3GlcNAc (I) > Gal alpha 1-->3Gal (B) > Gal beta 1-->3GalNAc (T). 768 Nov 48

A plasmid that included both an 8.9 kb chromosomal DNA insert containing genes from the rfb cluster of Shigella dysenteriae 1 and a smaller insert containing the rfp gene from a S. dysenteriae 1 multicopy plasmid resulted in efficient expression of O antigen in an rfb-deleted strain of Escherichia coli K-12. Eight genes were identified in the rfb fragment: the rfbB-CAD cluster which encodes dTDP-rhamnose synthesis, rfbX which encodes a hydrophobic protein involved in assembly of the O antigen, rfc which encodes the O antigen polymerase, and two sugar transferase genes. The production of an O antigen also required the E. coli K-12 rfe gene, which is known to encode a transferase which adds N-acetylglucosamine phosphate to the carrier lipid undecaprenol phosphate. Thus Rfe protein appears to function as an analogue of the Salmonella RfbP protein to provide the first sugar of the O unit. Functional analysis of the other genes was facilitated by the fact that partial O units of one, two or three sugars were efficiently transferred to the lipopolysaccharide core. This analysis indicated that the plasmid-encoded Rfp protein is the transferase that adds the second sugar of the O unit while the two rfb transferases add the distal sugars to make an O antigen whose structure is (Rha-Rha-Gal-GlcNAc)n. The use of the rfe gene product as the transferase that adds the first sugar of an O unit is a novel mechanism which may be used for the synthesis of other enteric O antigens.
Mol Microbiol 1993 Jul
PMID:Function of the rfb gene cluster and the rfe gene in the synthesis of O antigen by Shigella dysenteriae 1. 769 19

Trp62 in the binding subsite B of hen egg-white lysozyme shows general features often observed in protein-carbohydrate interactions including a stacking interaction and a hydrogen bonding network with water molecules. A previous report by our group showed that the perturbation of these interactions by substitution of Trp62 with tyrosine or phenylalanine affects the substrate binding modes and also enhances the hydrolytic activity. In order to elucidate the relationship between structural and functional changes of these protein-carbohydrate interactions, the Trp62Tyr and Trp62Phe mutants complexed with the substrate analogue, (GlcNAc)3, were analyzed at 1.8 A resolution by X-ray crystallography. The overall structures of the mutant enzymes are indistinguishable from that of the wild type enzyme. Although the wild-type enzyme binds (GlcNAc)3 in only one binding mode (A-B-C), the Trp62Tyr mutant binds (GlcNAc)3 in two binding modes (A-B-C, B-C-D) and the Trp62Phe mutant has an even weaker binding mode. The aromatic rings of Tyr62 and Phe62 maintain their interactions with the carbohydrate molecules, but make fewer stacking interactions with the GlcNAc in the B site than the wild-type enzyme does. The hydroxyl group of Tyr62 interacts weakly with a water molecule which mediates hydrogen bonding in the GlcNAc residues in the B and C sites. The C-6 hydroxyl group of the GlcNAc residue in the C site rotates around the C-5-C-6 bond to complete the hydrogen bond network in the Trp62Tyr mutant-(GlcNAc)3 complex. On the other hand, this hydrogen bonding network does not form in the Trp62Phe mutant-(GlcNAc)3. In addition to these structural studies, the kinetic parameters of the hydrolysis of 4-methylumbelliferyl N-acetyl-chitotriose, ((GlcNAc)3-MeU), have been determined in order to further characterize the enzymatic properties of these mutant lysozymes. This demonstrates that the modulation of the hydrogen bonding network, including the flexible part of the carbohydrate and water molecules and/or the slight reduction of stacking interaction in the B site, alters the binding mode toward the carbohydrate and induces an enhancement of the hydrolytic activity.
J Mol Biol 1995 Mar 24
PMID:Dissection of protein-carbohydrate interactions in mutant hen egg-white lysozyme complexes and their hydrolytic activity. 770 75

The activities of Gal beta 1-3(4)GlcNAc alpha 2-3 sialyltransferase and SAT-1 were measured in rat liver Golgi in inflammation; both enzymes decreased by about 50%. This compares with increases of about 3-fold for the Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase. All three sialyltransferases were released from disrupted Golgi membranes by incubation at reduced pH which activates an endogenous cathepsin D which is believed to be the lysosomal enzyme. Pepstatin A was found to block the release of all three sialyltransferases providing support for the role of cathepsin D as the proteinase that clips the catalytic portions of the enzymes from their membrane anchor and stem regions.
Comp Biochem Physiol B Biochem Mol Biol 1995 Feb
PMID:Release of sialyltransferases from rat liver Golgi membranes by a cathepsin D-like proteinase: comparison of the release of Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase, Gal beta 1-3(4)GlcNAc alpha 2-3 sialyltransferase and lactosylceramide alpha 2-3 sialyltransferase (SAT-1). 771 47

Class II chitinases (EC 3.2.1.14) are plant defense proteins. They hydrolyze chitin, an insoluble beta-1,4-linked polymer of N-acetylglucosamine (NAG), which is a major cell-wall component of many fungal hyphae. We previously reported the three-dimensional structure of the 26 kDa class II endochitinase from barley seeds at 2.8 A resolution, determined using multiple isomorphous replacement (MIR) methods. Here, we report the crystallographic refinement of this chitinase structure against data to 1.8 A resolution using rounds of hand rebuilding coupled with molecular dynamics (X-PLOR). The final model has an R-value of 18.1% for the 5.0 to 1.8 A data shell and 19.8% for the 10.0 to 1.8 A shell, and root-mean-square deviations from standard bond lengths and angles of 0.017 A and 2.88 degrees, respectively. The 243 residue molecule has one beta-sheet, ten alpha-helices and three disulfide bonds; 129 water molecules are included in the final model. We show structural comparisons confirming that chitinase secondary structure resembles lysozyme at the active site region. Based on substrate binding to lysozyme, we have built a hypothetical model for the binding of a hexasaccharide into the pronounced active site cleft of chitinase. This provides the first view of likely substrate interactions from this family of enzymes; the model is consistent with a lysozyme-like mechanism of action in which Glu67 acts as proton donor and Glu89 is likely to stabilize the transition state oxycarbonium ion. These binding site residues, and many hydrophobic residues are conserved in a range of plant chitinases. This endochitinase structure will serve as a model for other plant chitinases, and that catalytic models based on this structure will be applicable to the entire enzyme family.
J Mol Biol 1995 Apr 28
PMID:The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8 A resolution. 773 49


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