Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q07644 (polypeptide)
 72,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A pituitary polypeptide, acceleratory polypeptide-growth hormone (ACG), has been found to increase the sensitivity of fasting normal people to intravenous insulin. It is suggested that diminished activity of this polypeptide-or increased activity of another polypeptide, inhibitory polypeptide-growth hormone (ING)-may have a role in the genesis of diabetes mellitus.
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PMID:Potentiation of insulin action in normal subjects by a pituitary polypeptide. 581 55

Infection of BHK 21 cells by vesicular stomatitis virus (VSV) results in the intracellular synthesis of the five viral proteins which are easily detectable in polyacrylamide gels after short labeling periods with [35S]methionine. In addition, a 6th prominent radioactive protein band appears intracellularly in VSV-infected BHK cells. This additional polypeptide is also coded by the viral genome, because it is immunoprecipitated by antibodies against viral particles and more specifically by antibodies against purified G-protein. We propose to call this derivative of the G-protein Gsi-protein (short intracellular G-protein). It is associated with intracellular membranes and has an apparent mol. wt. of 58 000. Both G- and Gsi-protein have the same kinetics of appearance in the cell. The ratio of G-:Gsi-protein in BHK 21 cells is approximately 85:15. The mol. wt. difference of approximately 6000 daltons between G- and Gsi-protein is not due to variations in the degree of glycosylation because trypsin digestions of both [3H]mannose-labeled glycoproteins gave rise to identical glycopeptide patterns. Incubation of microsomes with trypsin demonstrates that Gsi-protein is protected in its full length by intracellular membranes. Gsi-protein is lacking an extended carboxy-terminal region of the viral G-protein sequence because it is not modified by palmitic acid and is not immunprecipitated by specific antibodies against a C-terminal peptide of the G-protein. Limited proteolysis by endoproteinase arg C indicates that the structure of Gsi-protein is very similar to the shedded form of the G-protein which has been previously described in the literature.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Intracellular appearance of a glycoprotein in VSV-infected BHK cells lacking the membrane-anchoring oligopeptide of the viral G-protein. 608 25

A bovine anterior pituitary polypeptide that stimulates the replication of rat and human adipocyte precursors has been purified. Its Mr is 44 000-53 000 and its isoelectric point is 9.8-10.3. While pituitary basic fibroblast growth factor is equally mitogenic on adipocyte precursors and skin fibroblasts, the polypeptide described here is selectively more active on the precursors. We postulate that this adipocyte growth factor plays a physiological role by modulating the number of adipocyte precursors.
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PMID:Purification of a pituitary polypeptide that stimulates the replication of adipocyte precursors in culture. 661 70

A cDNA plasmid bank has been constructed using mRNA from developing pea seeds and three cDNAs coding for vicilin polypeptides have been selected. These cDNAs have been sequenced and between them cover the whole of the coding sequence plus part of the 5' and 3' untranslated regions. Comparison with amino acid sequence data from the protein indicates that vicilin is synthesised as preprovicilin with subsequent removal of a signal peptide and a C-terminal peptide as well as post translational endo-proteolytic cleavage. The cDNAs represent two different classes of vicilin genes whilst amino acid data show that there are at least three major classes of vicilin polypeptide. The vicilin sequences show extensive homology with conglycinin and phaseolin except in the regions of the internal proteolytic cleavages. The evolutionary significance of this relationship is discussed.
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PMID:The vicilin gene family of pea (Pisum sativum L.): a complete cDNA coding sequence for preprovicilin. 668 41

The expression of the 7B2 protein, secreted from a variety of neural and endocrine tissues, increases dramatically in specific neuroendocrine tumors. We have recently shown that human 7B2 can act as a molecular chaperone in the deaggregation of proteins in vitro. In order to identify polypeptides which might bind 7B2 in vivo, the yeast two-hybrid system was employed. Surprisingly, mere covalent linkage of 7B2 to the DNA-binding domains of two yeast transcription activators, Ace1 and Gal4, activates transcription from the ACE1 and GAL4 operon. 7B2's ability to activate nuclear transcription surpasses that of Ace1 and compares favourably with the strong activation domain of the tumor suppressor protein, p53. Our results suggest that 7B2 must possess an activating sequence, a domain which defines all transcriptional activator proteins. Like the acidic activation domains of some transcriptional activators, 7B2 also binds the yeast TATA-box binding protein, an essential polypeptide in the basic transcription machinery. Deletion analysis of the gene encoding 7B2 reveals two independent transcriptional activating sequences in the 185 amino acid protein. It is therefore conceivable that 7B2 not only has a functional role in the secretory pathway but also in the nucleus. Moreover, these findings raise an intriguing question regarding the activation domains of 7B2 and their possible link to 7B2's oncogenic potential.
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PMID:The neuroendocrine protein 7B2 contains unusually potent transcriptional activating sequences. 748 73

Escherichia coli isoleucyl-tRNA synthetase has been shown to contain two enzyme-bound zinc atoms per polypeptide chain. To investigate the structural and functional significance of the C-terminal enzyme-bound zinc, mutagenesis was used to alter Cys 922 to Ser [IleRS(C922S)] and to replace Cys 922 through Ala 939 with a 33 amino acid peptide unable to bind zinc (AIleRS). Both IleRS(C922S) and AIleRS were found to contain only a single enzyme-bound zinc per polypeptide chain. Substitution of Co2+ for Zn2+ in IleRS(C922S) gave a visible spectrum characteristic of that expected for a single tetrahedrally coordinated enzyme-bound Co2+ atom. Little or no effect on the Km values for ATP or Ile and only a 5 fold reduction of the (kcat/Km)Ile was observed for IleRS(C922S) and AIleRS in the isoleucine-dependent ATP-pyrophosphate exchange reaction. In the tRNA-dependent aminoacylation reaction, Km values for tRNA(Ile) were only slightly affected in the mutant proteins. However, kcat/Km values were decreased approximately 200 and 2500 fold for IleRS(C922S) and AIleRS, respectively. These results suggest that both the C-terminal enzyme-bound zinc and the C-terminal peptide play important roles in aminoacylation of tRNA(Ile).
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PMID:Mutation of the carboxy terminal zinc finger of E. coli isoleucyl-tRNA synthetase alters zinc binding and aminoacylation activity. 748 60

The secretory polypeptide 7B2 is produced in different endocrine and neuroendocrine cells, where it is presumed to play a role in the hormone secretion mechanism. In this study, we examined a pattern of 7B2 mRNA expression in the mouse and rat pituitary gland. When [35S]-labeled antisense cRNA probes were used for in situ hybridization, 7B2 mRNA transcripts were detected within virtually all endocrine cells of the anterior lobe (gonadotrophs, thyrotrophs, corticotrophs, somatotrophs and lactotrophs) and of the intermediate lobe (melanotrophs). The posterior lobe was negative. By immunocytochemistry, 7B2 accumulation was observed within melanotrophs in the intermediate lobe and within gonadotrophs and thyrotrophs in the anterior lobe. The question of 7B2 production in other pituitary cells, such as corticotrophs, somatotrophs and lactotrophs, was studied under culture conditions. The corticotroph AtT-20 and somatrotroph GH3 cell lines both expressed 7B2 mRNA and contained 7B2 protein detectable by radioimmunoassay. However, this protein could not be visualized by immunocytochemistry. Thus, it is possible that 7B2 is produced in all hormone-synthesizing cells of the pituitary gland, being stored only within some of them and rapidly exported after synthesis from others.
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PMID:Expression of neuroendocrine secretory protein 7B2 mRNA in the mouse and rat pituitary gland. 750 8

Two cDNA clones encoding the GRA2 (G.P.28.5) secreted antigen of Toxoplasma gondii were expressed in Escherichia coli as glutathione-S-transferase fusion polypeptides. A high level of expression was obtained for the first clone expressing the 59C-terminal amino acids of GRA2. The other one was an open-reading-frame of 212 amino acids containing the entire GRA2 cDNA. By ELISA, IgG antibodies directed against the 59aa recombinant polypeptide were detected in 33/44 (75%) sera from patients chronically infected with T. gondii and in 19/23 (82.6%) sera derived from patients with acute, primary toxoplasmosis. 10 of the 11 "chronic" sera which were negative by the 59aa ELISA were tested in a immunoblot against the 212aa open-reading-frame of GRA2: 8/10 were positive. A peptide representing the 15 C-terminal amino acids of GRA2 has been shown to contain the epitope recognized by a mouse monoclonal antibody (TG17-179). The reactivity of human sera with the 59aa recombinant polypeptide was inhibited to varying degrees when the sera were co-incubated with this peptide. Twelve chronic sera showed a range of inhibition from 8 to 100% and twelve acute sera an inhibition range of 15 to 90%. This suggests that the 15aa C-terminal peptide contains an epitope recognized in both the acute and chronic phases of infection and that other major epitope(s) exist in the 59aa C-terminal region of GRA2. As a conclusion, the recombinant GRA2 protein appears to contain at least three B-cell epitopes.
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PMID:Multiple B-cell epitopes in a recombinant GRA2 secreted antigen of Toxoplasma gondii. 750 69

Endothelial-monocyte-activating polypeptide II (EMAP II) is a novel mediator isolated from conditioned medium of methylcholanthrene A-induced tumor cells which modulates properties of endothelial cells, mononuclear phagocytes (MPs), and polymorphonuclear leukocytes (PMNs) in vitro and induces an acute inflammatory response in vivo. A synthetic peptide comprising 15 residues from the N-terminal region (residues 6-20) was shown to induce directional migration of MPs and PMNs, with half-maximal effect at approximately 200-250 pM, whereas a peptide from the C terminus of EMAP II, as well as other irrelevant peptides, were without effect. Modulation of cellular phenotype by EMAP II-derived peptide was suggested by peptide-induced elevation of cytosolic free calcium concentration in fura-2-loaded MPs and PMNs and by stimulation of peroxidase release in PMNs. Consistent with these in vitro data, EMAP II-derived N-terminal peptide-albumin conjugates injected into the mouse footpad elicited inflammatory cell tissue infiltration, whereas albumin alone or EMAP II-derived C-terminal peptide conjugated to albumin incited little response. Binding of 125I-labeled EMAP II-derived peptide (residues 12-20) to MPs was saturable (Kd approximately 200 pM) and was blocked in a dose-dependent manner by the addition of intact EMAP II and unlabeled EMAP II-derived peptides (residues 6-20 and 12-20), whereas interleukin 1, tumor necrosis factor, formyl-methionyl-leucinyl-phenylalanine, or irrelevant peptides were without effect. Cross-linking of 125I-EMAP II-derived peptide (residues 12-20) by disuccinimidyl suberate to human MPs demonstrated a band, approximately 73 kDa, on reduced sodium dodecyl sulfate-polyacrylamide gel electrophoresis. 125I-EMAP II-derived peptide also demonstrated specific binding to human PMNs and murine RAW cells. These data indicate that the N-terminal region of EMAP II defines a biologically active locus of the molecule which interacts with target cells via a potentially novel cellular receptor.
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PMID:A peptide derived from the amino terminus of endothelial-monocyte-activating polypeptide II modulates mononuclear and polymorphonuclear leukocyte functions, defines an apparently novel cellular interaction site, and induces an acute inflammatory response. 754 17

A peptide consisting of the 17 N-terminal amino acids of native bovine rhodanese in combination with the chaperone DnaJ specifically inhibits release factor- and stop codon-dependent hydrolysis of N-formylmethionine from N(formyl)-methionyl-tRNA bound with AUG to salt-washed ribosomes. Neither the peptide nor DnaJ by itself causes this inhibition. The N-terminal peptide and DnaJ both singularly and combined do not affect the peptidyltransferase reaction per se. The total amount of rhodanese synthesized in the cell-free coupled transcription-translation system is reduced by the peptide, with concomitant accumulation of full-length enzymatically inactive rhodanese polypeptides on ribosomes. In combination with DnaJ, the N-terminal polypeptide inhibits the termination and release of full-length rhodanese peptides that have accumulated on Escherichia coli ribosomes during the course of uninhibited coupled transcription-translation in the cell-free system. This inhibition appears to involve release factor 2-mediated termination at the UGA termination codon in the coding sequence for rhodanese. It is suggested that the N-terminal peptide inhibits the binding of the release factor to ribosomes. These data appear to provide the first report of differential inhibition of the termination reaction on ribosomes without inhibition of the peptidyltransferase reaction and peptide elongation.
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PMID:Inhibition of the release factor-dependent termination reaction on ribosomes by DnaJ and the N-terminal peptide of rhodanese. 755 37


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