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

A 59-year-old man had explosive watery diarrhoea, tendency towards collapse, flushes and aphonia. Pre-operative serum concentrations of vasoactive intestinal polypeptide (VIP) were up to 1030 ng/l, those of gastric inhibitory polypeptide (GIP) up to 2675 ng/l, as measured by radioimmunoassay. Cross-reaction by antisera used in the radioimmunoassay were excluded. Pancreatic tumour was diagnosed by ultrasound and by elective coeliac arteriography. After excision the abnormal fidings disappeared as did the symptoms. Biological half-life of plasma-VIP (determined during removal of the tumour from plasma samples by radioimmunoassay) was about 45 minutes. The tumour produced both VIP and GIP.
 ...
PMID:[VIP and GIP-producing pancreatic tumour: relationship to the Verner-Morrison syndrome]. 17 72

Biochemical analysis indicates that lithium ion (Li+) has deleterious effects on the metabolism of at least two elements of the cytoskeleton in cultured chick dorsal root ganglia (DRG) neurons. Phosphorylation of newly synthesized middle molecular mass neurofilament polypeptide (NF-M) is inhibited by 10-25 mM LiCl, and tubulin (Tb) synthesized in the presence of Li+ is subject to rapid degradation. These Li(+)-induced metabolic abnormalities are accompanied by alterations in cellular and cytoskeletal morphology. Treatment of cultures having vigorously growing neurites with 25 mM LiCl results in the cessation of net neurite growth, without causing neurite retraction. Indirect immunofluorescence reveals that in these cultures Li+ provokes an aggregation of NF protein into a dense knot in the cell body/proximal neurite region. The knots contain accumulations of all three NF polypeptides and electron microscopic observation demonstrates that the knots contain intact, but disorganized, filaments. Both the inhibition of neurite outgrowth and NF collapse are reversible. Tubulin and intact microtubules are redistributed in immature cultures treated with Li+ insofar as they are excluded from the NF knots. Neurons in established cultures (e.g., 7 days and beyond) fail to show any difference between Li+ treatment and control conditions in the morphology of the cytoskeletal elements examined.
 ...
PMID:Lithium chloride alters cytoskeletal organization in growing, but not mature, cultured chick sensory neurons. 164 21

The terminal stage of differentiation of nucleated chicken erythrocytes is associated with an overall gene repression and a condensation of the repressed chromatin portion. Two-dimensional DNP electrophoresis has been used to separate transcriptionally active and repressed chromatin of mature chicken erythrocytes. The repressed chromatin fraction is shown to be enriched with histone H5 as well as with a 42-kDa nonhistone chromosomal protein. The 42-kDa protein designated here as MENT (mature erythrocyte nuclear termination stage-specific protein) is hyperexpressed at the terminal stage of chicken erythropoiesis and is accumulated in adult chicken erythrocyte nuclei. This protein was purified by ion-exchange chromatography from 0.4 M NaCl extracts of the erythrocyte nuclei. It appeared to be a basic polypeptide (pI 9.2) which, however, precipitated at low pH. When reconstituted in vitro with immature erythrocyte nuclei, MENT promoted condensation of intact nuclear chromatin and enhanced the solubilization of nuclease-digested polynucleosomes, thus mimicking the processes occurring in vivo at the final stage of erythrocyte maturation. The extent of dissociation of specific gene sequences from the nuclear matrix in MENT-treated nuclei is in striking correlation with their transcriptional activity. No other basic proteins (H5, cytochrome c, RNase A) added to the nuclear preparation at the same level as MENT (protein/DNA = 0.005) caused any effect on nuclear organization. No alterations were observed when MENT was mixed with erythroblasts and nonerythroid nuclei having little or no histone H5. We propose that MENT cooperates with histone H5 to complete the nuclear collapse in mature nucleated erythrocytes.
 ...
PMID:A novel nonhistone protein (MENT) promotes nuclear collapse at the terminal stage of avian erythropoiesis. 172 33

The background to the concept of the term "molten globule" as a description of intermediates observed in the folding of globular proteins is discussed. These compact intermediates are characterised by certain properties including the presence of secondary structure and considerable conformational mobility compared to the native, functional state. Those intermediates that are thermodynamically stable under mild denaturing conditions have many features in common with the transient intermediates that accumulate significantly during the process of folding. Attention is drawn to cases where the two types are however distinguished on grounds of their Stokes radius, in which cases there is currently no direct evidence for the involvement of the stable intermediates on the folding pathway. Experimental evidence relating to the early stages in folding is reviewed and compared, highlighting the temporal relationship between general collapse of the polypeptide chain and the formation of secondary structure. The continued use of the term "molten globule" is recommended where the minimum essential structural criteria for this state are met.
 ...
PMID:Molten globule intermediates and protein folding. 206 Apr 95

The mechanism of yolk deposition into developing oocytes of Drosophila was investigated by following the fate of a reporter protein fused to a vitellogenin, or yolk polypeptide (YP). Embryos were transformed with a hybrid gene consisting of the promotor and amino terminal 430 codons of the Yp2 gene fused to the cytoplasmic form of the invertase gene from the yeast Saccharomyces cerevisiae. RNA hybridization experiments with established lines of transformed flies showed that the hybrid gene was expressed in female fat bodies and ovaries but not in any male cells. Immunoblotting and endoglycosidase digestion showed that the hybrid protein was secreted from fat body cells via the secretory pathway, transported in hemolymph, and sequestered into developing oocytes. Transfusion experiments with hemolymph and pure invertase showed that sequestration of invertase depended on its attachment to YP. Immunocytochemistry demonstrated that the hybrid protein became localized in yolk granules as oocytes developed. Females homozygous for the fusion gene are generally sterile; their eggs containing the hybrid protein often collapse and their embryos fail to develop, suggesting that the structure of the yolk polypeptides is important for embryonic development. These experiments show that YP2 carries structural information sufficient to direct a reporter protein from fat body cells, through the hemolymph, and into the yolk granules of developing oocytes. This work provides a means of identifying the features of yolk polypeptides that are responsible for their deposition into yolk during oogenesis.
 ...
PMID:Vitellogenesis in Drosophila: sequestration of a yolk polypeptide/invertase fusion protein into developing oocytes. 211 78

We have identified a novel actin-related 60-kDa polypeptide in mammalian cells. The relatedness of this polypeptide to actin is indicated by its affinity for DNase I, two monoclonal anti-actin antibodies, and two independent peptide-specific anti-actin antibodies which bind to actin at around amino acid 244. It is not incorporated into cytoskeletal stress fibers, although it is a stable protein. Its expression (60-kDa polypeptide, pI of 5.4 to 5.5) is inhibited by the K+ ionophore, nonactin, which is known to collapse the energy-dependent translocation of cytoplasmically synthesized proteins into mitochondria.
 ...
PMID:A 60-kDa polypeptide in mammalian cells with epitopes related to actin. 244 92

Vaso-active intestinal polypeptide (VIP) and the related peptide, peptide histidine isoleucine, were infused intravenously in anaesthetized sheep. The VIP doses were designed to reproduce plasma concentrations seen after mesenteric ischaemia. The vasodilator action of VIP varied between different segments of the circulation and these differences in sensitivity were observed for both the degree and duration of the vaso-active action. A sustained vasodilation was detected in the coeliac artery and portal vein vascular beds during a 30-min VIP infusion. VIP is likely to be a contributory factor involved in the development of circulatory collapse during reperfusion after experimental mesenteric ischaemia.
 ...
PMID:Effect of vaso-active intestinal polypeptide on systemic and splanchnic haemodynamics: role in vasodilation following mesenteric ischaemia. 323 19

The kinetics of unfolding and refolding of porcine ribonuclease were investigated. The unfolded state of this protein was found to consist of a fast-refolding species (UF) and two slow-refolding species (UIS and UIIS). After the rapid collapse of the structure during the N (native)----UF unfolding reaction, UIS and UIIS are produced from UF by two independent slow isomerizations of the unfolded polypeptide chain, leading ultimately to a mixture of about 10% UF, 20% UIIS and 70% UIS molecules at equilibrium. This is at variance with all other ribonucleases investigated to date, which show a distribution of 20% UF, 60 to 70% UIIS and only 10 to 20% UIS. The two isomerizations of the unfolded porcine protein differ strongly in rate. The first process with tau = 250 seconds (10 degrees C) leads to an increase in the fluorescence of Tyr92 and was identified as cis in equilibrium trans isomerization of Pro93. At equilibrium, most unfolded molecules contain an incorrect trans Pro93. The second isomerization is much slower (tau = 1300 s at 10 degrees C) and leads to a predominance of the incorrect isomer as well. Like isomerization of Pro93, it is governed by an activation enthalpy of 22 kcal/mol (92 kJ/mol) and it was tentatively assigned to the Pro114-Pro115 sequence of porcine ribonuclease. Because of the wide separation in rate between the two reactions, molecules with an incorrect isomer only at Pro93 accumulate transiently after unfolding. These are the UIIS molecules. Most of them are finally converted to UIS by the 1300 second process. All molecules that have undergone this isomerization refold very slowly, i.e. the UIS molecules. The major fraction contains two incorrect isomers. A 1300 second isomerization after unfolding and a predominant very slow refolding reaction were observed only for the porcine protein. We suggest that these changes in the folding mechanism may be correlated with the presence of the Pro114-Pro115 sequence, which occurs only in porcine ribonuclease. The refolding pathway of porcine UIIS involves the rapid formation of a native-like intermediate with an incorrect trans Pro93 as was found previously for the bovine ribonuclease, where the UIIS species predominates in the unfolded state.
 ...
PMID:Folding mechanism of porcine ribonuclease. 380 74

In this article we show a Triton-insoluble, intermediate filament-associated protein of approximately 70 kD to be expressed ubiquitously in diverse mammalian cell types. This protein, assigned the name beta-internexin, exhibits extreme homology in each of the various cell lines as demonstrated by identical limited peptide maps, similar mobilities on two-dimensional gels, and detection in Triton-soluble and -insoluble extracts. beta-Internexin also shares some degree of homology with alpha-internexin, an intermediate filament-associated protein isolated and purified from rat spinal cord, which accounts for the immunologic cross-reactivity displayed by these polypeptides. Light microscopic immunolocalization of beta-internexin with a monoclonal antibody (mAb-IN30) reveals it to be closely associated with the vimentin network in fibroblasts. The antigen is also observed to collapse with the vimentin reticulum during the formation of a juxtanuclear cap induced by colchicine treatment. Ultrastructural localization, using colloidal gold, substantiates the affinity of beta-internexin for cytoplasmic filaments and, in addition, demonstrates its apparent exclusion from the intranuclear filament network. We examine also the resemblance of beta-internexin to a microtubule-associated polypeptide and the constitutively synthesized mammalian heat shock protein (HSP 68/70).
 ...
PMID:beta-Internexin, a ubiquitous intermediate filament-associated protein. 390 89

In an effort to stimulate the in vivo formation of active enzyme from newly synthesized polypeptide chains, we have studied the in vitro assembly of the active catalytic subunits of aspartate transcarbamoylase from unfolded polypeptide chains. Hydrodynamic and spectroscopic measurements showed that incubating the catalytic trimers in 4.7 M urea for 45 min at 9 degrees C produced unfolded polypeptide chains largely devoid of the secondary and tertiary structures characteristic of native subunits. Dilution of the urea solutions led to the slow restoration of enzyme activity and the formation of trimers at a rate which could be measured quantitatively by a hybridization technique using succinylated polypeptide chains as a "chase" to "stop" the assembly. Kinetic studies showed that reactivation and assembly of trimers were coincident with a half-time for completion of about 50 min at 0 degrees C. Also, the rate-limiting reaction was first order. Although these results suggest that chain folding is the slow process, spectroscopic studies indicated that large changes in the environments of the aromatic amino acid residues occur very rapidly. Indeed the changes in the absorption spectrum are largely complete before significant reactivation and trimer formation occur. The results are consistent with an assembly mechanism in which the first step is the rapid collapse of the expanded randomly coiled chains to give partially folded monomers. These monomers are not enzymically active and cannot associate to form trimers until a rate-limiting conformational change occurs. Subsequent to this slow process, the "competent" monomers associate via a series of reactions to form active trimers.
 ...
PMID:Assembly of the catalytic trimers of aspartate transcarbamoylase from unfolded polypeptide chains. 709 28


1 2 3 4 5 6 7 8 9 10 Next >>