Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.7.10.1 (ERK)
95,504 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

It is established that the part of the SEA and SEC2 polypeptide chain responsible for the binding of these toxin proteins with the membrane receptor on the surface of rabbit thymocytes and mitogenic effect is localised in the NH2-terminal region of the molecule. The SEC2 splits in two fragments T1 (17 kdalton) and T2 (12.5 kdalton) under limited proteolysis by trypsin in the presence of 2-ME. The amino acid terminal residues of SEA, SEC2 and their proteolytic fragments are also studied.
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PMID:NH2-terminal localization of that part of the staphylococcal enterotoxins polypeptide chain responsible for binding with membrane receptor and mitogenic effect. 348 88

Insulin-like growth factors (IGF's) circulate in blood complexed to specific carrier proteins. The BRL 3A and BRL 3A2 rat liver cell lines secrete a 30,000-50,000 mol wt IGF carrier protein. Since the liver parenchymal cell is a likely source of IGF carrier protein synthesis, we have evaluated medium conditioned by three human hepatocellular carcinoma- or hepatoblastoma-derived cell lines for the presence of IGF carrier protein. The HEP G2 and the HEP 3B, but not the PLC/PRF/5, cell lines secrete a specific IGF carrier protein(s) into serum-free medium. This carrier protein is specific for IGF molecules. Multiplication-stimulating activity, IGF I, and IGF II were equipotent in competing for the binding of [125I]multiplication-stimulating activity to HEP G2 medium. The HEP G2 IGF carrier protein is trypsin sensitive, acid stabile, and does not contain a glycoprotein moiety. It has a molecular size of 30,000-50,000, as assessed by Sephadex G-200 gel filtration. These studies suggest that the HEP G2 cell line is a useful model to study the synthesis and secretion of human IGF carrier protein.
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PMID:Demonstration that a human hepatoma cell line produces a specific insulin-like growth factor carrier protein. 618 61

Alpha 1 protease inhibitor antigen was identified in the culture medium of the human ascites hepatoma cell line SK-HEP-1. Trypsin inhibitory activity and alpha 1 Pl antigen accumulated in serum-free medium concomitantly over a period of several days. Radioactive alpha 1 Pl antigen was detected in conditioned medium from cultures supplemented with 35S-L-methionine, indicating a synthesis and release of the protein. Alpha 1 Pl antigen in conditioned medium appeared to be antigenically identical to that in human plasma, and the newly synthesized (radiolabeled) antigen co-migrated with plasma, alpha 1 Pl after immunoelectrophoresis or SDS-polyacrylamide gel electrophoresis. Moreover, evidence is presented that the synthesized inhibitor exhibits functional activity, since the 35S-labeled alpha 1 Pl in conditioned medium complexes with trypsin. We conclude that SK-HEP-1 cells in culture produce functionally active alpha 1 Pl which may be identical to that in plasma.
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PMID:Functional alpha 1 protease inhibitor produced by a human hepatoma cell line. 627 80

The cholecystokinin (CCK) receptor in purified plasma membranes prepared from mouse pancreatic acini had a binding affinity of 1.8 nM, an acid pH optimum between 6.0 and 6.5, and an analog specificity of CCK8 greater than CCK33 greater than desulphated CCK8 greater than CCK4. Binding of CCK to its receptor was abolished by pretreatment of plasma membranes with trypsin. When [125I]CCK was cross-linked to its receptors with disuccinimidyl suberate, and the preparation solubilized and subjected to gel electrophoresis and autoradiography, the hormone was associated with Mr 80 000 protein in both the presence and absence of the reducing agent dithiothreitol.
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PMID:The CCK receptor on pancreatic plasma membranes: binding characteristics and covalent cross-linking. 629 90

Supernatants from 24 hr cultures of PHA-pulsed human T lymphocytes inhibit the migration of human peripheral blood T lymphocytes and guinea pig macrophages in vitro. The factor responsible for the inhibition of T lymphocytes provisionally called TIF (T cell migration inhibitory factor) was separated from MIF by preparative PAGE, had apparent molecular weight (m.w.) of 1,000-10,000 daltons and isoelectric point of 3.1. TIF activity was resistant to treatment with trypsin, chymotrypsin and neuraminidase but sensitive to PMSF (phenyl-methyl-sulfonyl-fluoride). This suggests that TIF is presumably different from human MIF and may represent a novel lymphokine which preferentially affects T cell migration in vitro.
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PMID:Partial purification and physicochemical properties of human T cell migration inhibitory factor (TIF). 639 62

We have studied the physiological effects of mitomycin C induction on cells carrying ColE1 plasmids with differing configurations of three genes: the structural gene coding for colicin (cea), a gene responsible for mitomycin C lethality (kil) that we located as part of an operon with cea, and the immunity (imm) gene, which lies near cea but is not in the same operon. kil is close to or overlaps imm. When cea(+) plasmids are present mitomycin C induction results in 100-fold or greater increases in the level of colicin. Within an hour after induction more than 90% of cells carrying cea(+)kil(+) plasmids are killed and macromolecular synthesis stops, capacity for transport of proline, thiomethyl beta-D-galactoside, and alpha-methyl glucoside is lost, and the membrane becomes abnormally permeable as indicated by an increased accessibility of intracellular beta-galactosidase to the substrate o-nitrophenyl beta-D-galactoside. All of these events occur when a cea(-)kil(+)imm(+) plasmid is present and none does when the plasmid is cea(+)kil(-)imm(+), so the damage can be attributed solely to the Kil function and not to the presence of colicin. However, cells carrying a cea(+)kil(-)imm(-) plasmid are killed upon induction, apparently by action of endogenous colicin on the nonimmune cytoplasmic membrane. The pattern of accompanying physiological damage is distinguished from the kil(+)-associated damage by an enhancement of alpha-methyl glucoside uptake and accumulation and efflux of alpha-methyl glucoside 6-phosphate and by an absence of the alteration in membrane permeability for o-nitrophenyl beta-D-galactoside. These features are typical of colicin E1 action on the membrane. The induced damage is not prevented by trypsin and occurs in cells of a strain specifically tolerant to exogenous colicin E1, indicating that the attack is from inside the cell.
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PMID:Alternative forms of lethality in mitomycin C-induced bacteria carrying ColE1 plasmids. 640 39

Four fragments (F1-F4) of SEA, obtained via papain proteolysis were separated and isolated as individual components by means of the SDS-electrophoresis in polyacrilamide gel. Molecular masses of the pairs F1 + F4 and F2 + F3 are equal to the mass of the intact toxin--a fact that supposes a cleavage of polypeptide chain in two regions of "disulphide loop" in a SEA molecule. Neither fragment possesses any enterpathogenic properties. It was established, that interferonogenic and mitogenic activity of SEA is connected only with the part of molecule corresponding to F1(17,500) and F3(15,000). Two kinds of antigenic determinants in the SEA molecule were found: one was attributed to F1 and F3 fragments, the other was localised in F2 and F4. Proteolysis by trypsin led to cleavage of a small peptide from the N-terminal end of toxin molecule. Trypsinized SEA displayed all kinds of biological activity characterizing the native toxin.
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PMID:Topology of the functions in molecule of staphylococcal enterotoxin Type A. 670 70

Collagen synthesis in serially propagated cultures of rat mucosal keratinocytes (line RTK-I) was investigated. Analysis of biosynthetically labeled cell and media proteins retrieved after limited pepsin digestion revealed seven or eight collagen chains originating from four distinct collagens (types I, III, IV, V). Type III collagen was identified as the predominant species based on its electrophoretic and chromatographic behavior in the reduced and unreduced states, on the peptide pattern generated by limited cleavage with CNBr and with trypsin, and on the immunofluorescent detection of intracellular, collagen type III-reactive material. Evidence for the synthesis of two type IV collagen chains (155 k and 160 k after limited pepsin digestion) was provided by immunofluorescent and electrophoretic studies. Type V collagen was revealed by immunofluorescence, and two, possibly three, component chains were resolved in native type V collagen isolated from the harvest medium. Type I collagen, identified by comigration with authentic carriers, was a constant but quantitatively variable synthetic product. This study provides evidence that keratinocytes produce collagens normally found in mesenchymal matrices (type I and III) in addition to collagens characteristic of basement membranes (type IV) and of pericellular structures (type V). These findings reveal a hitherto unrecognized complexity and heterogeneity of the collagens synthesized by a highly differentiated epithelial cell type.
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PMID:Multiple collagen gene expression with type III predominance in rat mucosal keratinocytes. 712 46

Alternate splicing of a single exon encoding an NH2-terminal immunoglobulin (Ig) disulfide loop in the ectodomain of the fibroblast growth factor receptor (FGFR) types 1 and 2 results in alpha and beta isoforms that exhibit 3- and 2-Ig loops, respectively. Previously we demonstrated that alternately spliced Loop I has no independent ligand binding activity but is sufficiently interactive with the ligand- and heparin-binding site formed by Loops II and III to lower affinity for the same fibroblast growth factor (FGF) ligand. Here we show that a lower affinity of FGFR1 alpha for heparin parallels the lower affinity for FGF-1. A mutant of FGFR1 alpha in which the sequence between Loops I and II was deleted exhibits high affinity for both FGF-1 and heparin and other properties of the FGFR1 beta isoform, which include resistance to degradation by trypsin and display of specific antibody epitopes. This suggests that the interloop sequence facilitates the interaction of Loop I with Loops II and III. Lack of expression of both exons coding for Loop I and the sequence between Loops I and II in the FGFR2 gene characterizes rat prostate tumor cells, which exhibit a loss of the low affinity class of FGF receptors. Although the exon coding for the sequence between Loops I and II is alternately spliced in the FGFR2 beta isoform, coordinate expression with the exon coding for Loop I results in the functional differences between the FGFR alpha and FGFR beta variants.
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PMID:Alternately spliced NH2-terminal immunoglobulin-like Loop I in the ectodomain of the fibroblast growth factor (FGF) receptor 1 lowers affinity for both heparin and FGF-1. 773 Mar 27

We show that antibodies to the CD44 molecule trigger proliferation of human CD3+/CD4+ T-cell clones. Such effect is IL2-dependent, as shown by IL2 production induced by anti-CD44 mAb and by inhibition of cell proliferation in the presence of anti-IL2 antibodies or cyclosporin A (CsA). Moreover, anti-CD44 mAb triggered human cytolytic CD4+ and CD8+ TCR alpha/beta+ clones, and V delta 1 or V delta 2 TCR Y/delta+ clones to lyse Fc-gamma-R+ P815 cells and to release granule trypsin-like esterase enzymes. Anti-CD44 mAb-triggered proliferation and cytotoxicity were blocked by the PTK-inhibitor, genestein. In addition, ligation of the CD44 molecule induced tyrosine phosphorylation of proteins identical, by molecular weight, to those phosphorylated following anti-CD3 mAb-stimulation. Notably, anti-CD44 mAb does not induce tyrosine phosphorylation of a 21 kD protein (the phosphorylated zeta chain of the TcR molecular complex) typically observed upon anti-CD3 mAb stimulation.
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PMID:Ligation of the lymphocyte homing receptor CD44 triggers T-helper and cytolytic functions of human T cells. 776 33


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