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)

The isolation and characterization of an isotype-specific autoantibody-secreting hybridoma NET/2/3 from rats bearing the syngeneic tumour HSN is described. This rheumatoid factor of the IgM class recognizes an epitope within the hinge region of rat immunoglobulins of the IgG2b subclass which is destroyed by reduction of disulphide bonds. The specificity of NET/2/3, although not allotype-restricted, is highly isotype-restricted, as it does not bind to rat Ig other than IgG2b, nor does it react with the majority of mouse IgG, although some reactivity occurs with mouse IgG3. One remarkable feature of NET 2/3 is that it binds more strongly to F(ab')2 and Fab' fragments of rat IgG2b, obtained by digestion with pepsin, than to the whole molecule. This anti-isotype response is not peculiar to the HSN tumour model as NET/2/3-like antibodies have been found in the sera of rats immunized with various protein and cellular antigens. The possible biological role of this anti-isotype antibody is discussed.
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PMID:Isolation and characterization of a monoclonal rheumatoid factor specific for the hinge region of rat IgG2b. 186 82

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

Some prenatal pathological processes may be caused by biochemical and morphological alterations in the umbilical cord (UC). EPH-gestosis is the most common pregnancy-associated pathological process. For these reasons the role of collagen and glycos-aminoglycans (GAGs) of UC in pathobiochemistry of this syndrome seems to be important. We studied histology of extracellular matrix components, quantity, solubility and molecular polymorphism of collagen, proportional relationships between various types of collagen, the amounts of GAGs and proportional relationships between them in Wharton's jelly of control newborns delivered by healthy mothers and those delivered by mothers with EPH-gestosis. We found that Wharton's jelly is abundant in collagen and GAGs. This collagen is very insoluble and resistant to the action of depolymerizing agents (4% EDTA-Na2, pepsin). Types I, III and V collagens were isolated and quantified. Hyaluronic acid constitutes about 70%, whereas sulphated GAGs constitute about 30% of total GAGs. EPH-gestosis is accompanied by significant increase in sulphated GAGs: hyaluronic acid ratio. The EPH-gestosis-associated alterations in Wharton's jelly correspond to 'premature ageing' of this tissue.
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PMID:Collagen and glycosaminoglycans of Wharton's jelly and their alterations in EPH-gestosis. 873 30

Spherical microporous reservoir-type microcapsules, fabricated using a W/O/W double emulsion technique with solvent evaporation and composed of 330 kD poly(beta-hydroxybutyrate-hydroxyvalerate (P(HB-HV)) (10.8% HV)/20% PCL II containing a range of bovine serum albumin (BSA) loadings, were incubated in Hank's buffer, pH 7.4, newborn calf serum (NCS), 1.5% pancreatin and synthetic gastric juice containing 10% pepsin over 30 days, and their percentage weight loss (PWL) and change in ultrastructural morphology monitored by gravimetry and stereoscan electron microscopy (SEM), respectively. The greatest percentage weight loss from microcapsules was observed after incubation in NCS and decreased in the other NCS > pancreatin > synthetic gastric juice > Hank's buffer. Only 5, 10 and 15% bovine serum albumin (BSA) loaded microcapsules incubated in Hank's buffer and synthetic gastric juice showed a significant increase in PWL with increasing percentage BSA loading. The overall sequence of changes in structural morphology due to biodegradation occurred at different rates in the different 'physiological' media. An initial increase in micropore diameter was followed by the coalescence of microspores to form macroporous pits (Hank's buffer). Further biodegradation in NCS, pancreatin and synthetic juice was characterized by significant surface and bulk erosion. Only in pancreatin and NCS did biodegradation proceed to a loss of spherical shape and partial (pancreatin) and almost total (NCS) disruption of microcapsule structure after 30 days.
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PMID:In vitro biodegradation of polyhydroxybutyrate-hydroxyvalerate microcapsules exposed to Hank's buffer, newborn calf serum, pancreatin and synthetic gastric juice. 899 74

Type IV collagen (COL-IV) interacts with a variety of cell types. We present evidence that human mesangial cells (HMC) bind directly to COL-IV, its major triple helical domain, and the main non-collagenous, NC1 domain. A synthetic peptide, HEP-III, and its triple helical counterpart (THP-III), previously reported to be a heparin-binding domain, also promoted approximately 15% adhesion of HMC. HMC bound to solid-phase-immobilized, intact COL-IV (approximately 75%), isolated NC1 domain (approximately 15%), and a pepsin-derived triple helical fragment,which lacks Hep-III (approximately 65%). We further examined inhibition of HMC adhesion to COL-IV and its domains by using anti-integrin antibodies. Blocking monoclonal antibodies against the alpha2 integrin resulted in 70% inhibition of adhesion to COL-IV and 80% inhibition to HEP-III. Moderate inhibition was observed on the NC1 and triple helical fragments. Anti-alpha1 antibodies inhibited the binding of HMC to COL-IV, the NC1, and triple helical domains, but not to peptide HEP-III. Anti-beta1 antibodies inhibited almost completely (>95%) the adhesion to COL-IV, the NC1, and triple helical fragments; inhibition on HEP-III was approximately 30%. Affinity chromatography studies with solid-phase HEP-III and mesangial cell lysate also demonstrated the presence of integrin alpha2 beta1 along with alpha3 beta1. We conclude that alpha2 beta1 and alpha1 beta1 integrins mediate HMC adhesion to COL-IV. Peptide HEP-III is a major, specific site for alpha2 integrin-mediated binding of mesangial cells to COL-IV. Both the alpha1 beta1 and alpha2 beta1 integrins interact with the NC1 and triple helical fragments of COL-IV. Therefore, we demonstrate that several sites for integrin-mediated interactions exist on several collagenous and non-collagenous domains of COL-IV.
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PMID:Interactions of type IV collagen and its domains with human mesangial cells. 957 74

Spherical reservoir-type microcapsules fabricated using a water/oil/water (W/O/W) double emulsion technique with solvent evaporation and composed of poly(ethylene adipate) (PEAD) blended with 20% poly-epsilon-caprolactone (PCL II) containing a range of bovine serum albumin (BSA) loadings were incubated in Hank's buffer, pH 7.4, newborn calf serum, 1.5% pancreatin and synthetic gastric juice containing 10% pepsin A over 30 days and their percentage weight loss (PWL) and changes in ultrastructural morphology monitored by gravimetry and stereoscan electron microscopy (SEM) respectively. The greatest PWL from microcapsules was observed after incubation in newborn calf serum (NCS) and pancreatin and decreased in the order NCS > pancreatin > synthetic gastric juice > Hank's buffer. Only microcapsules theoretically loaded with 5-20% BSA and incubated in synthetic gastric juice showed a significant increase in PWL with increasing percentage BSA loading. The structural biodegradation of PEAD microcapsules in both Hank's buffer and synthetic gastric juice was minimal whilst the morphological changes observed during incubation in NCS involved pitting of the membrane, some surface erosion and reduction in diameter, followed by microcapsule membrane disruption and loss of reservoir contents. Biodegradation in pancreatin was associated with surface flaking and loss of large fragments of the microcapsule membrane. Only in NCS and pancreatin, where one would expect to see the effects of enzyme activity in addition to simple ester hydrolysis, did biodegradation proceed to the stage where there was a loss of spherical shape and almost total disruption of the microcapsule structure within 30 days.
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PMID:Biodegradation of poly(ethylene adipate) microcapsules in physiological media. 967 51

Fluorescence in situ hybridization (FISH) is difficult to accomplish using thin-sections of paraffin-embedded lymphoid tissue because of the high cellularity and truncated cells that interfere with accurate scoring of individual nuclei. We modified and tested a new technique to isolate individual nuclei from tissue cores of paraffin-embedded tissue processed with xylene, proteinase K, citric acid, and pepsin. The efficacy of this method to study paraffin-embedded tissue was investigated in six normal lymph nodes or tonsils and 32 malignant lymphomas including five mantle cell, five follicular, five Burkitt, five extranodal marginal zone lymphomas of mucosa-associated lymphoid tissue, five anaplastic large-cell, and seven diffuse large B-cell. Fusion of CCND1 and IgH, BCL2 and IgH, c-myc and IgH, and MALT1 and API2 were detected using probes with a dual-fusion FISH strategy. Anomalies involving ALK and BCL6 were detected using break-apart FISH probes. FISH studies were successful for each of the 38 specimens. Chromosome anomalies were detected in each malignant specimen, but not in the normal lymphoid tissue. The correct chromosome anomaly was detected in 22 of 22 specimens with genetic abnormalities that were established by other genetic techniques. This FISH technique is useful to detect chromosome anomalies with high sensitivity and specificity in paraffin-embedded tissue and may provide important diagnostic and prognostic genetic information.
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PMID:A new method to extract nuclei from paraffin-embedded tissue to study lymphomas using interphase fluorescence in situ hybridization. 1205 1

The degradation and erosion of solvent cast films and injection molded bars prepared from poly(epsilon-caprolactone) (PCL) and 2,2'-bis(2-oxazoline) linked poly(epsilon-caprolactone) (PCL-O) were evaluated in simulated gastric fluid (SGF) (pH 1.2, pepsin present) and in simulated intestinal fluid (SIF) (pH 7.5, pancreatin present). After incubation of the polymer films (10 mg) and bars (70 mg) in the medium, the resulting decrease in molecular weight (degradation) was determined by size exclusion chromatography and the weight loss of the preparations was measured. In addition, the effect of pancreatin on FITC-dextran (MW 4400) release from PCL and PCL-O microparticles, prepared by w/o/w double emulsion technique, was studied. No degradation or weight loss was observed for either PCL or PCL-O films in SGF (12 h incubation, 37 degrees C). When compared to PBS pH 7.4, pancreatin hardly enhanced the weight loss of PCL films and bars. In contrast, pancreatin enhanced substantially erosion of PCL-O films and bars. Unlike PCL preparations, the PCL-O preparations showed surface erosion in SIF. Pancreatin increased considerably FITC-dextran release from both PCL and PCL-O microparticles. In conclusion, the present results demonstrate the enzyme sensitivity of the novel PCL-O polymer. In addition, the results show that pancreatin present in intestinal fluid may substantially affect drug release from PCL based preparations.
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PMID:Pancreatin enhanced erosion of and macromolecule release from 2,2-bis(2-oxazoline)-linked poly(epsilon-caprolactone). 1252 18

Pepstatin A is well known to be an inhibitor of aspartic proteinases such as pepsin, cathepsins D and E. Except for its role as a proteinase inhibitor, however, the pharmacological action of pepstatin A upon cells remain unclear. In this study, we found that pepstatin A suppressed receptor activator of NF-kappaB ligand (RANKL)-induced osteoclast differentiation. Pepstatin A suppressed the formation of multinuclear osteoclasts dose-dependently. This inhibition of the formation only affected osteoclast cells, i.e., not osteoblast-like cells. Furthermore, pepstatin A also suppressed differentiation from pre-osteoclast cells to mononuclear osteoclast cells dose-dependently. This inhibition seems to be independent of the activities of proteinases such as cathepsin D, because the formation of osteoclasts was not suppressed with the concentration that inhibited the activity of cathepsin D. Cell signaling analysis indicated that the phosphorylation of ERK was inhibited in pepstatin A-treated cells, while the phosphorylation of IkappaB and Akt showed almost no change. Furthermore, pepstatin A decreased the expression of nuclear factor of activated T cells c1 (NFATc1). These results suggest that pepstatin A suppresses the differentiation of osteoclasts through the blockade of ERK signaling and the inhibition of NFATc1 expression.
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PMID:Pepstatin A, an aspartic proteinase inhibitor, suppresses RANKL-induced osteoclast differentiation. 1656 24

Bioactive peptides with a variety of effects have been described from several nutritive proteins. They exhibit antimicrobial, blood-pressure lowering, antithrombotic, immunomodulatory, and cholesterol-modulating effects. In this study, we have examined whether peptides derived from food proteins might influence bile acid synthesis. A reporter gene cell line that carries a cholesterol 7alpha-hydroxylase promoter fragment fused to firefly luciferase ( cyp7a-luc) was used to screen for nutritive peptides affecting cyp7a expression, the enzyme catalyzing the rate-limiting step in bile acid synthesis. Proteolytic hydrolysates were prepared from soy protein and bovine casein with pepsin, trypsin, chymotrypsin, and elastase and size fractionated using ultrafiltration. Several bioactive hydrolysates could be identified that inhibited luciferase expression. Also, an activation of kinase (AKT, ERK, p38-MAPK) signaling could be observed. Selected hydrolysates were further fractionated by reversed-phase HPLC. Bioactive HPLC-fractions were obtained from casein but not from soy hydrolysates; however, activity could not be recovered in single peak fractions. Peptides in such fractions were identified by mass spectrometry. Five selected peptides from alpha S1-casein present in active fractions were synthesized, but none of these showed activity in the cyp7a-luc screening system. However, two of them activated MAP-kinase signaling similar to the hydrolysates, which suggests, that these peptides are involved in cyp7a regulation by the casein hydrolysates.
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PMID:Screening for nutritive peptides that modify cholesterol 7alpha-hydroxylase expression. 1854 26


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