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PubMed1998

Characterization of the maize prolamin box-binding factor-1 (PBF-1) and its role in the developmental regulation of the zein multigene family.

A maize prolamin box (P-box)-binding factor (PBF-1) has been purified and characterized from immature endosperm tissue. PBF-1 has a molecular weight of 38kDa. It is detected only in endosperm, but not in root or leaf tissues, consistent with its tissue-specific function. Site-directed mutagenesis experiments reveal that both the P-box and its flanking sequences are important for PBF-1 DNA binding. Developmental studies show that PBF-1 accumulates in the endosperm from 8 to at least 30days after pollination (DAP). From 16 to 24DAP, however, multiple shifted bands of protein(s)-DNA complexes can be observed, which correlate with an increase in zein gene expression. PBF-1 can also bind to the P-box from '22-kDa' and '19-kDa' zein promoters, but at a lower affinity than to the '27-kDa' zein promoter. The effects of protein dephosphorylation and zinc ion chelators on PBF-1 DNA binding activity are also shown. A model is proposed where PBF-1 serves as a 'recruiter' of class-specific transcription factors like Opaque2 (O2).

Chromatography, Affinity↗
PubMed2004

Conformation of the Z19 prolamin by FTIR, NMR, and SAXS.

The alpha zein, the maize storage prolamin, is a mixture of several homologous polypeptides that shows two bands in SDS-PAGE, called Z19 and Z22. The conformation studies carried out by several authors in this mixture are conflicting. To elucidate these inconsistencies, we analyzed the conformation of the Z19 fraction, extracted from BR451 maize variety by Fourier transform infrared spectroscopy, nuclear magnetic resonance, and small-angle X-ray scattering. The infrared results show that Z19 has 46% of alpha helix and 22% of beta sheet. The fast N-H to N-D exchange measured by (1)H NMR spectroscopy showed that Z19 is not a compact structure. The scattering measurements indicated an extended structure with 12 by 130 A. With these data, we have modeled the Z19 structure as a hairpin, composed of helical, sheet, turns, and secondary structures, folded back on itself.

Magnetic Resonance Spectroscopy↗
PubMed1987

[Morphologic findings after intracerebral administration of an alcoholic prolamine solution].

Morphological studies were performed after intracerebral injection of Ethibloc (E.), an alcoholic prolamine solution, to prove the usefulness of E. as a drug depot in the local chemotherapy of brain gliomas. Organisation of E. starts 2-3 weeks after injection, but remains incomplete even 24 weeks later. This depot cannot be removed in case of diminished drug concentration because of the extremely close connection with the adjacent brain tissue. Further repeated injection of drug into the E. depot cannot reach the tumours periphery because of the surrounding glial scar and connective tissue.

Animals↗
PubMed2006

Barley and rye prolamins induce an mRNA interferon-gamma response in coeliac mucosa.

BACKGROUND: In coeliac disease, wheat, barley and rye are traditionally excluded in the gluten-free diet. However, few studies have examined the small intestinal immune response to barley and rye. AIM: To investigate the immunogenicity of barley and rye prolamins (hordein and secalin respectively) in comparison with wheat gliadin. METHODS: Duodenal biopsies from 22 coeliac patients and 23 disease controls were cultured for 4 h with gliadin, hordein or secalin and compared with culture medium alone. Proinflammatory cytokines, interferon-gamma and interleukin-2, were quantified by TaqMan polymerase chain reaction and enzyme-linked immunosorbent assay. RESULTS: Hordein caused the greatest increase in interferon-gamma mRNA in coeliac patients (median: 3.3-fold) in comparison with control subjects (median: 0.28-fold, P < 0.085). Secalin and gliadin induced similar levels of interferon-gamma mRNA with median fold-changes of 3.4 and 2.8, respectively, in coeliac patients in comparison with 1.6- and 1.1-fold increases in control subjects (P < 0.294 and P < 0.105, respectively). The median fold-changes for interleukin-2 mRNA did not differ between coeliac patients and controls. Cytokine protein was not upregulated. CONCLUSION: The findings of this study provide evidence that barley and rye cause immune activation in the mucosa of coeliac patients and support the practice that barley and rye should be excluded from the gluten-free diet.

Adult↗
PubMed2002

Characterization of pearl millet prolamins.

We report the physical-chemical characterization of the major alcohol-soluble proteins present in seeds of pearl millet (Pennisetum glaucum) by SDS-PAGE, bidimensional gel electrophoresis, MALDI-TOF/MS and RP-HPLC. We demonstrate the presence of three major prolamins, called A-, B- and C-pennisetin with mass values around 27, 22 and 12 kDa, respectively. We present partial amino acid sequences of these major proteins, which should allow the posterior isolation of the respective genes.

Amino Acid Sequence↗
PubMed1978

[Application of hydrophobic chromatography to the fractionation of wheat prolamins].

Hydrophobic chromatography is applied to the fractionation of wheat prolamins. Proteins are separated on "Phenyl Sepharose CL 4B" column. They are eluted by variations of pH and polarity of solvent. Components with the same electrophoretic mobility appear in several chromatographic fractions and gliadin groups, as indicated by Woychick classification, are heterogeneous. This method is excepted to give new information about interaction properties of gluten proteins.

Amino Acids↗
PubMed2006

Report of three cases of chronic pancreatic fistulas treated with prolamine as a sclerosing substance following pancreatic resection.

CONTEXT: Pancreatic fistulas are one of the most common and important complications after pancreatic resection and their consequences are a life-threatening event. Thus, they must be treated in the best way and resolved as soon as possible to avoid their morbidity. METHODS: Three cases of pancreatic fistula following pancreatic resection were reported. They were treated with percutaneous embolization using a sclerosing substance, prolamine, injected into the Wirsung duct via drainage catheter. RESULTS: No complications of the technique were revealed and closure of the pancreatic fistula was obtained shortly thereafter. CONCLUSIONS: The technique is safe and simple and can be repeated several times. It allows good results without complications. Finally, it avoids additional surgery allowing a shorter recovery time and a lower risk of morbidity.

Adult↗
PubMed1990

[Alternate method for closure of oro-antral fistulas. Plastic covering of jaw opening with lyophilized Dura and alcoholic solution of Prolamin].

The operative closure of an oroantral fistula due to tooth extractions by the method of Rehrmann consists of various disadvantages, e.g. postoperative pain, swelling, flattening of the vestibulum and scar-tissue. Two alternative methods to close fresh oroantral fistulas without surgical intervention are described. By the use of prolamin occlusion gel or lyophilized dura these disadvantages can be avoided. Both techniques were successfully attempted on patients. The rate of failure is on both counts under 4%. Some indications limits must be strictly regarded. Both methods are really a good alternative to the usual operative procedure of Rehrmann and can easily be applied even on patients of great risk.

Collagen↗
PubMed1983

Experimental studies on pancreatic duct occlusion with prolamine.

The effect of the occlusion of the pancreatic duct system with prolamine (Ethibloc) has been studied in animal experiments with dogs and mini-pigs. The solution becomes solid in the duct system and becomes disintegrated again within 11 days. This time, however, is sufficient to keep a high-grade atrophy of the exocrine parenchyma. With this method one doesn't risk the provocation of an acute pancreatitis. The endocrine function of the atrophied glands is satisfactory, no animal became diabetic. The basal jugular vein insulin shows no difference to that of the control group, but nevertheless the mean whole pancreas hormone content is reduced for insulin and somatostatin, but not for glucagon.

Animals↗
PubMed1980

[Comparative investigations of partial amino acid sequences of prolamines and glutelins from cereals. II. Fractionation of glutelins (author's transl)].

Glutelins of wheat, rye, barley, oats, rice, sorghum and maize, which remain as residual proteins after extraction of defatted flours with water, salt solution and aqueous ethanol, were successively extracted with dilute acetic acid. Protein distribution and amino acid composition differ greatly with wheat, rye, barley, oats and rice and depend on the number of extraction steps and the concentration of acid used. The glutelins of sorghum and maize are only slightly soluble in acetic acid. In the case of barley glutelin fractions with very different compositions were obtained. The solubility of wheat and maize glutelins was examined in disulfide reducing and surface active agents. Wheat glutelin but not maize glutelin is soluble in HgCl2- and 2-mercaptoethanol solutions. A mixture of 2-mercaptoethanol and sodium dodecylsulfate is an excellent solvent for both glutelins.

Amino Acid Sequence↗
PubMed2003

Linkage relationships between prolamin genes located on chromosome 1Hch in Hordeum chilense.

The endosperm storage proteins of Hordeum chilense Roem. et Schult., a species used in the synthesis of the amphiploid tritordeum (x Tritordeum Ascherson et Graebner), have a great effect on the gluten strength of this amphiploid. We have analysed electrophoretically the heredity of these proteins, which are synthesised by genes located on chromosome 1H(ch), and detected up to five loci in a cross between two lines of H. chilense. These loci present a certain homology with loci synthesising the same proteins in wheat. The genetic distances between these loci were calculated.

Chromosome Mapping↗
PubMed1996

Disulphide structure of a sunflower seed albumin: conserved and variant disulphide bonds in the cereal prolamin superfamily.

Disulphide mapping of a methionine-rich 2S albumin from sunflower seeds showed four intra-chain disulphide bonds which are homologous with those in a related heterodimeric albumin from lupin seeds (conglutin delta). Similar conserved disulphide bonds are also present in alpha-gliadin and gamma-gliadin storage proteins of wheat, but a lower level of conservation is present in a further related group of proteins, the cereal inhibitors of alpha-amylase and trypsin. These differences may relate to the different functions of the proteins.

2S Albumins, Plant↗
PubMed1996

Specific depletion of the house dust mite allergen Der p 1 cereal flour prolamins.

BACKGROUND: Quantitation of Der 1 and Der 2 in dust samples by specific monoclonal antibodies is a method used increasingly to evaluate mite allergen exposure. The level of Der 1 has been proposed as a risk factor for sensitization. AIM: We report a drastic decrease in the Der 1/Der 2 ratio when dust samples are collected in bakeries. METHODS: Wheat flour and purified mites were extracted simultaneously; levels of Der p 1 and Der p 2 and cysteine protease activity were determined by ELISA and inhibition experiments. RESULTS: High titers of Der 2, but only trace amounts of Der p 1, were detected in dust collected from bakeries. Both the level and proteolytic activity of Der p 1 appeared greatly decreased when mites and wheat flour were coextracted. CONCLUSION: Group 1 protein was found to be masked by flour components, resulting in an underestimation of the mite content in bakery dust. This problem was not found for group 2 allergen.

Allergens↗
PubMed2001

Prolamin aggregation, gluten viscoelasticity, and mixing properties of transgenic wheat lines expressing 1Ax and 1Dx high molecular weight glutenin subunit transgenes.

The composition of high molecular weight (HMW) subunits of glutenin determines the gluten strength and influences the baking quality of bread wheat. Here, the effect of transgenes coding for subunits 1Ax1 and 1Dx5 was studied in two near-isogenic wheat lines differing in their HMW subunit compositions and mixing properties. The subunits encoded by the transgenes were overexpressed in the transformed lines and accounted for 50-70% of HMW subunits. Overexpression of 1Ax1 and 1Dx5 subunits modified glutenin aggregation, but glutenin properties were much more affected by expression of the 1Dx5 transgene. This resulted in increased cross-linking of glutenin polymers. In dynamic assay, the storage and loss moduli of hydrated glutens containing 1Dx5 transgene subunits were considerably enhanced, whereas expression of the 1Ax1 transgene had a limited effect. The very high strength of 1Dx5 transformed glutens resulted in abnormal mixing properties of dough. These results are discussed with regard to glutenin subunit and glutenin polymer structures.

Chemical Phenomena↗
PubMed2001

Analysis of the effects of heat treatment on gliadin immunochemical quantification using a panel of anti-prolamin antibodies.

Antigen-labeled capture enzyme-linked immunosorbent assay with four different anti-gliadin monoclonal antibodies and an anti-gliadin serum and two different sample systems (purified gliadin fractions heat-treated in soluble phase and a model of dough simulating a baking process) were employed to study the effects of heat treatment on gliadin quantification. The analysis of purified gliadins showed that there is no particularly heat stable fraction. Remarkably, omega-gliadin did not present a differential heat stability. Reactivity varied depending on the time-temperature conditions of the treatment, the antibody employed, and the fraction analyzed. Heated dough samples showed an impairment of protein extraction depending on the intensity of the treatment. Capillary electrophoresis analysis of extracts showed that each gliadin group is affected to a different extent; omega-gliadin is less modified. Immunochemical analysis of the heat-treated samples using either of the five antibodies showed a decrease in the quantified gliadin, in concordance to the loss in the extracted proteins. Among the different sources of error in gliadin immunochemical quantification, the impairment in extraction efficiency in heat-treated samples appears as a major drawback to be overcome.

Antibodies, Monoclonal↗