Disease relevance of LOC396596

• However, NK1 but not NK3 receptor antagonists abolish both the hypermastocytosis induced by food allergy and the hypersecretion induced by antigenic challenge, suggesting different roles for NK1 and NK3 receptors in the mechanisms of sensitisation to beta-lactoglobulin [1].
• Milk sensitization was assessed by passive cutaneous anaphylaxis (PCA) against beta-lactoglobulin and by intestinal anaphylaxis measured in Ussing chambers by the increase in short circuit-current after addition of beta-lactoglobulin (deltaIsc(betaLg)) [2].
• BACKGROUND: The respective effect of milk and fermented milks on intestinal barrier capacity and on sensitization to beta-lactoglobulin was studied using a guinea pig model of cow's milk allergy [3].
• Immediate hypersensitivity reaction to beta-lactoglobulin in the epithelium lining the colon of guinea pigs fed cows' milk [4].

High impact information on LOC396596

• Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC [5].
• Intestinal permeability was evaluated from 51Cr-ethylenediaminetetraacetic acid (EDTA) recovery and beta-lactoglobulin serum level [6].
• When beta-lactoglobulin A, melittin, serum albumin, myoglobin, and a protein inhibiting lipase from soybean were preincubated with a dicaprin film at a surface pressure of 35 dynes/cm, no activity was detected with horse pancreatic or Rhizopus delemar lipases [7].
• We also studied the abilities of these different mutant receptors to respond to hormonal stimulation after transfection of each mutant complementary DNA into CHO-K1 cells along with a chimeric gene containing the promoter of a milk protein gene (beta-lactoglobulin) fused to chloramphenicol acetyltransferase coding sequence [8].
• This suggests that the regulation of the beta-lactoglobulin gene is distinct from that of beta-casein and WAP [9].

Biological context of LOC396596

• Comicroinjection of the genomic beta-lactoglobulin gene with rMAb light- and heavy-chain genes led to the generation of transgenic mice carrying the three transgenes [10].
• In this study, using radiolabeled lipases, serum albumin, and beta-lactoglobulin A, we investigated their respective binding with respect to lipolysis of dicaprin monolayers [11].
• Application of beta-lactoglobulin to sensitized preparations depolarized the membrane potential and increased neuronal excitability in small intestinal neurons but not in gastric neurons [12].
• Dimerization, stability and electrostatic properties of porcine beta-lactoglobulin [13].
• Fluorescence energy transfer measurements have been made for the complex of BLG with retinol and/or heme-CO [14].

Anatomical context of LOC396596

• Electrophysiological methods were used to investigate electrical and synaptic behavior of neurons in the stomach and small intestine during exposure to beta-lactoglobulin in guinea pigs sensitized to cow's milk [12].
• RESULTS: Application of 5-10 microM beta-lactoglobulin increased lymphatic vessel constriction frequency and decreased constriction amplitude (n = 12) [15].
• The biological function of BLG is not clear, but a potential role in carrying fatty acids through the digestive tract has been proposed [16].
• METHODS: Lymphatic vessel contractile activity was assessed in vitro by video microscopy of the mesentery of cow's milk-sensitized guinea pigs upon application of beta-lactoglobulin and compared to the response measured in sham animals [15].
• In presuckled colostrum, high levels of TIC, SCTI, albumin and beta-lactoglobulin were found, while the serum-type inhibitors appeared in amounts related to their molecular weights ranging from 3-6% of the adult serum levels for the macroglobulins to 42% for alpha 1-protease inhibitor [17].

Associations of LOC396596 with chemical compounds

• The role of serum retinol-binding protein in vitamin A transport in the circulation suggests that the other two homologous proteins may function in the binding and transport of retinoids; beta-lactoglobulin may facilitate the absorption of vitamin A from milk and protein HC may mediate the excretion of retinol-derived metabolites [5].
• Adding either a lipid emulsion or pure human pancreatic lipase (HPL) or human serum albumin or beta-lactoglobulin had no effect on the flux of transfer of orlistat [18].
• Polyethylene glycol was found to be more potent in precipitating this complex than dextrans, polyvinylpyrrolidones, ficoll, and beta-lactoglobulin [19].
• Heme-CO does not bind to the predominantly alpha-helix conformation of BLG, which occurs in solutions with more than 40% ethanol or methanol [14].
• The mean proportion of alpha-lactalbumin (LA) from caprine wheys from the manufacture of Chevre and Cheddar-type cheeses was higher than values previously reported for bovine whey from Cheddar cheese; proportions of serum albumin, immunoglobulin (Ig)G, and beta-lactoglobulin (LG) were lower [20].

Other interactions of LOC396596

• An indirect double-antibody enzyme-linked immunosorbent assay (ELISA) was developed for the measurement of human immunoglobulin E (IgE) and IgG to the cow's milk proteins (CMP) alpha-casein, alpha-lactalbumin, and beta-lactoglobulin [21].
• Known cholesterol uptake inhibitors at the micelle (green tea catechins) and at the Caco-2 cell (beta-lactoglobulin-derived peptide, IIAEK) were used as reference inhibitory compounds [22].
• By contrast, no specific hormonal requirements were established for accumulation of beta-lactoglobulin, which appeared to increase in vitro if tissue remained viable in various combinations of insulin, corticosterone and prolactin [23].

Analytical, diagnostic and therapeutic context of LOC396596

• We report here a physico-chemical characterization of porcine beta-lactoglobulin, purified from pooled milk: size-exclusion chromatography, CD and NMR measurements were used to study the aggregation and stability of this protein [13].
• Thermal denaturation of porcine BLG was studied by high-sensitivity differential scanning calorimetry within the pH range 2.0-10 [24].
• The total accumulation in tissue and culture medium of the whey proteins alpha-lactalbumin and beta-lactoglobulin has been measured using specific radioimmunoassays [23].
• The cDNA for bubaline beta-lactoglobulin (beta lg) has been cloned through RT-PCR approach and sequenced [25].
• Microelectrodes were used to record electrical and synaptic behavior in neurons from milk-sensitized and nonsensitized age-matched animals during exposure to beta-lactoglobulin [26].

References