scholarly journals Interactions in milk suggest a physiological role for β-lactoglobulin

2019 ◽  
Author(s):  
J.M. Crowther ◽  
M. Broadhurst ◽  
T. Laue ◽  
G.B. Jameson ◽  
A.J. Hodgkinson ◽  
...  
Keyword(s):  
Human Milk ◽  
Physiological Function ◽  
Physiological Role ◽  
Goat Milk ◽  
Sedimentation Velocity ◽  
Abundant Protein ◽  
Physiological Conditions ◽  
New Interactions ◽  
Β Lactoglobulin ◽  
Efficient Transfer

Abstractβ-Lactoglobulin is the most abundant protein in the whey fraction of ruminant milks, yet is absent in human milk. It has been studied intensively due to its impact on the processing and allergenic properties of ruminant milk products. However, the physiological function of β-lactoglobulin remains unclear. Sedimentation velocity experiments have identified new interactions between fluorescently-labelled β-lactoglobulin and other components in milk. Co-elution experiments support that these β-lactoglobulin interactions occur naturally in milk and provide evidence that the interacting partners are immunoglobulins, while further sedimentation velocity experiments confirm that an interaction occurs between these molecules. Ruminants (e.g. cows and goats) are born without circulating immunoglobulins, which they must obtain from their mothers’ milk, whilst humans obtain immunoglobulins both through milk and during gestation via the placenta. We propose that β-lactoglobulin serves to protect immunoglobulins within ruminant milk during digestion, ensuring their efficient transfer from mother to offspring.Statement of Significanceβ-Lactoglobulin is an abundant protein in the whey fraction of ruminant milks (e.g. cow and goat milk), yet it is completely absent in human milk. While this protein has been extensively studied, due to its impact on the processing and allergenic properties of milk, its physiological function remains unclear. We fluorescently labelled β-lactoglobulin to monitor its interactions with other milk components within its physiological environment, milk. Under these near physiological conditions β-lactoglobulin is capable of interacting with several classes of immunoglobulins. Immunoglobulins are susceptible to digestion, but are required to confer immunity from the mother to the offspring. We propose that β-lactoglobulin serves to protect immunoglobulins within ruminant milk during digestion, ensuring their efficient transfer from mother to offspring.

scholarly journals Vanin 1: Its Physiological Function and Role in Diseases

2019 ◽  
Vol 20 (16) ◽  
pp. 3891 ◽  
Author(s):  
Roberta Bartucci ◽  
Anna Salvati ◽  
Peter Olinga ◽  
Ykelien L. Boersma
Keyword(s):  
Energy Production ◽  
Coenzyme A ◽  
Physiological Function ◽  
Complex Function ◽  
Pantothenic Acid ◽  
Physiological Role ◽  
Complete Understanding ◽  
Major Function ◽  
Physiological Conditions

The enzyme vascular non-inflammatory molecule-1 (vanin 1) is highly expressed at gene and protein level in many organs, such as the liver, intestine, and kidney. Its major function is related to its pantetheinase activity; vanin 1 breaks down pantetheine in cysteamine and pantothenic acid, a precursor of coenzyme A. Indeed, its physiological role seems strictly related to coenzyme A metabolism, lipid metabolism, and energy production. In recent years, many studies have elucidated the role of vanin 1 under physiological conditions in relation to oxidative stress and inflammation. Vanin’s enzymatic activity was found to be of key importance in certain diseases, either for its protective effect or as a sensitizer, depending on the diseased organ. In this review, we discuss the role of vanin 1 in the liver, kidney, intestine, and lung under physiological as well as pathophysiological conditions. Thus, we provide a more complete understanding and overview of its complex function and contribution to some specific pathologies.

scholarly journals Physiological Role for Phosphatidic Acid in the Translocation of the Novel Protein Kinase C Apl II in Aplysia Neurons

2008 ◽  
Vol 28 (15) ◽  
pp. 4719-4733 ◽  
Author(s):  
Carole A. Farah ◽  
Ikue Nagakura ◽  
Daniel Weatherill ◽  
Xiaotang Fan ◽  
Wayne S. Sossin
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phosphatidic Acid ◽  
Physiological Role ◽  
C2 Domain ◽  
The Novel ◽  
Physiological Conditions ◽  
Kinase C ◽  
Neuronal Membranes ◽  
Novel Protein

ABSTRACT In Aplysia californica, the serotonin-mediated translocation of protein kinase C (PKC) Apl II to neuronal membranes is important for synaptic plasticity. The orthologue of PKC Apl II, PKCε, has been reported to require phosphatidic acid (PA) in conjunction with diacylglycerol (DAG) for translocation. We find that PKC Apl II can be synergistically translocated to membranes by the combination of DAG and PA. We identify a mutation in the C1b domain (arginine 273 to histidine; PKC Apl II-R273H) that removes the effects of exogenous PA. In Aplysia neurons, the inhibition of endogenous PA production by 1-butanol inhibited the physiological translocation of PKC Apl II by serotonin in the cell body and at the synapse but not the translocation of PKC Apl II-R273H. The translocation of PKC Apl II-R273H in the absence of PA was explained by two additional effects of this mutation: (i) the mutation removed C2 domain-mediated inhibition, and (ii) the mutation decreased the concentration of DAG required for PKC Apl II translocation. We present a model in which, under physiological conditions, PA is important to activate the novel PKC Apl II both by synergizing with DAG and removing C2 domain-mediated inhibition.

Human Breast Milk Contains Bovine lgG. Relationship to Infant Colic?

PEDIATRICS ◽  
1991 ◽  
Vol 87 (4) ◽  
pp. 439-444
Author(s):  
Patrick S. Clyne ◽  
Anthony Kulczycki
Keyword(s):  
Breast Milk ◽  
Human Milk ◽  
Milk Protein ◽  
Cow’S Milk ◽  
Human Breast Milk ◽  
Human Breast ◽  
Cow's Milk ◽  
Milk Samples ◽  
Infant Colic ◽  
Β Lactoglobulin

Previous studies have suggested that an unidentified cow's milk protein, other than β-lactoglobulin and casein, might play a pathogenetic role in infant colic. Therefore, a radioimmunoassay was used to analyze human breast milk and infant formula samples for the presence of bovine IgG. Milk samples from 88 of the 97 mothers tested contained greater than 0.1 µg/mL of bovine IgG. In a study group of 59 mothers with infants in the colic-prone 2- to 17-week age group, the 29 mothers of colicky infants had higher levels of bovine IgG in their breast milk (median 0.42 µg/mL) than the 30 mothers of noncolicky infants (median 0.32 µg/mL) (P < .02). The highest concentrations of bovine IgG observed in human milk were 8.5 and 8.2 µg/mL. Most cow's milk-based infant formulas contained 0.6 to 6.4 µg/mL of bovine IgG, a concentration comparable with levels found in many human milk samples. The results suggest that appreciable quantities of bovine IgG are commonly present in human milk, that significantly higher levels are present in milk from mothers of colicky infants, and that bovine IgG may possibly be involved in the pathogenesis of infant colic.

scholarly journals The Lipocalin Apolipoprotein D Functional Portrait: A Systematic Review

2021 ◽  
Vol 12 ◽  
Author(s):  
Diego Sanchez ◽  
Maria D. Ganfornina
Keyword(s):  
Systematic Review ◽  
Physiological Function ◽  
Physiological Role ◽  
Future Research ◽  
Lipid Management ◽  
Health And Disease ◽  
Apolipoprotein D ◽  
Extracellular Structures ◽  
Cellular Compartments

Apolipoprotein D is a chordate gene early originated in the Lipocalin protein family. Among other features, regulation of its expression in a wide variety of disease conditions in humans, as apparently unrelated as neurodegeneration or breast cancer, have called for attention on this gene. Also, its presence in different tissues, from blood to brain, and different subcellular locations, from HDL lipoparticles to the interior of lysosomes or the surface of extracellular vesicles, poses an interesting challenge in deciphering its physiological function: Is ApoD a moonlighting protein, serving different roles in different cellular compartments, tissues, or organisms? Or does it have a unique biochemical mechanism of action that accounts for such apparently diverse roles in different physiological situations? To answer these questions, we have performed a systematic review of all primary publications where ApoD properties have been investigated in chordates. We conclude that ApoD ligand binding in the Lipocalin pocket, combined with an antioxidant activity performed at the rim of the pocket are properties sufficient to explain ApoD association with different lipid-based structures, where its physiological function is better described as lipid-management than by long-range lipid-transport. Controlling the redox state of these lipid structures in particular subcellular locations or extracellular structures, ApoD is able to modulate an enormous array of apparently diverse processes in the organism, both in health and disease. The new picture emerging from these data should help to put the physiological role of ApoD in new contexts and to inspire well-focused future research.

Oxygen control of nitrogen oxide respiration, focusing on α-proteobacteria

2011 ◽  
Vol 39 (1) ◽  
pp. 179-183 ◽  
Author(s):  
James P. Shapleigh
Keyword(s):  
Nitrate Reductase ◽  
Nitrogen Oxide ◽  
Physiological Function ◽  
Physiological Role ◽  
Present Review ◽  
Oxygen Control ◽  
Anoxic Conditions ◽  
Periplasmic Nitrate Reductase

Denitrification is generally considered to occur under micro-oxic or anoxic conditions. With this in mind, the physiological function and regulation of several steps in the denitrification of model α-proteobacteria are compared in the present review. Expression of the periplasmic nitrate reductase is quite variable, with this enzyme being maximally expressed under oxic conditions in some bacteria, but under micro-oxic conditions in others. Expression of nitrite and NO reductases in most denitrifiers is more tightly controlled, with expression only occurring under micro-oxic conditions. A possible exception to this may be Roseobacter denitrificans, but the physiological role of these enzymes under oxic conditions is uncertain.

scholarly journals A physiological role for the dopamine D5 receptor as a regulator of BDNF and Akt signalling in rodent prefrontal cortex

2012 ◽  
Vol 16 (2) ◽  
pp. 477-483 ◽  
Author(s):  
Melissa L. Perreault ◽  
Jace Jones-Tabah ◽  
Brian F. O'Dowd ◽  
Susan R. George
Keyword(s):  
Prefrontal Cortex ◽  
Physiological Function ◽  
Physiological Role ◽  
Wide Distribution ◽  
D1 Receptor ◽  
Therapeutic Effects ◽  
Receptor Kinase ◽  
Bdnf Expression ◽  
Dopamine D5 Receptor ◽  
Gsk 3Β

Abstract The dopamine D5 receptor (D5R) exhibits a wide distribution in prefrontal cortex (PFC) but its role in this region has not yet been elucidated. In the present study, we identified a novel physiological function for the D5R as a regulator of brain-derived neurotrophic factor (BDNF) and Akt signalling in PFC. Specifically, acute activation of the D5R by the dopamine agonist SKF 83959 enhanced BDNF expression and signalling through its receptor, tropomyosin receptor kinase B (TrkB), in rats and in mice gene-deleted for the D1 receptor but not the D5R. These changes were concomitant with increased expression of GAD67, a protein whose down-regulation has been implicated in the aetiology of schizophrenia. Furthermore, D5R activation increased phosphorylation of Akt at the Ser473 site, consequently decreasing the activity of its substrate GSK-3β. These findings could have wide-reaching implications given evidence showing activation of these pathways in PFC has therapeutic effects in neuropsychiatric disorders such as drug addiction, schizophrenia and depression.

Measurement of N- and C-terminal-region fragments of parathyroid hormone-related peptide in milk from lactating women and investigation of the relationship of their concentrations to calcium in milk

1997 ◽  
Vol 153 (3) ◽  
pp. 445-451 ◽  
Author(s):  
H Uemura ◽  
T Yasui ◽  
N Yoneda ◽  
M Irahara ◽  
T Aono
Keyword(s):  
Parathyroid Hormone ◽  
Human Milk ◽  
Physiological Role ◽  
Terminal Region ◽  
Related Peptide ◽  
Milk Volume ◽  
Parathyroid Hormone Related Peptide ◽  
High Concentrations ◽  
Relationship Of ◽  
The Relationship

Abstract Parathyroid hormone-related peptide (PTHrP) is found in very high concentrations in the milk of various mammals. However, little is known about its physiological role in this fluid. To obtain detailed profiles of PTHrP in milk, we measured the concentrations of PTHrP in human milk by two different region-specific assays, PTHrP(1–87) (N-PTHrP) and PTHrP(109–141) (C-PTHrP). We also examined the correlations between PTHrP and Ca concentrations in milk as well as the correlations between PTHrP and secreted milk volume. The levels of N-PTHrP and C-PTHrP were relatively low after delivery and gradually increased to 13·87 ± 2·40 nmol/l (mean ± s.e.m.) and 56·39 ± 11·31 nmol/l respectively on the 10th day postpartum. N-PTHrP concentration remained steady until the 6th month postpartum when weaning starts, at which point it decreased slightly. C-PTHrP levels changed in a similar way to N-PTHrP levels but were 2- to 5-fold higher. Milk Ca concentration, and content, correlated with C-PTHrP concentration, and content (r=0·422 and r=0·769 respectively; P<0·0001) but not with N-PTHrP. N-PTHrP concentration in the milk samples on the 4th day postpartum correlated with the volume of milk secreted during the 24 h before the samples were taken (r=0·524, P<0·01), but C-PTHrP concentration did not. These results suggest that PTHrP in human milk may play some role in the maintenance of lactation through the N-terminal region and in promoting Ca transfer into milk via the C-terminal region. Journal of Endocrinology (1997) 153, 445–451

scholarly journals Glucose Regulatory Hormones in Camel, Cow, Goat, and Human Milk (P06-034-19)

2019 ◽  
Vol 3 (Supplement_1) ◽  
Author(s):  
Wafa Almohmadi ◽  
Jonathan Allen
Keyword(s):  
Glucose Metabolism ◽  
Human Milk ◽  
Human Insulin ◽  
Bovine Milk ◽  
Goat Milk ◽  
Model Systems ◽  
Camel Milk ◽  
Insulin Concentration ◽  
Diabetic Patients ◽  
Medical Food

Abstract Objectives Diabetes Mellitus is globally predicted to affect 592 million people by 2035 with the greatest rates of increase in low and middle income countries. Various plant and animal foods are being tested as alternatives to medication to control blood glucose. Regular consumption of milk from camels has had a positive anti-diabetic effect in both type 1 and type 2 diabetics. Epidemiological studies, research in diabetic rat and mouse model systems, and clinical studies in diabetic patients support the anti-diabetic effects of camel milk, but the mechanism of action is unclear. This study investigated hormones that impact glucose metabolism in humans from milks from different species and their stability with pasteurization. We tested hypotheses in the literature that camel milk antidiabetic properties are due to a high content of insulin or insulinotropic hormones. Methods Five milk samples: Human, Bovine, Goat, and Camel from two different farms were analyzed with a multiplex panel for hormones that impact glucose metabolism in humans. Immunoreactivity to human Insulin, C-peptide, Glucagon, Ghrelin, Leptin, GIP, GLP-1, Resistin, Visfatin, and PAI-1 (total) were determined with a multiplex assay (Biorad Bioplex diabetes panel) using a Magpix analyzer. Results Insulin immunoreactivity was present in both human and goat milk at approximately 200 pg/mL. Both camel samples were below the range of detection with this anti-human insulin antibody; but 5 pg/mL of insulin was detected in bovine milk. GIP was detected in all milks but was highest in human milk. Camel milk had higher immunoreactivity to resistin, visfatin, and ghrelin than goat or bovine milk. GLP-1 and leptin were only detected in human milk. Neither HTST nor Holder pasteurization significantly reduced the immunoreactivity of these hormones in milk. Conclusions Although literature suggests camel milk is an effective medical food for diabetics, we did not find high insulin concentration in camel milk. The hypoglycemic effect of camel milk might be due to other components of camel milk. Assays using different antibodies or insulin receptors might show different results. The insulin concentration in goat milk suggests that this product should be tested as a medical food for glucose control. Funding Sources NIFA; NCSU; Saudi Cultural Mission.

scholarly journals Effects of High Intensity Ultrasound on Physiochemical and Structural Properties of Goat Milk β-Lactoglobulin

Molecules ◽  
2020 ◽  
Vol 25 (16) ◽  
pp. 3637
Author(s):  
Xinhui Zhou ◽  
Cuina Wang ◽  
Xiaomeng Sun ◽  
Zixuan Zhao ◽  
Mingruo Guo
Keyword(s):  
Thermal Stability ◽  
Structural Properties ◽  
High Intensity ◽  
Structural Changes ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Goat Milk ◽  
High Intensity Ultrasound ◽  
Hydrophobicity Index ◽  
Β Lactoglobulin

This study aimed to compare the effects of high intensity ultrasound (HIU) applied at various amplitudes (20~40%) and for different durations (1~10 min) on the physiochemical and structural properties of goat milk β-lactoglobulin. No significant change was observed in the protein electrophoretic patterns by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Deconvolution and second derivative of the Fourier transform infrared spectra (FTIR) showed that the percentage of β-sheet of goat milk β-lactoglobulin was significantly decreased while those of α-helix and random coils increased after HIU treatment The surface hydrophobicity index and intrinsic fluorescence intensity of samples was enhanced and increased with increasing HIU amplitude or time. Differential scanning calorimetry (DSC) results exhibited that HIU treatments improved the thermal stability of goat milk β-lactoglobulin. Transmission electron microscopy (TEM) of samples showed that the goat milk β-lactoglobulin microstructure had changed and it contained larger aggregates when compared with the untreated goat milk β-lactoglobulin sample. Data suggested that HIU treatments resulted in secondary and tertiary structural changes of goat milk β-lactoglobulin and improved its thermal stability.

Metabolism at the pyruvate branch point in the radula retractor muscle of the whelk, Busycon contrarium

1982 ◽  
Vol 60 (11) ◽  
pp. 2973-2977 ◽  
Author(s):  
W. Ross Ellington
Keyword(s):  
Branch Point ◽  
Physiological Role ◽  
Redox Balance ◽  
Retractor Muscle ◽  
Physiological Conditions ◽  
Wet Weight ◽  
Octopine Dehydrogenase

The radula retractor muscle of the whelk Busycon contrarium contains high activities of both octopine dehydrogenase (~500 μmol∙min−1∙g wet weight−1) and strombine dehydrogenase (~150 μmol∙min−1∙g wet weight−1). Experiments were conducted with in vitro radula muscle preparations to assess under what physiological conditions these dehydrogenases function. Alanopine–strombine accumulated during anoxia, postanoxic recovery, and potassium-induced contractures in radula retractor muscles. No significant accumulation of octopine was observed. Although the accumulation of alanopine–strombine was significant, it was quantitatively small when compared with the production of succinate. Thus, it appears that alanopine–strombine formation has only an accessory role in cytoplasmic redox balance in B. contrarium radula retractor muscle. The physiological role of octopine dehydrogenase in this system remains unclear.

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