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1.
Nutrients ; 14(8)2022 Apr 12.
Article in English | MEDLINE | ID: mdl-35458155

ABSTRACT

Fish is considered an important part of a healthy diet, in part due to the content of long chain omega-3 fatty acids. However, both lean and fatty fish have beneficial health effects, suggesting that micronutrients and proteins may play a role. In a randomised, controlled, cross-over trial, five healthy male participants consumed 5.2 g of protein from either salmon fishmeal or whey. Blood samples were taken before and 30 and 60 min after intake. The concentration of glucose, lipids, hormones and metabolites, including 28 different amino acids and derivatives, were measured in serum or plasma. Cultured HepG2 cells were incubated with or without serum from the participants, and transcriptomic profiling was performed using RNA sequencing. The ingestion of both salmon fishmeal and whey reduced the glucose and triglyceride levels in serum. Protein intake, independent of the source, increased the concentration of 22 amino acids and derivatives in serum. Fishmeal increased the concentration of arginine, methionine, serine, glycine, cystathionine and 2-aminobutyric acid more than whey did. Incubation with postprandial serum resulted in large transcriptomic alterations in serum-fasted HepG2 cells, with the differential expression of >4500 protein coding genes. However, when comparing cells cultivated in fasting serum to postprandial serum after the ingestion of fishmeal and whey, we did not detect any differentially regulated genes, neither with respect to the protein source nor with respect to the time after the meal. The comparable nutrigenomic effects of fishmeal and whey do not change the relevance of fish by-products as an alternative food source.


Subject(s)
Liver , Whey Proteins , Animals , Humans , Male , Amino Acids , Blood Glucose/metabolism , Cross-Over Studies , Gene Expression , Glucose , Liver/metabolism , Postprandial Period , Salmon , Whey Proteins/metabolism
2.
Nutrients ; 10(12)2018 Nov 22.
Article in English | MEDLINE | ID: mdl-30469459

ABSTRACT

Hypertension is the leading risk factor for cardiovascular disease, and prevention of high blood pressure through diet and lifestyle should be a preferred approach. High intake of fish is associated with lower blood pressure, possibly mediated through the proteins since peptides with angiotensin-converting enzyme (ACE) inhibiting capacities have been identified in fish skin, backbone, and fillet. The effects of cod meals made from residual materials and fillet on blood pressure were investigated in obese Zucker fa/fa rats which spontaneously develop high blood pressure. Rats were fed diets containing water-soluble (stickwater) or water-insoluble (presscake) fractions of protein-rich meals from cod residual materials (head, gut, backbone with muscle residuals, skin, trimmings) or fillet. Rats were fed diets containing 25% of total protein from cod meal and 75% of protein from casein, or casein as the sole protein source (control group) for four weeks. Results show that a diet containing residual presscake meal with high gut content prevented blood pressure increase, and this cod residual meal also showed the strongest in vitro inhibitions of ACE and renin activities. In conclusion, a diet containing water-insoluble proteins (presscake meal) with high gut content prevented increase in blood pressure in obese Zucker fa/fa rats.


Subject(s)
Blood Pressure/drug effects , Fish Proteins, Dietary/pharmacology , Gadiformes , Hypertension/prevention & control , Peptidyl-Dipeptidase A/blood , Renin/blood , Seafood , Animals , Diet , Hypertension/blood , Male , Obesity/complications , Obesity/drug therapy , Rats, Zucker
3.
Heliyon ; 3(7): e00343, 2017 Jul.
Article in English | MEDLINE | ID: mdl-28721399

ABSTRACT

Fresh by-products of whitefish such as cod and saithe is processed to fishmeal (FM) on-board seagoing Norwegian trawlers. The aim of this study was to document the properties of whitefish FM (WFM) protein with respect to, physicochemical and bioactive properties. Analysis of the proximate composition of representative seasonal WFM batches show that the production is robust without much variance. The mean protein (61.9 ± 1.2), fat (8.9 ± 1.1%), moisture (5 ± 1.2%) and ash content (22.4 ± 0.8%), reflect the use of lean and bony raw-material. The WFM has a low content of free amino acids (0.7%) and biogenic amines (< 1000 mg/kg) that confirm the high quality and freshness of the raw material. Amino-acid analysis identified the presence of all nutritionally essential amino acids. The WFM physicochemical properties was comparable to soy-bean meal (SBM) by analysis of solubility, water-holding capacity (WHC), the emulsion stability (ES). Proteolytic degradation of the WFM was used to demonstrate the presence of bioactive peptides with inhibiting activity against angiotensin-converting enzyme (ACE) activity, in vitro. Taken together, WFM produced from fresh by-products is an excellent protein source with attributes of interest beyond the aquafeed-market.

4.
Microbiology (Reading) ; 150(Pt 8): 2689-2697, 2004 Aug.
Article in English | MEDLINE | ID: mdl-15289565

ABSTRACT

CytK is a pore-forming toxin of Bacillus cereus that has been linked to a case of necrotic enteritis. PCR products of the expected size were generated with cytK primers in 13 of 29 strains. Six strains were PCR-positive for the related gene hly-II, which encodes haemolysin II, a protein that is 37 % identical to the original CytK. Five of the strains were positive for both genes. The DNA sequences of putative cytK genes from three positive strains were determined, and the deduced amino acid sequences were 89 % identical to that of the original CytK. The authors have designated this new cytK variant cytK-2, and refer to the original cytK as cytK-1. The CytK-2 proteins from these three strains were isolated, and their identity was verified by N-terminal sequencing. blast analysis using the cytK-2 gene sequences revealed very high homology with two cytK-2 sequences in the genomes of B. cereus strains ATCC 14579 and ATCC 10987. The differences between CytK-1 and the CytK-2 proteins were clustered to certain regions of the proteins. The isolated CytK-2 proteins were haemolytic and toxic towards human intestinal Caco-2 cells and Vero cells, although their toxicity was about 20 % of that of CytK-1. Both native and recombinant CytK-2 proteins from B. cereus 1230-88 were able to form pores in planar lipid bilayers, but the majority of the channels observed were of lower conductance than those created by CytK-1. It is likely that CytK-2 toxins contribute to the enterotoxicity of several strains of B. cereus, although not all of the CytK-2 toxins may be as harmful as the CytK-1 originally isolated.


Subject(s)
Bacillus cereus/genetics , Bacterial Toxins/genetics , Cytotoxins/genetics , Genes, Bacterial , Multigene Family , Amino Acid Sequence , Animals , Bacillus cereus/pathogenicity , Bacterial Toxins/toxicity , Base Sequence , Caco-2 Cells , Chlorocebus aethiops , Cytotoxins/toxicity , DNA, Bacterial/genetics , Humans , Lipid Bilayers , Molecular Sequence Data , Polymerase Chain Reaction , Sequence Homology, Amino Acid , Vero Cells
5.
J Bacteriol ; 186(10): 3078-85, 2004 May.
Article in English | MEDLINE | ID: mdl-15126469

ABSTRACT

Streptococcus pneumoniae secretes two different peptide pheromones used for intercellular communication. These peptides, which have completely unrelated primary structures, activate two separate signal transduction pathways, ComABCDE and BlpABCSRH, which regulate natural genetic transformation and bacteriocin production, respectively. Each signal transduction pathway contains a response regulator (ComE and BlpR, respectively) that activates transcription of target genes by binding to similar, but not identical, imperfect direct repeat motifs. In general the direct repeat binding sites are specific for one or the other of the two response regulators, ensuring that competence development and bacteriocin production are regulated separately. However, in the present study we show that the rate of transcription of an operon, encoding an ABC transporter of unknown function, can be stimulated by both peptide pheromones. We also show that this cross-induction is due to a hybrid direct repeat motif that can respond to both ComE and BlpR. To our knowledge this kind of convergent gene regulation by two separate two-component regulatory systems has not been described before in bacteria.


Subject(s)
ATP-Binding Cassette Transporters/genetics , Gene Expression Regulation, Bacterial , Signal Transduction , Streptococcus pneumoniae/genetics , Amino Acid Sequence , Base Sequence , Binding Sites , Molecular Sequence Data , Operon , Promoter Regions, Genetic , Streptococcus pneumoniae/physiology , Transcription, Genetic , Transcriptional Activation , Up-Regulation
6.
J Bacteriol ; 184(13): 3426-32, 2002 Jul.
Article in English | MEDLINE | ID: mdl-12057935

ABSTRACT

Many streptococcal species belonging to the mitis and anginosus phylogenetic groups are known to be naturally competent for genetic transformation. Induction of the competent state in these bacteria is regulated by a quorum-sensing mechanism consisting of a secreted peptide pheromone encoded by comC and a two-component regulatory system encoded by comDE. Here we report that a natural isolate of a mitis group streptococcus (Atu-4) is competent for genetic transformation even though it has lost the gene encoding the competence pheromone. In contrast to other strains, induction of competence in Atu-4 is not regulated by cell density, since highly diluted cultures of this strain are still competent. Interestingly, competence in the Atu-4 strain is lost if the gene encoding the response regulator ComE is disrupted, demonstrating that this component of the quorum-sensing apparatus is still needed for competence development. These results indicate that mutations in ComD or ComE have resulted in a gain-of-function phenotype that allows competence without a competence pheromone. A highly similar strain lacking comC was isolated independently from another individual, suggesting that strains with this phenotype are able to survive in nature in competition with wild-type strains.


Subject(s)
Bacterial Proteins/genetics , Multienzyme Complexes , Streptococcus/physiology , Transformation, Bacterial , Amino Acid Sequence , Histidine Kinase , Molecular Sequence Data , Protein Kinases/genetics
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