7 results match your criteria: "National Research Council - Institute for Marine Biosciences[Affiliation]"

Enhanced killing of breast cancer cells by a d-amino acid analog of the winter flounder-derived pleurocidin NRC-03.

Exp Mol Pathol

December 2015

Department of Microbiology and Immunology, Dalhousie University, Halifax B3H 4R2, Canada; Department of Pathology, Dalhousie University, Halifax B3H 4R2, Canada; Department of Surgery, Dalhousie University, Halifax B3H 4R2, Canada. Electronic address:

Cationic antimicrobial peptides (CAPs) defend against pathogens and, in some cases, exhibit potent anticancer activities. We previously reported that the pleurocidin NRC-03 causes lysis of breast cancer and multiple myeloma cells. NRC-03 also reduces the EC50 of other cytotoxic compounds and prevents tumor growth in vivo.

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This study examined changes in Atlantic salmon Salmo salar epidermal mucus proteins following short- and long-term handling stress. Short-term stress consisted of a single removal of fish from water for 15 s with long-term stress consisting of daily removal of fish from water for 15 s over 21 days. In the long-term handling stress study, there was a high level of individual variability with respect to mucus alkaline phosphatase, cathepsin B and lysozyme activities, with no correlation to treatment group.

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Altered expression of glycolysis proteins is an important yet poorly understood characteristic of cancer. To better understand the glycolytic changes during tumorigenesis, we designed a liquid chromatography multiple reaction monitoring (LC-MRM) assay targeting the "glycolysis proteome" in MCF-7 breast cancer cells, using isotope-coded dimethylation of peptides for relative quantification. In silico, dimethyl labeled tryptic peptides [M + 2H](2+) (of length n) and their y(n-1) fragment ions were determined based on UniprotKB database sequence entries for glycolysis proteins, related branching pathways, and reference proteins.

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Changes in Atlantic salmon (Salmo salar) epidermal mucus protein composition profiles following infection with sea lice (Lepeophtheirus salmonis).

Comp Biochem Physiol Part D Genomics Proteomics

September 2009

National Research Council-Institute for Marine Biosciences, 1411 Oxford St., Halifax, Nova Scotia, Canada B3H 3Z1; Department of Biology, Dalhousie University, Halifax, 1355 Oxford St., Nova Scotia, Canada B3H 4J1.

The mucus protein profile of Atlantic salmon (Salmo salar) and changes due to infection with sea lice (Lepeophtheirus salmonis) were examined. Two-dimensional gel electrophoresis was performed on salmon skin mucus and comparisons between control and infected fish mucus were made. LC MS/MS identified intracellular proteins, calmodulin, actin, and hemopexin and plasma proteins, such as apolipoproteins, lectin, plasminogen and transferrin.

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The mucus layer on the surface of fish consists of several antimicrobial agents that provide a first line of defense against invading pathogens. To date, little is known about the antimicrobial properties of the mucus of Arctic char (Salvelinus alpinus), brook trout (S. fontinalis), koi carp (Cyprinus carpio sub sp.

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Fish epidermal mucus and its components provide the first line of defense against pathogens. Little is known about the role of epidermal mucus enzymes in the innate immune system of fish species such as Arctic char (Salvelinus alpinus), brook trout (S. fontinalis), koi carp(Cyprinus carpio), striped bass (Morone saxatilis), haddock, (Melanogrammus aeglefinus), Atlantic cod (Gadus morhua) and hagfish (Myxine glutinosa).

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The nucleotide sequences of three small (5.2-5.6 kb) plasmids from Aeromonas salmonicida subsp.

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