Human beta casein fragment (54-59) modulates M. bovis BCG survival and basic transcription factor 3 (BTF3) expression in THP-1 cell line

Autor: Bhupendra N. Singh, Wahajul Haq, Raj Kamal Tripathi, Reshu Saxena, Vandana Singh, Seturam B. Katti, Dharamsheela Thakur
Jazyk: angličtina
Rok vydání: 2012
Předmět:
Bacterial Diseases
Lipopolysaccharides
Chemokine
Proteome
Applied Microbiology
Gene Expression
lcsh:Medicine
Apoptosis
Peptide
Toxicology
Biochemistry
Intracellular Receptors
Immunotoxicology
Drug Discovery
Molecular Cell Biology
Gene expression
Signaling in Cellular Processes
Protein Isoforms
THP1 cell line
lcsh:Science
Peptide sequence
chemistry.chemical_classification
Multidisciplinary
Cell Death
biology
Caseins
Nuclear Proteins
Mycobacterium bovis
Nuclear Signaling
Infectious Diseases
Host-Pathogen Interactions
Medicine
Cytokines
Chemokines
Research Article
Biotechnology
Signal Transduction
Genetic Toxicology
Immunology
Molecular Sequence Data
Down-Regulation
Bioengineering
Nitric Oxide
Microbiology
Cell Line
Molecular Genetics
Immune system
Genetics
Humans
Immunologic Factors
Amino Acid Sequence
Biology
Antibiotics
Antitubercular
Transcription factor
Microbial Viability
lcsh:R
Proteins
Computational Biology
Macrophage Activation
Molecular biology
Peptide Fragments
chemistry
Small Molecules
Cell culture
biology.protein
lcsh:Q
Transcription Factors
Zdroj: PLoS ONE, Vol 7, Iss 9, p e45905 (2012)
PLoS ONE
ISSN: 1932-6203
Popis: Immunostimulatory peptides potentiate the immune system of the host and are being used as a viable adjunct to established therapeutic modalities in treatment of cancer and microbial infections. Several peptides derived from milk protein have been reported to induce immunostimulatory activity. Human β -casein fragment (54-59), natural sequence peptide (NS) carrying the Val-Glu-Pro-Ile-Pro-Tyr amino acid residues, was reported to activate the macrophages and impart potent immunostimulatory activity. In present study, we found that this peptide increases the clearance of M. bovis BCG from THP-1 cell line in vitro. The key biomolecules, involved in the clearance of BCG from macrophage like, nitric oxide, pro-inflammatory cytokines and chemokines, were not found to be significantly altered after peptide treatment in comparison to the untreated control. Using proteomic approach we found that BTF3a, an isoform of the Basic Transcription Factor, BTF3, was down regulated in THP-1 cell line after peptide treatment. This was reconfirmed by real time RT-PCR and western blotting. We report the BTF3a as a novel target of this hexapeptide. Based on the earlier findings and the results from the present studies, we suggest that the down regulation of BTF3a following the peptide treatment may augment the M. bovis BCG mediated apoptosis resulting in enhanced clearance of M. bovis BCG from THP-1 cell line.
Databáze: OpenAIRE
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