The influence of flavonoid compounds on the in vitro inhibition study of a human fibroblast collagenase catalytic domain expressed in E. coli

2013 ◽  
Vol 52 (1) ◽  
pp. 26-31 ◽  
Author(s):  
Thi Thanh Hanh Nguyen ◽  
Young-Hwan Moon ◽  
Young-Bae Ryu ◽  
Young-Min Kim ◽  
Seung-Hee Nam ◽  
...  
Keyword(s):  
Human Fibroblast ◽  
Catalytic Domain ◽  
Inhibition Study ◽  
E Coli ◽  
Flavonoid Compounds ◽  
Fibroblast Collagenase ◽  
In Vitro Inhibition

scholarly journals Fibroblast and neutrophil collagenases cleave at two sites in the cartilage aggrecan interglobular domain

1993 ◽  
Vol 295 (1) ◽  
pp. 273-276 ◽  
Author(s):  
A J Fosang ◽  
K Last ◽  
V Knäuper ◽  
P J Neame ◽  
G Murphy ◽  
...  
Keyword(s):  
Human Fibroblast ◽  
Catalytic Domain ◽  
Polymorphonuclear Leucocyte ◽  
Gelatinase A ◽  
Cleavage Sites ◽  
Similar Extent ◽  
Human Sequence ◽  
Fibroblast Collagenase ◽  
Gelatinases A And B

The actions of recombinant human fibroblast collagenase (MMP1), purified polymorphonuclear leucocyte collagenase (MMP8) and their N-terminal catalytic domain fragments against cartilage aggrecan and an aggrecan G1-G2 fragment have been investigated in vitro. After activation with recombinant human stromelysin and typsin, both collagenases were able to degrade human and porcine aggrecans to a similar extent. An N-terminal G1-G2 fragment (150 kDa) was used to identify specific cleavage sites occurring within the proteinase-sensitive interglobular domain between G1 and G2. Two specific sites were found; one at an Asn341-Phe342 bond and another at Asp441-Leu442 (human sequence). This specificity of the collagenases for aggrecan G1-G2 was identical with that of the truncated metalloproteinase matrilysin (MMP7), but different from those of stromelysin (MMP3) and the gelatinases (MMP2 or gelatinase A; MMP9 or gelatinase B) which cleave at the Asn-Phe site, but not the Asp-Leu site. In addition, collagenase catalytic fragments lacking C-terminal hemopexin-like domains were tested and shown to exhibit the same specificities for the G1-G2 fragment as the full-length enzymes. Thus the specificity of the collagenases for cartilage aggrecan was not influenced by the presence or absence of the C-terminal domain. Together with our previous findings, the results show that stromelysin-1, matrilysin, gelatinases A and B and fibroblast and neutrophil collagenases cleave at a common, preferred site in the aggrecan interglobular domain, and additionally that both fibroblast and neutrophil collagenases cleave at a second site in the interglobular domain that is not available to stromelysin or gelatinases.

In Vitro Inhibition of the Growth of Salmonella typhimurium and Escherichia coli 0157:H7 by Bacteria Isolated from the Cecal Contents of Adult Chickens

1991 ◽  
Vol 54 (7) ◽  
pp. 496-501 ◽  
Author(s):  
ARTHUR HINTON ◽  
GEORGE E. SPATES ◽  
DONALD E. CORRIER ◽  
MICHAEL E. HUME ◽  
JOHN R. DELOACH ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Lactic Acid ◽  
Salmonella Typhimurium ◽  
Mixed Cultures ◽  
Enterococcus Durans ◽  
E Coli ◽  
Pure Cultures ◽  
In Vitro Inhibition ◽  
Lactic Acids

A Veillonella species and Enterococcus durans were isolated from the cecal contents of adult broilers. Mixed cultures of Veillonella and E. durans inhibited the growth of Salmonella typhimurium and Escherichia coli 0157:H7 on media containing 2.5% lactose (w/v). The growth of S. typhimurium or E. coli 0157:H7 was not inhibited by mixed cultures containing Veillonella and E. durans on media containing only 0.25% lactose or by pure cultures of Veillonella or E. durans on media containing either 0.25% or 2.5% lactose. The mixed cultures of Veillonella and E. durans produced significantly (P<0.05) more acetic, propionic, and lactic acids in media containing 2.5% lactose than in media containing 0.25% lactose. The inhibition of the enteropathogens was related to the production of lactic acid from lactose by the E. durans and the production of acetic and propionic acids from lactic acid by the Veillonella.

scholarly journals Cytometric measurement of in vitro inhibition of Plasmodium falciparum field isolates by drugs: a new approach for re-invasion inhibition study

2014 ◽  
Vol 13 (1) ◽  
pp. 110 ◽  
Author(s):  
Marie Varela ◽  
Romy Razakandrainibe ◽  
Delphine Aldebert ◽  
Jean Barale ◽  
Ronan Jambou
Keyword(s):  
Plasmodium Falciparum ◽  
Inhibition Study ◽  
New Approach ◽  
Field Isolates ◽  
In Vitro Inhibition ◽  
Invasion Inhibition

scholarly journals Characterization of the Phe-81 and Val-82 Human Fibroblast Collagenase Catalytic Domain Purified fromEscherichia coli

1995 ◽  
Vol 270 (38) ◽  
pp. 22507-22513 ◽  
Author(s):  
Michael R. Gehring ◽  
Brad Condon ◽  
Stephen A. Margosiak ◽  
Chen-Chen Kan
Keyword(s):  
Human Fibroblast ◽  
Catalytic Domain ◽  
Fromescherichia Coli ◽  
Fibroblast Collagenase

Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor

1994 ◽  
Vol 1 (2) ◽  
pp. 106-110 ◽  
Author(s):  
N. Borkakoti ◽  
F.K. Winkler ◽  
D.H. Williams ◽  
A. D'Arcy ◽  
M.J. Broadhurst ◽  
...  
Keyword(s):  
Human Fibroblast ◽  
Catalytic Domain ◽  
Fibroblast Collagenase

scholarly journals In vitro inhibition of H. pylori in a preferential manner using bioengineered L. lactis releasing guided Antimicrobial peptides

2021 ◽  
Author(s):  
Ankan Choudhury ◽  
Patrick Ortiz ◽  
Christopher Michel Kearney
Keyword(s):  
Microbial Community ◽  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Targeted Therapies ◽  
Microbial Ecosystem ◽  
Knock Out ◽  
E Coli ◽  
In Vitro Inhibition ◽  
H Pylori

Objectives: Targeted therapies seek to selectively eliminate a pathogen without disrupting the resident microbial community. This is even more important when a pathogen like H. pylori resides in stomach, a sensitive microbial ecosystem. Using a probiotic like Lactococcus lactis and bioengineering it to release a guided Antimicrobial Peptide (AMP) targeted towards the pathogen offers a pathway to specifically knock-out the deleterious species and not disturbing the stomach microbiome. Results: Three AMPs, Alyteserin, CRAMP and Laterosporulin, were genetically fused to a guiding peptide MM1, which selectively binds to Vacuolating Toxin A (VacA) of H. pylori and cloned into an excretory vector pTKR inside L. lactis. When cultured together in vitro, the L. lactis bioengineered with guided AMPs selectively killed H. pylori when compared to E. coli or Lactobacillus plantarum, as determined by qPCR. Chemically synthesized Alyteserin and MM1-Alyteserin showed similar preferential inhibition of H. pylori when compared against E. coli, with the MIC of MM1-Alyteserin becoming significantly higher for E. coli than Alytserin whereas no such effet was observed against H. pylori. Conclusions: Probiotics bioengineered to excrete guided AMPs can be a novel and useful approach for combating pathogens without endangering the natural microbial flora. Given the wealth of AMPs and guiding ligands, both natural and synthetic, this approach can be adapted to develop a diverse array of chimeric guided AMPs and can be cloned into probiotics to create a safe and effective alternative to conventional chemical antibiotics.

scholarly journals Quaternary structure and biochemical properties of mycobacterial RNase E/G

2007 ◽  
Vol 403 (1) ◽  
pp. 207-215 ◽  
Author(s):  
Mirijam-Elisabeth Zeller ◽  
Agnes Csanadi ◽  
Andras Miczak ◽  
Thierry Rose ◽  
Thierry Bizebard ◽  
...  
Keyword(s):  
Quaternary Structure ◽  
Catalytic Domain ◽  
Biochemical Properties ◽  
Cleavage Sites ◽  
Rrna Processing ◽  
Rnase E ◽  
Human Pathogens ◽  
E Coli ◽  
Gram Positive Bacteria

The RNase E/G family of endoribonucleases plays the central role in numerous post-transcriptional mechanisms in Escherichia coli and, presumably, in other bacteria, including human pathogens. To learn more about specific properties of RNase E/G homologues from pathogenic Gram-positive bacteria, a polypeptide comprising the catalytic domain of Mycobacterium tuberculosis RNase E/G (MycRne) was purified and characterized in vitro. In the present study, we show that affinity-purified MycRne has a propensity to form dimers and tetramers in solution and possesses an endoribonucleolytic activity, which is dependent on the 5′-phosphorylation status of RNA. Our data also indicate that the cleavage specificities of the M. tuberculosis RNase E/G homologue and its E. coli counterpart are only moderately overlapping, and reveal a number of sequence determinants within MycRne cleavage sites that differentially affect the efficiency of cleavage. Finally, we demonstrate that, similar to E. coli RNase E, MycRne is able to cleave in an intercistronic region of the putative 9S precursor of 5S rRNA, thus suggesting a common function for RNase E/G homologues in rRNA processing.

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