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Article ; Online: Differential impact on motility and biofilm dispersal of closely related phosphodiesterases in Pseudomonas aeruginosa.

Cai, Yu-Ming / Hutchin, Andrew / Craddock, Jack / Walsh, Martin A / Webb, Jeremy S / Tews, Ivo

2020 Volume 10, Issue 1, Page(s) 6232

Abstract: ... for this motility in biofilm dispersal. Hence P. aeruginosa is able to differentiate c-di-GMP output using ...

Abstract	In Pseudomonas aeruginosa, the transition between planktonic and biofilm lifestyles is modulated by the intracellular secondary messenger cyclic dimeric-GMP (c-di-GMP) in response to environmental conditions. Here, we used gene deletions to investigate how the environmental stimulus nitric oxide (NO) is linked to biofilm dispersal, focusing on biofilm dispersal phenotype from proteins containing putative c-di-GMP turnover and Per-Arnt-Sim (PAS) sensory domains. We document opposed physiological roles for the genes ΔrbdA and Δpa2072 that encode proteins with identical domain structure: while ΔrbdA showed elevated c-di-GMP levels, restricted motility and promoted biofilm formation, c-di-GMP levels were decreased in Δpa2072, and biofilm formation was inhibited, compared to wild type. A second pair of genes, ΔfimX and ΔdipA, were selected on the basis of predicted impaired c-di-GMP turnover function: ΔfimX showed increased, ΔdipA decreased NO induced biofilm dispersal, and the genes effected different types of motility, with reduced twitching for ΔfimX and reduced swimming for ΔdipA. For all four deletion mutants we find that NO-induced biomass reduction correlates with increased NO-driven swarming, underlining a significant role for this motility in biofilm dispersal. Hence P. aeruginosa is able to differentiate c-di-GMP output using structurally highly related proteins that can contain degenerate c-di-GMP turnover domains.
MeSH term(s)	Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biofilms/growth & development ; Cyclic GMP/metabolism ; Gene Expression Regulation, Bacterial/physiology ; Genes, Bacterial/genetics ; Nitric Oxide/metabolism ; Phosphoric Diester Hydrolases/genetics ; Phosphoric Diester Hydrolases/metabolism ; Protein Domains ; Pseudomonas aeruginosa/physiology ; Sequence Deletion
Chemical Substances	Bacterial Proteins ; Nitric Oxide (31C4KY9ESH) ; Phosphoric Diester Hydrolases (EC 3.1.4.-) ; Cyclic GMP (H2D2X058MU)
Language	English
Publishing date	2020-04-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-020-63008-5
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: H2S biogenesis by cystathionine beta-synthase: mechanism of inhibition by aminooxyacetic acid and unexpected role of serine

Petrosino, Maria / Zuhra, Karim / Kopec, Jola / Hutchin, Andrew / Szabó, Csaba / Majtan, Tomas

Cell. Mol. Life Sci.. 2022 Aug., v. 79, no. 8 p.438-438

2022

Abstract: Cystathionine beta-synthase (CBS) is a pivotal enzyme of the transsulfuration pathway responsible for diverting homocysteine to the biosynthesis of cysteine and production of hydrogen sulfide (H₂S). Aberrant upregulation of CBS and overproduction of H₂S ... ...

Abstract	Cystathionine beta-synthase (CBS) is a pivotal enzyme of the transsulfuration pathway responsible for diverting homocysteine to the biosynthesis of cysteine and production of hydrogen sulfide (H₂S). Aberrant upregulation of CBS and overproduction of H₂S contribute to pathophysiology of several diseases including cancer and Down syndrome. Therefore, pharmacological CBS inhibition has emerged as a prospective therapeutic approach. Here, we characterized binding and inhibitory mechanism of aminooxyacetic acid (AOAA), the most commonly used CBS inhibitor. We found that AOAA binds CBS tighter than its respective substrates and forms a dead-end PLP-bound intermediate featuring an oxime bond. Surprisingly, serine, but not cysteine, replaced AOAA from CBS and formed an aminoacrylate reaction intermediate, which allowed for the continuation of the catalytic cycle. Indeed, serine rescued and essentially normalized the enzymatic activity of AOAA-inhibited CBS. Cellular studies confirmed that AOAA decreased H₂S production and bioenergetics, while additional serine rescued CBS activity, H₂S production and mitochondrial function. The crystal structure of AOAA-bound human CBS showed a lack of hydrogen bonding with residues G305 and Y308, found in the serine-bound model. Thus, AOAA-inhibited CBS could be reactivated by serine. This difference may be important in a cellular environment in multiple pathophysiological conditions and may modulate the CBS-inhibitory activity of AOAA. In addition, our results demonstrate additional complexities of using AOAA as a CBS-specific inhibitor of H₂S biogenesis and point to the urgent need to develop a potent, selective and specific pharmacological CBS inhibitor.
Keywords	Down syndrome ; aminooxyacetic acid ; biogenesis ; biosynthesis ; crystal structure ; cystathionine beta-synthase ; cysteine ; energy metabolism ; enzyme activity ; homocysteine ; humans ; hydrogen ; hydrogen sulfide ; mitochondria ; models ; pathophysiology ; serine ; therapeutics
Language	English
Dates of publication	2022-08
Size	p. 438.
Publishing place	Springer International Publishing
Document type	Article ; Online
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-022-04479-9
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: An embedded lipid in the multidrug transporter LmrP suggests a mechanism for polyspecificity.

Debruycker, Vincent / Hutchin, Andrew / Masureel, Matthieu / Ficici, Emel / Martens, Chloé / Legrand, Pierre / Stein, Richard A / Mchaourab, Hassane S / Faraldo-Gómez, José D / Remaut, Han / Govaerts, Cédric

Nature structural & molecular biology

2020 Volume 27, Issue 9, Page(s) 829–835

Abstract: Multidrug efflux pumps present a challenge to the treatment of bacterial infections, making it vitally important to understand their mechanism of action. Here, we investigate the nature of substrate binding within Lactococcus lactis LmrP, a prototypical ... ...

Abstract	Multidrug efflux pumps present a challenge to the treatment of bacterial infections, making it vitally important to understand their mechanism of action. Here, we investigate the nature of substrate binding within Lactococcus lactis LmrP, a prototypical multidrug transporter of the major facilitator superfamily. We determined the crystal structure of LmrP in a ligand-bound outward-open state and observed an embedded lipid in the binding cavity of LmrP, an observation supported by native mass spectrometry analyses. Molecular dynamics simulations suggest that the anionic lipid stabilizes the observed ligand-bound structure. Mutants engineered to disrupt binding of the embedded lipid display reduced transport of some, but not all, antibiotic substrates. Our results suggest that a lipid within the binding cavity could provide a malleable hydrophobic component that allows adaptation to the presence of different substrates, helping to explain the broad specificity of this protein and possibly other multidrug transporters.
MeSH term(s)	Anti-Bacterial Agents/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Binding Sites ; Biological Transport ; Crystallography, X-Ray ; Lactococcus lactis/chemistry ; Lactococcus lactis/metabolism ; Ligands ; Membrane Transport Proteins/chemistry ; Membrane Transport Proteins/metabolism ; Molecular Dynamics Simulation ; Phosphatidylglycerols/chemistry ; Phosphatidylglycerols/metabolism ; Protein Conformation ; Substrate Specificity
Chemical Substances	Anti-Bacterial Agents ; Bacterial Proteins ; Ligands ; Membrane Transport Proteins ; Phosphatidylglycerols
Language	English
Publishing date	2020-07-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2126708-X
ISSN	1545-9985 ; 1545-9993
ISSN (online)	1545-9985
ISSN	1545-9993
DOI	10.1038/s41594-020-0464-y
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Article: Hemobilia: massive hemorrhage from the common bile duct due to a T tube.

HUTCHIN, P / SMITH, E P

American journal of surgery

2003 Volume 100, Page(s) 623–629

MeSH term(s)	Bile Duct Diseases ; Common Bile Duct ; Drainage ; Hemobilia ; Humans
Language	English
Publishing date	2003-04-21
Publishing country	United States
Document type	Journal Article
ZDB-ID	2953-1
ISSN	1879-1883 ; 0002-9610
ISSN (online)	1879-1883
ISSN	0002-9610
DOI	10.1016/0002-9610(60)90336-6
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Article ; Online: Differential impact on motility and biofilm dispersal of closely related phosphodiesterases in Pseudomonas aeruginosa

Yu-ming Cai / Andrew Hutchin / Jack Craddock / Martin A. Walsh / Jeremy S. Webb / Ivo Tews

Scientific Reports, Vol 10, Iss 1, Pp 1-

2020 Volume 12

Abstract: ... a significant role for this motility in biofilm dispersal. Hence P. aeruginosa is able to differentiate c-di-GMP ...

Abstract	Abstract In Pseudomonas aeruginosa, the transition between planktonic and biofilm lifestyles is modulated by the intracellular secondary messenger cyclic dimeric-GMP (c-di-GMP) in response to environmental conditions. Here, we used gene deletions to investigate how the environmental stimulus nitric oxide (NO) is linked to biofilm dispersal, focusing on biofilm dispersal phenotype from proteins containing putative c-di-GMP turnover and Per-Arnt-Sim (PAS) sensory domains. We document opposed physiological roles for the genes ΔrbdA and Δpa2072 that encode proteins with identical domain structure: while ΔrbdA showed elevated c-di-GMP levels, restricted motility and promoted biofilm formation, c-di-GMP levels were decreased in Δpa2072, and biofilm formation was inhibited, compared to wild type. A second pair of genes, ΔfimX and ΔdipA, were selected on the basis of predicted impaired c-di-GMP turnover function: ΔfimX showed increased, ΔdipA decreased NO induced biofilm dispersal, and the genes effected different types of motility, with reduced twitching for ΔfimX and reduced swimming for ΔdipA. For all four deletion mutants we find that NO-induced biomass reduction correlates with increased NO-driven swarming, underlining a significant role for this motility in biofilm dispersal. Hence P. aeruginosa is able to differentiate c-di-GMP output using structurally highly related proteins that can contain degenerate c-di-GMP turnover domains.
Keywords	Medicine ; R ; Science ; Q
Subject code	572
Language	English
Publishing date	2020-04-01T00:00:00Z
Publisher	Nature Publishing Group
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: SURGICAL THERAPY OF OMPHALOCELE AND GASTROSCHISIS.

HUTCHIN, P / GOLDENBERG, I S

Archives of surgery (Chicago, Ill. : 1960)

2003 Volume 90, Page(s) 22–28

MeSH term(s)	Abdominal Wall ; Congenital Abnormalities ; Gastrointestinal Diseases ; Gastroschisis ; Heart Defects, Congenital ; Hernia, Umbilical ; Hernia, Ventral ; Humans ; Infant ; Infant, Newborn ; Infant, Newborn, Diseases ; Mortality ; Pathology ; Prognosis ; Surgical Procedures, Operative ; Urologic Diseases
Language	English
Publishing date	2003-05-03
Publishing country	United States
Document type	Journal Article
ZDB-ID	80055-7
ISSN	1538-3644 ; 0004-0010 ; 0096-6908 ; 0272-5533
ISSN (online)	1538-3644
ISSN	0004-0010 ; 0096-6908 ; 0272-5533
DOI	10.1001/archsurg.1965.01320070024005
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Article: Environmental conservation and the risk industry

Hutchin, James W

The Geneva papers on risk and insurance - issues and practice : a quarterly journal on risk, uncertainty and insurance economics Vol. 27, No. 2 , p. 246-254

a natural alignment of interests

2002 Volume 27, Issue 2, Page(s) 246–254

Author's details	by James W. Hutchin
Keywords	Umweltschutz ; Risikomodell ; Versicherung
Language	English
Size	graph. Darst
Publisher	Palgrave Macmillan
Publishing place	Basingstoke
Document type	Article
ZDB-ID	196109-3
Database	ECONomics Information System

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Article ; Online: Non-specific interference in the measurement of plasma ammonia: importance of using a sample blank.

Herrera, Daniel Juan / Hutchin, Tim / Fullerton, Donna / Gray, George

Annals of clinical biochemistry

2010 Volume 47, Issue Pt 1, Page(s) 81–83

Abstract: ... of NAD(P)H to NAD(P)(+) by a spectrophotometric technique are the most common methods to measure plasma ... to interference by substances in plasma able to oxidize NAD(P)H at a substantial rate, thereby providing falsely ...

Abstract	Background: Enzymatic assays using glutamate dehydrogenase (GLDH) to monitor the transformation of NAD(P)H to NAD(P)(+) by a spectrophotometric technique are the most common methods to measure plasma ammonia (PA) in routine laboratories worldwide. However, these assays can potentially be subject to interference by substances in plasma able to oxidize NAD(P)H at a substantial rate, thereby providing falsely high results. Methods: To study this potential interference, we spiked a plasma pool with a liver homogenate and measured the ammonia concentration using a dry chemistry system (Vitros 250, Ortho Clinical Diagnostic, Raritan, NJ, USA), an enzymatic assay without a sample blanking step (Infinity Ammonia Liquid Stable Reagent, Thermo Fisher Scientific, Waltham, USA) and an enzymatic assay that corrects for the non-specific oxidation of NADPH (Ammonia kit, RANDOX Laboratories Ltd, Crumlin, UK). Results: This experiment shows that the Infinity ammonia reagent kit is subject to a clinically significant interference and explains the discrepancies previously reported between these methods in patients with acute liver failure (ALF). Conclusion: When using enzymatic methods for the assessment of PA, we recommend including a sample blanking correction and this should be mandatory when monitoring patients with ALF.
MeSH term(s)	Ammonia/analysis ; Ammonia/blood ; Ammonia/metabolism ; Artifacts ; Enzyme Assays/methods ; Enzyme Assays/standards ; Glutamate Dehydrogenase (NADP+)/metabolism ; Humans ; Liver/chemistry ; Liver/metabolism ; Liver Failure, Acute/blood ; Liver Failure, Acute/diagnosis ; Liver Failure, Acute/metabolism ; Osmolar Concentration ; Quality Control ; Reference Standards ; Substrate Specificity
Chemical Substances	Ammonia (7664-41-7) ; Glutamate Dehydrogenase (NADP+) (EC 1.4.1.4)
Language	English
Publishing date	2010-01
Publishing country	England
Document type	Evaluation Studies ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	390309-6
ISSN	1758-1001 ; 0004-5632
ISSN (online)	1758-1001
ISSN	0004-5632
DOI	10.1258/acb.2009.009145
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Article: Mitochondrial defects and hearing loss.

Hutchin, T P / Cortopassi, G A

Cellular and molecular life sciences : CMLS

2000 Volume 57, Issue 13-14, Page(s) 1927–1937

Abstract: The techniques of human molecular genetics have been rapidly applied to the study of hearing loss. These studies have implicated more than 60 loci as causes of nonsyndromic hearing loss. Mutations at more than a dozen nuclear genes have been demonstrated ...

Abstract	The techniques of human molecular genetics have been rapidly applied to the study of hearing loss. These studies have implicated more than 60 loci as causes of nonsyndromic hearing loss. Mutations at more than a dozen nuclear genes have been demonstrated to cause hearing loss, and these have been covered in recent reviews. However, a perhaps unexpected feature of the molecular characterization of human hearing loss has been the occurrence of mutations in the mitochondrial DNA (mtDNA). The importance of mitochondrial function in hearing is emphasized by the recent discovery of mutations in a nuclear-encoded mitochondrial protein which results in hearing loss. This article reviews the current status of our knowledge of mtDNA mutations that have been shown to cause hearing loss, and the suggestion of potential molecular, cellular and tissue-specific pathophysiological mechanisms by which dysfunction of mitochondria may lead to a loss of hearing.
MeSH term(s)	Aminoglycosides/toxicity ; Cell Nucleus/genetics ; Cochlea/metabolism ; Cochlea/pathology ; DNA, Mitochondrial/genetics ; Deafness/genetics ; Deafness/pathology ; Deafness/therapy ; Genetic Counseling ; Humans ; Mitochondrial Myopathies/genetics ; Mitochondrial Myopathies/pathology ; Mitochondrial Myopathies/therapy ; Models, Biological ; Mutation ; RNA, Ribosomal/genetics ; RNA, Transfer, Leu/genetics ; RNA, Transfer, Ser/genetics ; Syndrome
Chemical Substances	Aminoglycosides ; DNA, Mitochondrial ; RNA, Ribosomal ; RNA, Transfer, Leu ; RNA, Transfer, Ser ; RNA, ribosomal, 12S
Language	English
Publishing date	2000-12
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/PL00000673
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Article: The insurance industry must champion sustainability

Shea, Matthew I / Hutchin, James W

Thunderbird international business review Vol. 55, No. 6 , p. 659-672

2013 Volume 55, Issue 6, Page(s) 659–672

Author's details	by Matthew I. Shea; James W. Hutchin
Language	English
Size	graph. Darst.
Publisher	Wiley
Publishing place	New York, NY
Document type	Article
ZDB-ID	1411657-1 ; 2070466-5
ISSN	1520-6874 ; 1096-4762
ISSN (online)	1520-6874
ISSN	1096-4762
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