Cadaver organ procurement in Kuwait

Al-Mousawi, M; Samhan, M; Al-Mezairee, I; Razzak, Muhammad Abdel; Khawari, F

doi:10.1016/s0041-1345(99)00829-5

Cited by 3 publications

(2 citation statements)

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“…The role of cineole 1 is somewhat unclear, although it is believed to be involved in a number of functions including defense against herbivores (11,12) and pathogens (13), attracting pollinators and fruit-dispersing animals (14), and/or as an allelopathic agent (15,16). The Australian eucalypt population collectively produces and releases an estimated 500,000 tons of cineole 1 into the environment annually (17).…”

mentioning

confidence: 99%

Cytochrome P450cin (CYP176A), Isolation, Expression, and Characterization

Hawkes¹,

Adams²,

Burlingame³

et al. 2002

Journal of Biological Chemistry

113

131

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Cytochromes P450 are members of a superfamily of hemoproteins involved in the oxidative metabolism of various physiologic and xenobiotic compounds in eukaryotes and prokaryotes. Studies on bacterial P450s, particularly those involved in monoterpene oxidation, have provided an integral contribution to our understanding of these proteins, away from the problems encountered with eukaryotic forms. We report here a novel cytochrome P450 (P450 cin , CYP176A1) purified from a strain of Citrobacter braakii that is capable of using cineole 1 as its sole source of carbon and energy. This enzyme has been purified to homogeneity and the amino acid sequences of three tryptic peptides determined. By using this information, a PCR-based cloning strategy was developed that allowed the isolation of a 4-kb DNA fragment containing the cytochrome P450 cin gene (cinA). Sequencing revealed three open reading frames that were identified on the basis of sequence homology as a cytochrome P450, an NADPH-dependent flavodoxin/ferrodoxin reductase, and a flavodoxin. This arrangement suggests that P450 cin may be the first isolated P450 to use a flavodoxin as its natural redox partner. Sequencing also identified the unprecedented substitution of a highly conserved, catalytically important active site threonine with an asparagine residue. The P450 gene was subcloned and heterologously expressed in Escherichia coli at ϳ2000 nmol/liter of original culture, and purification was achieved by standard protocols. Postulating the native E. coli flavodoxin/flavodoxin reductase system might mimic the natural redox partners of P450 cin , it was expressed in E. coli in the presence of cineole 1. A product was formed in vivo that was tentatively identified by gas chromatography-mass spectrometry as 2-hydroxycineole 2. Examination of P450 cin by UV-visible spectroscopy revealed typical spectra characteristic of P450s, a high affinity for cineole 1 (K D ‫؍‬ 0.7 M), and a large spin state change of the heme iron associated with binding of cineole 1. These facts support the hypothesis that cineole 1 is the natural substrate for this enzyme and that P450 cin catalyzes the initial monooxygenation of cineole 1 biodegradation. This constitutes the first characterization of an enzyme involved in this pathway.The cytochrome P450s (P450s) 1 are a superfamily of oxidative hemoproteins (1, 2) that carry out an enormous variety of oxidative transformations. These range from simple alkene epoxidation and heteroatom oxidation all the way through oxygen insertion into unactivated C-H bonds and C-C bond cleavage (3). P450s are broadly categorized as either soluble, e.g. most bacterial P450s, or as membrane bound/microsomal monooxygenases, e.g. most eukaryotic P450s. All P450s, however, contain a prosthetic heme group that is ligated to the protein backbone by a cysteinyl sulfur coordinated to the heme iron. It is this heme-thiolate moiety that is responsible for much of the chemistry carried out by these enzymes. The typical reaction catalyzed by a P450 is given by Reaction...

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mentioning

confidence: 99%

Cytochrome P450cin (CYP176A), Isolation, Expression, and Characterization

Hawkes¹,

Adams²,

Burlingame³

et al. 2002

Journal of Biological Chemistry

113

131

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“…Several countries have had success with improved training of doctors and transplant coordinators. Kuwait and other Gulf states saw an increase in cadaveric donations after developing a protocol that placed a special emphasis on having transplant coordinators work with neurologists on brain death cases (al-Mousawi et al 1999). Spain achieved a 142 percent increase in donations since 1989 by placing transplant coordinators in intensive care units across the country.…”

Section: Organ Donation Policies and The Emergence Of Legally Bindingmentioning

confidence: 99%

Assisting Altruism: Evaluating Legally Binding Consent in Organ Donation Policy

Mesich-Brant

Grossback

2005

Journal of Health Politics, Policy and Law

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The growing need for organ and tissue transplants has led a number of states to enforce a policy that views a donor's declared intent to be an organ donor as legally binding. This allows health officials to harvest organs without the permission of the next of kin. Legally binding consent is controversial because of concerns that it may anger family members, lead to negative publicity, and discourage potential donors. We use interviews and a pooled time-series data set of cadaveric donation rates in U.S. states to evaluate the effectiveness of this policy. Our research indicates that enforcement of legally binding consent has marginally increased cadaveric donations while not significantly affecting donor registration. We also find evidence that the effect of the policy might be greater if it were more fully implemented and coordinated with efforts to improve public acceptance and awareness.

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Incentives for Providing Organs

McCarrick

Darragh²

2003

ken

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Cadaver organ procurement in Kuwait

Cited by 3 publications

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Cytochrome P450cin (CYP176A), Isolation, Expression, and Characterization

Cytochrome P450cin (CYP176A), Isolation, Expression, and Characterization

Assisting Altruism: Evaluating Legally Binding Consent in Organ Donation Policy

Incentives for Providing Organs

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