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Ann Smith

Publications and source records attributed to Ann Smith.

5 recordsLinked to original sources
PubMed2003

Minimising waste in the food and drink sector: using the business club approach to facilitate training and organisational development.

The aim of the East Anglian Waste Minimisation in the Food And Drink Industry Project was to develop waste minimisation capability in food and drink sector companies by providing a structured training programme and consultancy support to participating members of a business club. The business club forum provided the structure within which interactive training and development sessions were delivered. Expertise and assistance in implementing waste minimisation and waste management programmes was given to member companies at their sites. The project resulted in pound 1,800,000 per annum of identified savings with pound 1,100,000 of verified savings already achieved. Training and development contributed fundamentally to these project outcomes and achievements. The structured training package used three different approaches or methods. Teaching and workshop sessions were used to present interactive training on waste minimisation practice. These were supplemented by interactive 'report-back' sessions where the 'project champions' presented progress reports to the club on waste minimisation at their sites. An overview of the business club approach is described, together with an account of the successes and challenges of applying a structured training and development programme and the barriers to waste minimisation that were overcome. Training effectiveness was measured according to reaction, learning, application and impact.

Beverages↗
PubMed2002

Structure-function relationships in heme-proteins.

Biological systems rely on heme-proteins to carry out a number of basic functions essential for their survival. Hemes, or iron-porphyrin complexes, are the versatile and ubiquitous active centers of these proteins. In the past decade, discovery of new heme-proteins, together with functional and structural research, provided a wealth of information on these diverse and biologically important molecules. Structure determination work has shown that nature has used a variety of different scaffolds and architectures to bind heme and modulate functions such as redox properties. Structural data have also provided insights into the heme-linked protein conformational changes required in many regulatory heme-proteins. Remarkable efforts have been made towards the understanding of factors governing redox potentials. Site-directed mutagenesis studies and theoretical calculations on heme environments investigated the roles of hydrophobic and electrostatic residues, and analyzed the effect of heme solvent accessibility. This review focuses on the structure-function relationships underlying the association of heme in signaling and iron metabolism proteins. In addition, an account is given about molecular features affecting heme's redox properties; this briefly revisits previous conclusions in the light of some more recent reports.

Animals↗
PubMed2002

Membrane phospholipid reorganization differentially regulates metallothionein and heme oxygenase by heme-hemopexin.

Heme-hemopexin coordinately regulates genes encoding protective proteins including metallothionein-I (MT-I) and heme oxygenase 1 (HO-1). Hexamethylene-bisacetamide (HMBA), which induces differentiation and activates protein kinase C (PKC), synergistically augments the induction of both MT-I and MT-II mRNAs in response to heme-hemopexin, but attenuates the induction of HO-1. HMBA also augments the increase in MT mRNA in response to cobalt protoporphyrin-hemopexin, a hemopexin (HPX) receptor ligand that activates signaling cascades without tetrapyrrole uptake. Unlike the PKC-activating phorbol esters that induce MT-I and HO-1, HMBA has minimal effects on MT-I or HO-1. HMBA is an amphipathic molecule, and is shown here to interact physically with lipids in model membranes using differential scanning calorimetry (DSC). The data are consistent with a stabilization of the lipid bilayer and an HMBA-induced segregation of lipids into separate domains each relatively enriched in one of the lipids. HMBA also perturbs membrane-protein interactions, and causes a loss of PKC and G-protein subunits from plasma membranes in vitro. Taken together, these observations reveal an additional level of complexity in the regulation of protective proteins induced by HPX, and which may take place in vivo in response to natural compounds that reorganize membrane phospholipids. A model is proposed whereby a reorganization of lipids by HMBA alters signaling pathways and fusion events considered to be the etiology of the differential response of the MT-1 (and MT-II) and the HO-1 genes to HMBA and heme-HPX.

Acetamides↗