• Birth defects and anti–heat shock protein 70 antibodies in early pregnancy

      Child, David F.; Hudson, Peter R.; Hunter-Lavin, Claire; Mukhergee, Sagarika; China, Susnata; Williams, Clive P.; Williams, John H. H.; University of Chester (Hunter-Lavin & Williams) (Springer-Verlag, 2006-03)
    • Folate supplementation reduces serum Hsp70 levels in patients with type 2 diabetes

      Hunter-Lavin, Claire; Hudson, Peter R.; Mukhergee, Sagarika; Davies, Gareth K.; Williams, Clive P.; Harvey, John N.; Child, David F.; Williams, John H. H.; University College Chester ; Wrexham Maelor Hospital, North East Wales NHS Trust ; Wrexham Maelor Hospital, North East Wales NHS Trust ; Wrexham Maelor Hospital, North East Wales NHS Trust ; Wrexham Maelor Hospital, North East Wales NHS Trust ; Wrexham Maelor Hospital, North East Wales NHS Trust ; Wrexham Maelor Hospital, North East Wales NHS Trust ; University College Chester (Cell Stress Society International, 2004-10)
      Type 2 diabetes patients are subject to oxidative stress as a result of hyperglycemia. The aim of this study was to determine whether administration of the antioxidant folic acid, previously shown to reduce homocysteine levels, would reduce circulating levels of Hsp70 while improving the condition of type 2 diabetes patients with microalbuminuria. Plasma homocysteine fell from pretreatment values of 12.9 to 10.3 μM (P < 0.0001). The urine albumin-creatinine ratio fell from 12.4 to 10.4 mg/mM (P = 0.38). Pretreatment Hsp70 levels were higher in patients not taking insulin (5.32 ng/mL) compared with those on insulin (2.44 ng/mL) (P = 0.012). Folic acid supplementation resulted in a significant fall in Hsp70 (5.32 to 2.05 ng/mL) (P = 0.004). There was no change in Hsp70 in those receiving insulin. Folic acid supplementation in non–insulin-treated type 2 diabetes patients, therefore, resulted in a fall in Hsp70, reflecting an improvement in oxidative stress. The data shows that improvement in homocysteine status can lead to a reduction in Hsp70, indicating the possibility of its use as a marker for severity of disease.
    • Hsp70 release from peripheral blood mononuclear cells

      Hunter-Lavin, Claire; Davies, Emma L.; Bacelar, Maria M. F. V. G.; Marshall, Michael J.; Andrew, Sarah M.; Williams, John H. H.; University of Chester ; University of Chester ; University of Chester ; The Robert Jones and Agnes Hunt Orthopaedic Hospital, Oswestry ; University College Chester ; University College Chester (Elsevier, 2004-11-12)
      There are an increasing number of studies reporting the presence of Hsps in human serum. We have investigated the release of Hsp70 into blood and culture medium from peripheral blood mononuclear cells (PBMCs), and whether this release is due to cell damage or active secretion from the cells. Intact Hsp70 was released from cells within whole blood and from purified PBMCs under normal culture conditions. Hsp70 release was rapid (0.1 ng/106 cells/h) over the first 2 h of culture and continued at a reduced rate up to 24 h (<0.025 ng/106 cells/h). Using viable cell counts and lactate dehydrogenase release we were able to confirm that the release of Hsp70 was not due to cellular damage. Hsp70 release was inhibited by monensin, methyl-β-cyclodextrin, and methylamine, but not by brefeldin A. These data suggest that Hsp70 is released from cells via a non-classical pathway, possibly involving lysosomal lipid rafts.
    • Measuring the secretion of heat shock proteins from cells

      Ireland, H. Elyse; Leoni, Francesca; Altaie, Ala; Birch, Catherine S.; Coleman, Robert C.; Hunter-Lavin, Claire; Williams, John H. H.; University of Chester (Elsevier, 2007-10-03)
      This article outlines procedures, using Hsp70 as the example, to: ensure the status of cells (viable, apoptotic or necrotic); identify the heat shock protein secreted; and quantify the secreted protein. Hsp70 has previously been quantified by ELISA, but newer methods are now being adopted, such as BIAcore and bead-based assays for use by FACS. These methods have the advantages of being more sensitive and requiring less sample than ELISA. The BIAcore has the potential to analyse Hsp70 ligands and provide affinity constants.
    • Preliminary study of heat shock protein 70 gene expression and serum levels in newly diagnosed type 1 and type 2 diabetes

      Hunter-Lavin, Claire; Stanaway, Stephen; Bowen-Jones, David; Jones, I. R.; Loenard, M.; Clooney, K.; Williams, John H. H.; University College Chester (Hunter-Lavin) (Williams) (American Diabetes Association, 2004)