Circulating lectin pathway proteins do not predict short-term cardiac outcomes after myocardial infarction.

Despite improvements in treatment, coronary artery disease is still responsible for one-third of all deaths globally, due predominantly to myocardial infarction (MI) and stroke. There is an important potential in developing new strategies for treatment of patients with these conditions. Inflammation, and in particular the actions of the complement system, has emerged as part of the pathogenesis in reperfusion injury in patients with MI. To further qualify this, we examined the association between the plasma levels of lectin pathway proteins and myocardial end-points, left ventricular ejection fraction (LVEF) and infarct size in a cohort of patients with ST-elevation myocardial infarction (STEMI). A blood sample was drawn the day after percutaneous coronary intervention from 73 patients with STEMI. The primary end-points, LVEF and infarct size, were measured with magnetic resonance imaging 6-9 days after the infarct. Complement pattern-recognition molecules of the lectin pathway (mannan-binding lectin, H-ficolin, L-ficolin and M-ficolin) were analysed along with soluble membrane attack complex (sMAC) and C-reactive protein (CRP) in plasma with immunofluorometric assays <50%. CRP correlated negatively with LVEF, regression coefficient = -0·17 (P = 0·01). None of the lectin pathway proteins correlated to LVEF or infarct size, nor did soluble membrane attack complex (sMAC). There were no differences in plasma levels of these complement proteins when comparing patients with ejection fraction <50% to patients with ejection fraction <50%. Pattern-recognition molecules of the lectin pathway and sMAC do not predict short-term cardiac outcomes after MI.

Plasma levels of MASP-1, MASP-3 and MAp44 in patients with type 2 diabetes: influence of glycaemic control, body composition and polymorphisms in the MASP1 gene.

Mounting evidence indicates that adverse activation of the complement system plays a role in the development of diabetic vascular complications. Plasma levels of the complement proteins mannan-binding lectin (MBL) and its associated serine proteases (MASP-1 and MASP-2) are elevated in diabetes. We hypothesized that single nucleotide polymorphisms (SNPs) in the MASP1 gene may contribute to altered plasma levels of the belonging gene products; MASP-1, MASP-3 and mannan-binding lectin-associated protein of 44 kDa (MAp44) in patients with type 2 diabetes. To investigate this, we compared plasma levels of MASP-1, MASP-3 and MAp44 in 100 patients with type 2 diabetes and 100 sex- and age-matched controls. Ten carefully selected SNPs were analysed using TaqMan® genotyping assay. Additionally, we included a streptozotocin-induced diabetes mouse model to directly examine the effect of inducing diabetes on MASP-1 levels. MASP-1 levels were significantly higher among patients with type 2 diabetes compared with healthy controls (P = 0·017). Five SNPs (rs874603, rs72549254, rs3774275, rs67143992, rs850312) in the MASP1 gene were associated with plasma levels of MASP-1, MASP-3 and MAp44. In the diabetes mouse model, diabetic mice had significantly higher MASP-1 levels than control mice (P = 0·003). In conclusion, MASP-1 levels were higher among patients with type 2 diabetes and diabetic mice. The mechanism behind this increase remains elusive.

Substances which inhibit ice nucleation: a review.

There are a number of substances described in the published literature which inhibit ice nucleation. Certain bacterial strains, mostly found among the nonfluorescent pseudomonade species, release material into the growth medium which reduces the nucleation temperature of water droplets to below that of distilled water. Extracts from the seeds of food crops including apricot, peach and plum can reduce the nucleation temperature of water droplets and dispersions of silver iodide. Antifreeze glycoproteins can reduce the nucleation temperature of saline solutions. Antifreeze proteins can inhibit the activity of some biological ice nucleators but not others. Certain novel polymers have been shown to inhibit the nucleation activity of dispersions of silver iodide and ice-nucleating bacteria.

The effect of antifreeze proteins and poly(vinyl alcohol) on the nucleation of ice: a preliminary study.

Three substances have been tested for ice nucleation inhibition. These were an antifreeze protein AFP III from the fish Macrozoarces americanus, an antifreeze glycoprotein AFGP from the fish Dissostichus mawsoni, and an 80% hydrolysed poly(vinyl alcohol) with a molecular weight of 9 to 10 kD. A nucleation spectrometer was used to test nucleation inhibition at a range of concentrations against two types of ice nuclei: those present in tap water and a bacterial nucleator from Pseudomonas syringae. The PVA reduced the nucleation temperature of tap water and the bacterial dispersions at all the concentrations which were tested. The AFGP reduced the nucleation temperature of tap water but enhanced the nucleation activity of the bacterial nucleators. At low concentrations the AFP III reduced the nucleation temperature of both tap water and the bacterial nucleator. At high concentrations the AFP III enhanced the nucleation temperature of the bacterial nucleator and broadened the nucleation spectrum of the tap water to encompass the nucleation spread of the control. The possible mechanisms of nucleation suppression and enhancement are discussed.

The physico-chemical characterization of a boiling stable antifreeze protein from a perennial grass (Lolium perenne).

We have characterized a cold-induced, boiling stable antifreeze protein. This highly active ice recrystallization inhibition protein shows a much lower thermal hysteresis effect and displays binding behavior that is uncharacteristic of any AFP from fish or insects. Ice-binding studies show it binds to the (1 0 1 0) plane of ice and FTIR studies reveal that it has an unusual type of highly beta-sheeted secondary structure. Ice-binding studies of both glycosylated and nonglycosylated expressed forms indicate that it adsorbs to ice through the protein backbone. These results are discussed in light of the currently proposed mechanisms of AFP action.

MEASUREMENT OF TOMATO FIRMNESS WITH A UNIVERSAL TESTING MACHINE.

A technique of punch-testing tomatoes to measure the firmness of the different anatomical parts has been developed. A plunger with a 0.040 inch diameter tip tapering to a 0.020 inch diameter shaft is attached to the crosshead of an Instron Universal Testing Machine and driven into the tomato at a speed of 1 cm/min. Distinct peaks are observed on the force-displacement trace which are related to the firmness of the various parts of the structure. The method can be used to follow changes in firmness during ripening, to detect ripening abnormalities, to measure differences between varieties and to detect variations in firmness over the surface of individual tomatoes.