Effect of modified atmosphere packaging on the quality of minimally processed pineapple cv.'Smooth Cayenne' fruit

The effects of modified atmosphere (MA) conditions on the quality of minimally processed pineapple slices were determined. Commercial pineapple slice packs sealed with 40 pm thick polyester film were kept at 4.5 degrees C for 14 d. The oxygen transmission rate of the film was 23 ml m(-2) day(-1) atm(-1) (at 25 degrees C, 75% RH). In-built atmospheres and the quality of the products were determined. O-2 concentrations within the packs stabilised at 2%, while CO2 concentrations increased to 70% by day 14. The high CO2 level suggested an inappropriate lidding film permeability for the product, and hence affected its quality. Three batches of pineapple slices were packed in the laboratory using lidding films with oxygen transmission rate of 75, 2790 or 5000 ml m(-2) day(-1) atm(-1) (at 23 degrees C, 0% RH). Headspace atmospheres from laboratory-packed pineapple slices suggested an optimum equilibrium modified atmosphere of ca. 2% O-2 and 15% CO2. Respiration data from the laboratory-prepared packs were pooled together and used to develop a correlation model relating respiration rates to O-2 and CO2 concentrations. The model showed a decrease in respiration rate with decreasing O-2 and increasing CO2 concentrations. Respiration rate stabilised at 2% 02 and 10% CO2. The high concentrations of CO2 observed in the commercial packs did not fit the range in the respiration model. The model could aid in selection of MA conditions for minimally processed pineapple fruit.

Interferon-induced, antiviral human MxA protein localizes to a distinct subcompartment of the smooth endoplasmic reticulum

Human MxA protein belongs to the superfamily of dynamin-like large GTPases that are involved in intracellular membrane trafficking. MxA is induced by interferons-alpha/beta (IFN-alpha/beta) and is a key component of the antiviral response against RNA viruses. Here, we show that MxA localizes to membranes that are positive for specific markers of the smooth endoplasmic reticulum, such as Syntaxin17, but is excluded from other membrane compartments. Overexpression of MxA leads to a characteristic reorganization of the associated membranes. Interestingly, Hook3, mannose-6-phosphate receptor, and Lamp-1, which normally accumulate in cis-Golgi, endosomes, and lysosomes, respectively, also colocalized with MxA, indicating that these markers were redistributed to the MxA-positive compartment. Functional assays, however, did not show any effect of MxA on endocytosis or the secretory pathway. The present results demonstrate that MxA is an IFN-induced antiviral effector protein that resembles the constitutively expressed large GTPase family members in its capacity to localize to and reorganize intracellular membranes.

A role for Rho in smooth muscle phenotypic regulation

The role of the small GTP-binding protein Rho in the process of smooth muscle cell (SMC) phenotypic modulation was investigated using cultured rabbit aortic SMCs. Both Rho transcription and Rho protein expression were high for the first 3 days of culture (contractile state cells), with expression decreasing after change to the synthetic state and peaking upon return to the contractile phenotype. Activation of Rho (indicated by translocation to the membrane) also peaked upon return to the contractile state and was low in synthetic state SMCs. Transient transfection of synthetic state rabbit SMCs with constitutively active Rho (val14rho) caused a dramatic decrease in cell size and reorganization of cytoskeletal proteins to resemble those of the contractile phenotype; alpha-actin and myosin adopted a tightly packed, highly organized arrangement, whereas vimentin localized to the immediate perinuclear region and focal adhesions were enlarged. Conversely, specific inhibition of endogenous Rho, by expression of C3 transferase, resulted in the complete loss of actin and myosin filaments without affecting the distribution of vimentin. Focal adhesions were reduced in number. Thus, Rho plays a key role in regulating SMC phenotypic expression.