Publications by authors named "Tommy Hui"

Species that inhabit high-shore environments on rocky shores survive prolonged periods of emersion and thermal stress. Using two Hong Kong high-shore littorinids ( and . ) as models, we examined their behavioral repertoire to survive these variable and extreme conditions.

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Continuous release of the highly toxic triphenyltin compounds (TPT) from antifouling paints and fungicides has caused serious pollution to urbanized coastal marine environments worldwide since the 1960s. Using gas-chromatography mass-spectrometry (GC-MS), this study investigated the distribution profile of TPT in 15 types of tissues of four marine teleost fish species collected from Hong Kong waters. Concentrations of TPT in various tissues had a significant positive correlation with protein contents in the tissues (r = 0.

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Populations at the edge of their species' distribution ranges are typically living at the physiological extreme of the environmental conditions they can tolerate. As a species' response to global change is likely to be largely determined by its physiological performance, subsequent changes in environmental conditions can profoundly influence populations at range edges, resulting in range extensions or retractions. To understand the differential physiological performance among populations at their distribution range edge and center, we measured levels of mRNA for heat shock protein 70 (hsp70) as an indicator of temperature sensitivity in two high-shore littorinid snails, Echinolittorina malaccana and E.

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Osteopontin (OPN) is a pro-inflammatory protein that paradoxically protects against inflammation and bone destruction in a mouse model of endodontic infection. Here we have tested the hypothesis that this effect of OPN is mediated by effects on migration of innate immune cells to the site of infection. Using the air pouch as a model of endodontic infection in mice, we showed that neutrophil accumulation at the site of infection with a mixture of endodontic pathogens is significantly reduced in OPN-deficient mice.

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Osteopontin (OPN) is a ligand for the α4ß1 integrin, but the physiological importance of this binding is not well understood. Here, we have assessed the effect of post-translational modifications on OPN binding to the α4 integrin on cultured human leukocyte cell lines and compared OPN interaction with α4 integrin to that of VCAM and fibronectin. Jurkat cells, whose α4 integrins are inherently activated, adhered to different preparations of OPN in the presence of Mn(2+): the EC50 of adhesion was not affected by phosphorylation or glycosylation status.

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