Focal liver lesions in cirrhosis: value of contrast-enhanced ultrasonography compared with Doppler ultrasound and alpha-fetoprotein levels.

PURPOSE: This study aimed to evaluate the diagnostic value of contrast-enhanced ultrasound (CEUS) in characterising focal liver lesions in cirrhosis and to validate its use in lesions discovered during surveillance for hepatocellular carcinoma (HCC). MATERIALS AND METHODS: Between 2003 and 2006, 128 cirrhotic patients with focal liver lesions at baseline ultrasonography (US) were studied by power colour Doppler US (Doppler US) and CEUS. Serum alpha-fetoprotein (AFP) levels were assessed in all patients. Fine-needle biopsy or other reference modalities such as computed tomography (CT), magnetic resonance imaging (MRI) or digital subtraction angiography (DSA) were used as the gold standard. The accuracy of baseline US, Doppler US, AFP levels, combined US and AFP levels and combined US, Doppler US and CEUS in characterising focal liver lesions was assessed. Diagnostic performance was compared using the McNemar test. RESULTS: A total of 207 focal liver lesions (101 benign and 106 malignant) were identified in 128 patients. CEUS sensitivity and specificity for lesion characterisation were 96.2% and 97.0%, respectively, whereas its positive and negative predictive values were 97.1% and 96.1%. CEUS accuracy was 96.6%, higher than that of US (72.0%), Doppler US (70.0%), AFP levels (65.7%), combined US and Doppler US (70.0%) and combined US and AFP levels (90.3%). The differences between US and CEUS were statistically significant (p<0.05). CONCLUSIONS: CEUS can characterise focal liver lesions with 96.6% accuracy, a value higher than US, Doppler US, AFP levels, combined US and AFP levels and combined US and Doppler US. CEUS should therefore be used to characterise focal liver lesions detected during HCC surveillance of cirrhotic patients.

The major antenna complex of photosystem II has a xanthophyll binding site not involved in light harvesting.

We have characterized a xanthophyll binding site, called V1, in the major light harvesting complex of photosystem II, distinct from the three tightly binding sites previously described as L1, L2, and N1. Xanthophyll binding to the V1 site can be preserved upon solubilization of the chloroplast membranes with the mild detergent dodecyl-alpha-d-maltoside, while an IEF purification step completely removes the ligand. Surprisingly, spectroscopic analysis showed that when bound in this site, xanthophylls are unable to transfer absorbed light energy to chlorophyll a. Pigments bound to sites L1, L2, and N1, in contrast, readily transfer energy to chlorophyll a. This result suggests that this binding site is not directly involved in light harvesting function. When violaxanthin, which in normal conditions is the main carotenoid in this site, is depleted by the de-epoxidation in strong light, the site binds other xanthophyll species, including newly synthesized zeaxanthin, which does not induce detectable changes in the properties of the complex. It is proposed that this xanthophyll binding site represents a reservoir of readily available violaxanthin for the operation of the xanthophyll cycle in excess light conditions.

Lhc proteins and the regulation of photosynthetic light harvesting function by xanthophylls.

Photoprotection of the chloroplast is an important component of abiotic stress resistance in plants. Carotenoids have a central role in photoprotection. We review here the recent evidence, derived mainly from in vitro reconstitution of recombinant Lhc proteins with different carotenoids and from carotenoid biosynthesis mutants, for the existence of different mechanisms of photoprotection and regulation based on xanthophyll binding to Lhc proteins into multiple sites and the exchange of chromophores between different Lhc proteins during exposure of plants to high light stress and the operation of the xanthophyll cycle. The use of recombinant Lhc proteins has revealed up to four binding sites in members of Lhc families with distinct selectivity for xanthophyll species which are here hypothesised to have different functions. Site L1 is selective for lutein and is here proposed to be essential for catalysing the protection from singlet oxygen by quenching chlorophyll triplets. Site L2 and N1 are here proposed to act as allosteric sites involved in the regulation of chlorophyll singlet excited states by exchanging ligand during the operation of the xanthophyll cycle. Site V1 of the major antenna complex LHC II is here hypothesised to be a deposit for readily available substrate for violaxanthin de-epoxidase rather than a light harvesting pigment. Moreover, xanthophylls bound to Lhc proteins can be released into the lipid bilayer where they contribute to the scavenging of reactive oxygen species produced in excess light.