Interrelation between Lignin Deposition and Polysaccharide Matrices during the Assembly of Plant Cell Walls

Abstract: The modifications caused by genetic down-regulation of the enzyme cinnamoyl CoA reductase (CCR) from monolignol biosynthetic pathways on tobacco and Arabidopsis thaliana were investigated at the ultrastructural level. A typical result was that the same transformation led to similar abnormality in secondary wall formation of fibres in both plants. The cell wall alterations mainly consisted in an important disorganization and loosening of cellulose microfibrils in the inner part of the S₂ layer. This inability of the transformants to form a coherent cell wall coincided with a lack of synthesis of non-condensed forms of lignin in this disorganized region of the wall, as demonstrated by immunolabelling of lignin subunits. A similar disorganization was observed during fibre wall formation in the differentiating tissues of young Populus and A. thaliana plants. The transitory lack of organization of cellulose microfibrils, also coincided with a depletion in non-condensed forms of lignins. These results suggest that such lignin substructures may be involved in the cohesion of secondary walls during cell wall biogenesis. The mutual influence of the cellulose-hemicellulose environment and monolignol local polymerization is discussed.     

Comparison of aryl hydrocarbon hydroxylase and epoxide hydratase. Induction in primary fetal rat liver cell culture

The activity of aryl hydrocarbon hydroxylase (AHH) and/or epoxide hydratase (EH) is induced in primary fetal rat liver cell culture by benz[a]anthracene (BA), phenobarbital (PB), cigarette smoke condensate (CSC), 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) and trans-stilbene oxide (TSO). The response of the two enzymes to the different chemicals varies as follows: (a) AHH is induced by lower concentrations of BA, PB and CSC than those required to significantly induce EH; (b) AHH is selectively induced by TCDD and by low BA concentrations; (c) the kinetics of AHH induction by BA, PB and CSC are faster than that of EH; (d) TSO is a selective inducer of EH. As described earlier for AHH, RNA and protein synthesis and the continuous presence of the inducer are required in the early phases of EH induction. Later, when the EH activity has reached a plateau, intact RNA and protein synthesis is not necessary to maintain the enzyme at its optimal value. The removal of the inducer determines a decay of the EH activity, allowing the estimation of a biological $\text{t}{}_{\mathrm{<mtext>1</mtext><mtext>2</mtext>}}$ of about 72 h. TSO prevents the AHH induction by PB, but not that mediated by BA and CSC. Added together with PB, BA, CSC or PB plus BA, TSO induces the EH activity in a more than additive manner. This effect is only seen after 6 days of continuous treatment. These results indicate that in this tissue culture model, the mechanism of AHH and EH induction can clearly be dissociated.