Articles written in Journal of Biosciences
Volume 17 Issue 2 June 1992 pp 183-192
Light, besides initiating primary photochemical processes, alters the redox state of soluble components in chloroplast. The present review attempts to cover the mechanism of reductive photoactivation of enzymes of photosynthetic carbon reduction cycle using key enzymes as examples. The reduced soluble components — ferredoxin, thioredoxin and NADPH, in turn, cause the reduction of disulphides to dithiols of chloroplastic enzymes. NADP-malate dehydrogenase is subject to activation by light through changes in NADPH/NADP. The key enzyme of C4 photosynthesis-PEP carboxylase, though cytosolic, has been shown to be activated by disulphide/sulphhydryl interconversion by reductants generated in light through chloroplast electron transport flow. Pyruvate
Volume 41 Issue 3 September 2016 pp 507-534 Review
Galectins is a family of non-classically secreted, β-galactoside-binding proteins that has recently received considerableattention in the spatio-temporal regulation of surface ‘signal lattice’ organization, membrane dynamics, cell-adhesionand disease therapeutics. Galectin-9 is a unique member of this family, with two non-homologous carbohydraterecognition domains joined by a linker peptide sequence of variable lengths, generating isoforms with distinctproperties and functions in both physiological and pathological settings, such as during development, immunereaction, neoplastic transformations and metastasis. In this review, we summarize the latest knowledge on thestructure, receptors, cellular targets, trafficking pathways and functional properties of galectin-9 and discuss howgalectin-9-mediated signalling cascades can be exploited in cancers and immunotherapies.