Chromosomal location of α-amylase structural genes in rye (Secale cereale L.)

Summary Rye (Secale cereale L.) -amylase isozymes are controlled by at least four loci located on the 5R (three) and 7R (one) chromosomes. In the case of Imperial and King II cultivars, two of the three 5R chromosome loci could be specifically located on the 5Rl chromosome arm; the other one was located on the 5RS. The locus of 7R chromosome was located on the 7RL chromosome arm of Imperial rye.     

Production ofβ-ergokryptine by a strain ofClaviceps purpurea (Fr.) tul. in submerged culture

Summary A strain ofClaviceps purpurea, labelled 231 F.I., produced in submerged culture 1200 /ml of a mixture of peptidic alkaloids composed for 30% by -ergokryptine. Cultural media, conditions of culture and development features of a typic fermentation are reported.     

In vitro dopaminergic neuroprotective and in vivo antiparkinsonian-like effects of Δ3,2-hydroxybakuchiol isolated from Psoralea corylifolia (L.)

Cocktail recipes containing Psoralea corylifolia seeds (PCS) are used to empirically treat Parkinson disease. A PCS isolate Δ³,2-hydroxybakuchiol (BU) can inhibit dopamine uptake in dopamine transporter (DAT) transfected Chinese hamster ovary (CHO) cells, and dopamine reuptake blockade may provide an alternative approach for ameliorating parkinsonism. Here, we assessed the potential dopaminergic neuroprotective, and antiparkinsonian-like activity of BU. BU sample size was increased by using a scale-up extraction paradigm. Pharmacologically, BU significantly protected SK-N-SH cells from 1-methyl-4-phenylpyridinium (MPP⁺) insult, produced striking inhibitory actions on dopamine/norepinephrine uptake and WIN35,428 binding in synaptosomes on in vivo administration, and significantly preventing poor performance on rotarod and dopaminergic loss in substantia nigra in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) mice. BU acts by protecting dopaminergic neurons from MPP⁺ injury and preventing against MPTP-induced behavioral and histological lesions in the Parkinson’s disease (PD) model, possibly by inhibiting monoamine transporters. These findings suggest that BU could be meaningful in PD treatment. Received 14 January 2009; received after revision 22 February 2009; accepted 10 March 2009     

Is β-(4-chlorophenyl)-GABA a specific antagonist of substance P on cerebral cortical neurons?

Summary -(4-chlorophenyl)-GABA (Baclofen, Lioresal antagonized the excitant actions of acetylcholine and substance P to comparable extents.L-glutamate-induced excitation was affected to a lesser extent These findings do not support the suggestion that -(4-chlorophenyl)-GABA is a specific substance P antagonist.Acknowledgments. The author is indebted to Ciba-Geigy (Canada) Ltd. for a gift of -COPG.Brenda Robson provided technical assistance. This work was supported by grants from the CanadianM. R. C. and the university of Saskatchewan.     

Transformation of amyloid β(1–40) oligomers into fibrils is characterized by a major change in secondary structure

Alzheimer’s disease (AD) is a neurodegenerative disorder occurring in the elderly. It is widely accepted that the amyloid beta peptide (Aβ) aggregation and especially the oligomeric states rather than fibrils are involved in AD onset. We used infrared spectroscopy to provide structural information on the entire aggregation pathway of Aβ(1–40), starting from monomeric Aβ to the end of the process, fibrils. Our structural study suggests that conversion of oligomers into fibrils results from a transition from antiparallel to parallel β-sheet. These structural changes are described in terms of H-bonding rupture/formation, β-strands reorientation and β-sheet elongation. As antiparallel β-sheet structure is also observed for other amyloidogenic proteins forming oligomers, reorganization of the β-sheet implicating a reorientation of β-strands could be a generic mechanism determining the kinetics of protein misfolding. Elucidation of the process driving aggregation, including structural transitions, could be essential in a search for therapies inhibiting aggregation or disrupting aggregates.