Helical Poly(phenylacetylene) Bearing Chiral and Achiral Imidazolidinone-Based Pendants that Catalyze Asymmetric Reactions due to Catalytically Active Achiral Pendants Assisted by Macromolecular Helicity.

A series of optically active helical copolymers of phenylacetylenes are prepared by the rhodium-catalyzed copolymerization of the imidazolidinone-linked, catalytically active achiral phenylacetylenes and catalytically inactive chiral phenylacetylenes. The obtained chiral/achiral copolymers exhibit an induced circular dichroism in the UV-vis regions of the copolymer backbones resulting from a preferred-handed helical conformation biased by the chiral imidazolidinone units incorporated in the copolymers. The copolymers are found to catalyze the asymmetric Diels-Alder reaction and produce the products with a moderate enantioselectivity in spite of the fact that the catalytically active units of the copolymers are achiral, indicating that the observed enantioselectivity totally originates from the helical chirality dynamically induced by the optically active, but catalytically inactive imidazolidinone units incorporated in the copolymers.

[Case of neuro-Behçet disease with homonymous quadrantanopsia due to an inflammatory lesion involving the lateral geniculate body].

We report a rare case of a 57-year-old woman of neuro-Behçet disease with homonymous quadrantanopsia due to an inflammatory lesion involving the lateral geniculate body. She had oral and genital ulcers since 1983, and uveitis since May 1985. She received diagnosis of incomplete Behçet disease and was prescribed cyclophosphamide since June 1985. After the treatment, she recovered completely from uveitis in July 1985. Painful subcutaneous nodules appeared in her right leg on June 21, 2004 and she had a high fever, headache and left visual disturbance on June 29, 2004. Therefore, she was admitted to our hospital on July 1, 2004. Physical and neurological examination showed erythema nodosum in the right lower extremity and left lower homonymous quadrantanopsia. Laboratory findings on admission showed leucocytosis, increased erythrocyte sedimentation rate and C-reactive protein, and positive HLA-B51. Cerebrospinal fluid analysis showed pleocytosis and a markedly high level of protein and interleukin-6. Brain magnetic resonance imaging (MRI) of T2-weighted images showed high intensity lesions in the circumference of the caudal thalamus, optic radiations, and right occipital cortex. T1-weighted images with gadolinium enhancement showed an enhanced lesion in the circumference of the right lateral geniculate body. From these results, she was diagnosed as having an acute relapsing phase of neuro-Behçet disease and she received steroid pulse therapy. Immediately after steroid pulse therapy, she received high-dose prednisolone which was gradually tapered. Brain MRI after treatment showed a high intensity lesion in the right lateral geniculate body. Homonymous quadrantanopsia remained nearly unchanged.

Sarcospan: ultrastructural localization and its relation to the sarcoglycan subcomplex.

Sarcospan is a 25 kDa transmembrane component of dystrophin-associated glycoprotein. We generated a rabbit polyclonal antibody against synthetic peptide of the N-terminal domain of human sarcospan. Using this antibody we investigated the localization of sarcospan and its spacial relation to the components of sarcoglycan subcomplex in normal human skeletal myofibers by immunofluorescent microscopy and immunogold electron microscopy. In immunofluorescence the reaction was observed continuously at the myofiber surface. Ultrastructurally the gold signals of rabbit anti sarcospan antibody were present along the muscle plasma membrane, mainly at its inside surface. The triple immunogold labeled muscle samples showed that the signals of rabbit or sheep polyclonal anti alpha-, beta-, gamma- and delta-sarcoglycan antibodies and/or mouse monoclonal anti beta-, gamma- and delta-sarcoglycan antibodies were located along the muscle plasma membrane, and the cluster formation of different two or three sarcoglycan molecules was observed. The triple immunogold labeling also revealed that the signal of sarcospan molecules are present frequently in doublets and/or triplets with the components of sarcoglycan subcomplex, resulting in the cluster formation of signals of sarcoglycan and sarcospan molecules. The result of this study showed that sarcospan was expressed at the myofiber surface and that sarcospan was present in close association with alpha-, beta-, gamma- and delta-sarcoglycans and formed a functional unit with sarcoglycan subcomplex.