Demonstration of brain region-specific neuronal vulnerability in human iPSC-based model of familial Parkinson's disease.

Parkinson's disease (PD) is a neurodegenerative disorder characterized by protein inclusions mostly composed of aggregated forms of α-synuclein (α-Syn) and by the progressive degeneration of midbrain dopaminergic neurons (mDANs), resulting in motor symptoms. While other brain regions also undergo pathologic changes in PD, the relevance of α-Syn aggregation for the preferential loss of mDANs in PD pathology is not completely understood yet. To elucidate the mechanisms of the brain region-specific neuronal vulnerability in PD, we modeled human PD using human-induced pluripotent stem cells (iPSCs) from familial PD cases with a duplication (Dupl) of the α-Syn gene (SNCA) locus.

Power profiles and short-term visual performance of soft contact lenses.

Purpose: To investigate the manner in which contemporary soft contact lenses differ in the distribution of optical power within their optic zones and establish if these variations affect the vision of wearers or the prescribing procedure for back vertex power (BVP).

Methods: By using a Visionix VC 2001 contact lens power analyzer, power profiles were measured across the optic zones of the following contemporary contact lenses ACUVUE 2, ACUVUE ADVANCE, O2OPTIX, NIGHT & DAY and PureVision. Single BVP measures were obtained using a Nikon projection lensometer.

Professional master's degree programs in regulatory affairs and biomedical quality systems.

Two new programs are designed to supply biotechnology professionals with industry-specific skills required for successful biomedical product development.

Regulatory differences among avian ecto-ATPases.

Extracellular ATP is found to produce a variety of important biological responses. Ecto-ATPases are located on numerous cell types in many different species, regulate extracellular ATP levels and can be a key step in generating adenosine. Studies conducted on chicken ecto-ATPases from liver and cardiac and smooth muscle show a variety of differing properties including (1) different apparent Km's, (2) lectin sensitivity, (3) responses to detergents, (4) responses to lipid mediators, and (5) responsiveness to nucleotide-mimetic affinity labels.

The skeletal muscle transverse tubular Mg-ATPase: identity with Mg-ATPases of smooth muscle and brain.

Purified chicken skeletal muscle transverse tubule (T-tubule, TT) membrane preparations contain a very active Ca- or Mg-ATPase (EC 3.6.1.

Direct effects of phorbol esters and diacylglycerols on the T-tubule Mg(2+)-ATPase.

T-tubule membrane vesicles isolated from skeletal muscle contain a very active Mg(2+)-ATPase (EC 3.6.1.

Amino acid sequence of chicken calsequestrin deduced from cDNA: comparison of calsequestrin and aspartactin.

We have previously reported the amino terminal sequence of adult chicken calsequestrin, an intraluminal Ca2(+)-binding protein isolated from fast-twitch skeletal muscle. The partial sequence showed homology with mammalian calsequestrins contained in the PIR data bank and complete identity with the amino terminus of a putative laminin-binding protein of the extracellular matrix, aspartactin. Based on these data, oligonucleotide primers were synthesized for PCR amplification and direct DNA sequencing.

Calsequestrin, an intracellular calcium-binding protein of skeletal muscle sarcoplasmic reticulum, is homologous to aspartactin, a putative laminin-binding protein of the extracellular matrix.

Calsequestrin was isolated from chicken fast-twitch skeletal muscle, and partial amino terminal sequence was determined. The sequence (NH2) EEGLNFPTYDGKDRVIDLNE shows high identity with known mammalian calsequestrins contained in the Protein Identification Resource data bank (1). Most importantly, this 20 amino acid sequence shares complete identity with the amino terminus of aspartactin, a putative laminin-binding protein of the extracellular matrix (2, 3).

Biochemical properties of isolated transverse tubular membranes.

This review addresses the major biochemical and structural characteristics of isolated transverse tubule (T-tubule) membranes, including methods of isolation and morphology of purified membranes, evaluation of attendant membrane activities, including ion pumps and channels, and structural and compositional analyses of functionally relevant components. Particular emphasis is placed on the Mg2+-ATPase, its localization in the T-system, its unusual kinetic properties, its possible functions, and its potential regulation by diacylglycerol and other biologically-relevant lipids. Conclusions are drawn with respect to the biochemical markers characteristic of T-tubule membranes and the criteria to be applied in the assessment of isolated T-tubule membrane purity.

Common structural domains in the sarcoplasmic reticulum Ca-ATPase and the transverse tubule Mg-ATPase.

Transverse tubule (TT) membranes isolated from chicken skeletal muscle possess a very active magnesium-stimulated ATPase (Mg-ATPase) activity. The Mg-ATPase has been tentatively identified as a 102-kD concanavalin A (Con A)-binding glycoprotein comprising 80% of the integral membrane protein (Okamoto, V.R.

Studies on the transverse tubule membrane Mg-ATPase. Lectin-induced alterations of kinetic behavior.

Transverse tubule (TT) membrane vesicles contain a very active Mg-ATPase (EC 3.6.1.

Characterization of transverse tubule membrane proteins: tentative identification of the Mg-ATPase.

Vesiculated fragments of chicken skeletal muscle transverse tubule (TT) membranes were analyzed for their content of loosely associated and integral membrane proteins. Of particular interest was the identification of the magnesium-stimulated ATPase (Mg-ATPase), which is characteristically located in native isolated TT vesicles of chicken skeletal muscle [R. A.

Interaction of fluorescent adenine nucleotide derivatives with the ADP/ATP carrier in mitochondria. 2. [5-(Dimethylamino)-1-naphthoyl]adenine nucleotides as probes for the transition between c and m states of the ADP/ATP carrier.

The binding to the ADP/ATP carrier in mitochondrial membranes of the 3'-O-(dimethylamino)naphthoyl (DAN) derivatives of AMP, ADP, and ATP was quantitatively analyzed. The sidedness of the fluorescent type binding to the "m" side only was shown comparing the mitochondrial membranes in various stages of integrity and surface orientation. In particles displacement by bongkrekate (BKA) is direct, whereas in the case of carboxyatractylate (CAT) the requirement for ADP and ATP demonstrates the transition from the "m" to the "c" state.

Interaction of fluorescent adenine nucleotide derivatives with the ADP/ATP carrier in mitochondria. 1. Comparison of various 3'-O-ester adenine nucleotide derivatives.

Fluorescent 3'-O-acyl-substituted adenine nucleotide (dimethylamino)naphthoyl and trinitrophenyl groups were studied for binding to the ADP/ATP carrier in mitochondria and submitochondrial particles. The changes in fluorescence intensity and emission maximum are for the most part similar to those observed in nonaqueous solvents. The (dimethylamino)naphthoyl derivatives from a largely quenched aqueous state have a shortwave shift up to 85 nm and increase up to 90-fold (1,5 derivative), whereas the little quenched naphthoyl derivatives show a fluorescence decrease and the weakly fluorescent trinitrophenyl derivative shows only a small increase on binding.