The effects of microinjection of carbachol or hemicholinium into the amygdala on the levels of plasma and adrenal corticosterone in rats

Microinjections of 0.4 microgram of carbachol into the amygdala caused a rise of corticosterone (CS) in the morning when the prestimulating level of CS was lower. But the same procedure with a larger dose had no effect in the afternoon, when the prestimulating level of CS was higher.     

Anomeric compositions of D-glucose in tissues and blood of rat

The anomeric compositions of D-glucose in the liver, kidney, heart, blood and plasma of rat were determined by our methods for the assay of D-glucose anomers and the percentages of the beta-anomer were found to be 61.8, 61.0, 62.4, 62.7 and 62.9, respectively.     

Rheological and functional impairments in cholesterol-loaded human erythrocytes

Summary Decreased deformability, slightly increased suspension viscosity and retarded oxygen egress were observed in cholesterol-loaded, human erythrocytes. These functional changes resulted from the decreased membrane fluidity induced by cholesterol.     

Cloning, sequencing and expression of complementary DNA encoding the muscarinic acetylcholine receptor

Cloning and sequence analysis of DNA complementary to porcine cerebral messenger RNA encoding the muscarinic acetylcholine receptor predict the complete amino-acid sequence of this protein. Expression of the complementary DNA produced functional muscarinic receptor in Xenopus oocytes. The muscarinic receptor is homologous with the beta-adrenergic receptor and rhodopsin in both amino-acid sequence and suggested transmembrane topography.     

Selective coupling with K+ currents of muscarinic acetylcholine receptor subtypes in NG108-15 cells

The primary structures of two muscarinic acetylcholine receptor (mAChR) species, designated as mAChR I and mAChR II, have been elucidated by cloning and sequence analysis of DNAs complementary to the porcine cerebral and cardiac messenger RNAs, respectively. mAChR I and mAChR II expressed in Xenopus oocytes differ from each other both in acetylcholine-induced response and in antagonist binding properties. These results, together with the differential tissue location of the two mAChR mRNAs, have indicated that pharmacologically distinguishable subtypes of the mAChR represent distinct gene products. The primary structures of two additional mammalian mAChR species, designated as mAChR III and mAChR IV, have subsequently been deduced from the nucleotide sequences of the cloned cDNAs or genomic DNAs. We report here that mAChR I and mAChR III expressed in NG108-15 neuroblastoma-glioma hybrid cells, but not mAChR II and mAChR IV, efficiently mediate phosphoinositide hydrolysis, activation of a Ca2+-dependent K+ current and inhibition of the M-current, a voltage-dependent K+ current sensitive to muscarinic agonists.     

The acceleration of cosmic-ray protons in the supernova remnant RX J1713.7-3946

Protons with energies up to approximately 10(15) eV are the main component of cosmic rays, but evidence for the specific locations where they could have been accelerated to these energies has been lacking. Electrons are known to be accelerated to cosmic-ray energies in supernova remnants, and the shock waves associated with such remnants, when they hit the surrounding interstellar medium, could also provide the energy to accelerate protons. The signature of such a process would be the decay of pions (pi(0)), which are generated when the protons collide with atoms and molecules in an interstellar cloud: pion decay results in gamma-rays with a particular spectral-energy distribution. Here we report the observation of cascade showers of optical photons resulting from gamma-rays at energies of approximately 10(12) eV hitting Earth's upper atmosphere, in the direction of the supernova remnant RX J1713.7-3946. The spectrum is a good match to that predicted by pion decay, and cannot be explained by other mechanisms.     

Structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand

In a variety of cells, the Ca2+ signalling process is mediated by the endoplasmic-reticulum-membrane-associated Ca2+ release channel, inositol 1,4,5-trisphosphate (InsP3) receptor (InsP3R). Being ubiquitous and present in organisms ranging from humans to Caenorhabditis elegans, InsP3R has a vital role in the control of cellular and physiological processes as diverse as cell division, cell proliferation, apoptosis, fertilization, development, behaviour, memory and learning. Mouse type I InsP3R (InsP3R1), found in high abundance in cerebellar Purkinje cells, is a polypeptide with three major functionally distinct regions: the amino-terminal InsP3-binding region, the central modulatory region and the carboxy-terminal channel region. Here we present a 2.2-A crystal structure of the InsP3-binding core of mouse InsP3R1 in complex with InsP3. The asymmetric, boomerang-like structure consists of an N-terminal beta-trefoil domain and a C-terminal alpha-helical domain containing an 'armadillo repeat'-like fold. The cleft formed by the two domains exposes a cluster of arginine and lysine residues that coordinate the three phosphoryl groups of InsP3. Putative Ca2+-binding sites are identified in two separate locations within the InsP3-binding core.     

Partial sequence of the tyrosine region of neocarzinostatin

Zusammenfassung Das antitumoraktive Protein-Antibiotikum Neocarzinostatin wurde mit Dithiothreit in flüssigem Ammoniak reduziert und mit Chloressigsäure alkyliert. Tryptische Spaltung des tetra-S-carboxymethylierten Proteins ergab 5 Fragmente. Die Sequenz von 25 Aminosäureresten im tyrosinhaltigen Fragment H₃ wurde durchEdman-Abbau im automatisierten Sequenator ermittelt.

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This work was supported in part by Public Health Service Research Grants No. C-6516 from the National Cancer Institute and No. FR-05526 from the Division of Research Facilities and Resource, National Institutes of Health, to the Children's Cancer Research Foundation and by grants No. AM 04501 and No. AM 11794 from the National Institute of Arthritis and Metabolic Diseases to the Endocrine Unit, Massachusetts General Hospital.     

Restoration of the poor oxygen transport function of ACD-stored blood by pyridoxal 5'-phosphate.

Pyridoxal 5'-phosphate is easily incorporated into ACD-stored erythrocytes without decrease of ATP, and restores the poor oxygen transport function with a similar effect to 2,3'-diphosphoglycerate.