The organization and structure of nerve and muscle in the jellyfish Cyanea capillata (coelenterata; scyphozoa)

The perirhopalial tissue and swimming muscle of Cyanea were examined with light microscopical and electron microscopical techniques. The perirhopalial tissue is a thin, triangular septum found on the subumbrellar surface of the animal. It separates part of the gastric canal system from the surrounding seawater, and is bound on two sides by radial muscle bands and on the third, the shorter side, by a rhopalium and the margin of the bell. The ectoderm of the perirhopalial tissue is composed of large, somewhat cuboidal, vacuolated, myoepithelial cells. The muscle tails of these cells form a single layer of radial, smooth muscle. Neurons of the “giant fiber nerve net” (GFNN), which form an extensive net over the perirhopalial tissue, lie at the base of the vacuolated portion of the myoepithelial cells. These neurons are visible in living tissue. The morphology of individual GFNN neurons was examined following intracellular injection of the fluorescent dye Lucifer Yellow. The neurons are usually bipolar and free of branches. At the electron microscope level, one usually finds that the GFNN neurons contain large vacuoles. The other characteristic feature of these cells is that they form symmetrical, or nonpolarized, synapses; that is, synaptic vesicles are found on both sides of the synapse. The swimming muscle is striated and composed of myoepithelial cells. Each myoepithelial cell has several muscle tails, and those of adjacent cells are linked to gether by desmosomes. The endoderm of the perirhopalial tissue also was examined. This investigation of the organization and ultrastructure of the perirhopalial tissue and surrounding muscle was undertaken to provide essential background information for an ongoing physiological study of the GFNN neurons and their synapses.     

Ultrastructure of oesophageal appendages ("peptonephridia") in enchytraeids (Annelida: Clitellata)

Abstract. Although the oesophageal appendages in the four enchytraeids Enchytrueus crypticus, Fredericia strinta, Buchholzia appendiculata , and Achaeta sp. are quite different from one another in shape and position, their histology and ultrastructure are basically the same. These are intestinal appendages, the lumina of which distally end blind and proximally open into the oesophagus. Almost all of the few cells in their single-layered epithelium have a microvillous, cilia-free border at the apex, facing towards the lumen, and basally comprise an extremely extensive labyrinth. The presence of the latter, composed of very thin cell processes, and of numerous mitochondria identifies the organs as energy-producing and -consuming, transport-active structures. Their possible function as a food-moistening organ or osmoregulatory organ is discussed, and they are compared with other intestinal appendages in enchytraeids and other oligochaetes.     

Testicular metamorphosis rates in European Starlings maintained under short daily photophases

Juvenile male European Starlings(Sturnus vulgaris) were maintained under discrete fixed daily photophases ranging from 1 to 11 h in duration. Treatment began on 20 December when all birds were reproductively quiescent, and continued until 14 June of the following year.In situ measurements of left testis widths at monthly intervals documented testicular width increases to levels associated with complete spermatogenesis in birds under all photoperiod regimens. Starlings maintained under the shortest and longest photoperiods required fewer days of treatment to achieve spermatogenic testes than did those under intermediate-length photoperiods. Data are consistent with the hypothesis that prolonged daily periods of darkness result in oscillations of a circadian timing system stimulating increased gonadotropin secretion and consequent testicular metamorphosis.     

Studien Über Verbreitung und Bildung der Säureamide in der höheren Pflanze

Ohne ZusammenfassungMit 1 Textabbildung.Dissertation der Philosophischen Fakultät der Universität Leipzig.     

Identification and partial characterization of a latent ATP,Mg-dependent protein phosphatase in rabbit skeletal muscle cytosol

Summary Fractionation of rabbit skeletal muscle cytosol on Aminohexyl-Sepharose has resulted in the identification of a latent ATP, Mg-dependent protein phosphatase whose catalytic subunit is in the active conformation, but is inhibited by the presence of more than one modulator unit. The partially purified enzyme is converted to an inactive, kinase F_A-dependent form upon incubation at 30°C unless modulator-specific polyclonal antibodies are added to the preparation. The immunoglobulins also relieve the inhibition which is responsible for the low basal phosphatase activity of the enzyme, and they counteract all of the heat-stable inhibitor activity present in the preparation. Addition of free catalytic subunit abolishes the inhibition of the latent enzyme in a dose-dependent way, but cannot prevent the inactivation process. The inactivated phosphatase and the original latent enzyme exhibit the same apparent M _r in sucrose density-gradient centrifugation (70 000) and in gel filtration (110 000).Abbreviations PMSF Phenylmethanesulphonyl Fluoride - TLCK L-l-chloro-3-(4-tosylamido)-7-amino2-heptanone-hydrochloride - TPCK L-l-chloro-3-(4-tosvlamido)-4-phenyl-2-butanone     

The N-Myc oncoprotein is associated in vivo with the phosphoprotein Max(p20/22) in human neuroblastoma cells.

Proteins encoded by the proto-oncogenes c-myc, L-myc, and N-myc contain at their carboxy-terminus a tripartite segment comprising a basic DNA binding region (BR), a helix-loop-helix (HLH) and a leucine zipper motif (Zip), that are believed to be involved in DNA binding and protein-protein interaction. The N-Myc oncoprotein is overexpressed in certain human tumors that share neuroectodermal features due to amplification of the N-myc gene. Using a monoclonal antibody directed against an N-terminal epitope of the N-Myc protein in immunoprecipitations performed with extracts of neuroblastoma cells, two nuclear phosphoprotein, p20/22, forming a hetero-oligomeric complex with N-Myc are identified. Both proteins are phosphorylated by casein kinase II in vitro. By partial proteolytic maps we show that p20 and p22 are structurally related to each other and that p20 is identical with Max, a recently described in vitro binding partner of myc proteins. Time course experiments show the presence of the complex in cellular extracts immunoprecipitated within a 5 min interval after the preparation of the cell extract. While the expression of N-myc is restricted, expression of both Max(p20/22) and the murine homolog Myn(p20/22) was observed in cells of diverse human and murine embryonal lineages as detected by heterologous complex formation. By introduction of expression vectors containing the wild type N-myc gene or N-myc genes with in frame deletions or point mutations into recipient cells and subsequent immunoprecipitation of the resulting N-Myc proteins we show that the HLH-Zip region is essential to the formation of the N-Myc-p20/22 complex.     

Selectivity of juxtaposition between cup-shaped lactotrophs and gonadotrophs from rat anterior pituitary in culture

Summary Semi-thin sections of three-dimensional reaggregates from adult female rat pituitary, cultured in serum-free defined medium, were stained for prolactin, gonadotropin, thyrotropin, growth hormone and S-100, using the double immunolabelling technique. The frequency of juxtaposition between lactotrophs and gonadotrophs was enumerated and compared with the expected frequency at random distribution of polygonal cell profiles in a hexagonal configuration. The proportions of lactotrophs and gonadotrophs in the aggregate sections were determined using stereometrical analysis. The observed frequency of juxtaposition did not differ significantly from the expected frequency. Hence, no reason was found to assume a selective adhesion between lactotrophs and gonadotrophs in adult female rat pituitary reaggregates. A constant proportion of lactotrophs was found to meet the criteria of a cup-shaped morphology, and 70%±9% (mean ±S.D.) of these so-called cupshaped lactotrophs were found to be juxtaposed at their concave side to gonadotrophs. Administration of 0.01 nM 17-oestradiol to the culture medium resulted in a significant reduction of the proportion of cup-shaped lactotrophs but did not affect the selectivity of juxtaposition to gonadotrophs. The selectivity of juxtaposition between cup-shaped lactotrophs and gonadotrophs may be the morphological correlate of the functional relationship between these cells, which are known to be involved in an intra-pituitary paracrine communication system.     

Positive effectors of the binding of an active site-directed amino steroid to rabbit cytochrome P-450 3c

The binding of the amino steroid, 22-amino-23,24-bisnor-5-cholen-3 beta-ol (22-ABC), to rabbit liver cytochrome P-450 3c was studied using purified P-450 3c and liver microsomes prepared from rifampicin-treated B/J rabbits. 22-ABC binds to purified cytochrome P-450 3c producing a type II spectral change reflecting the coordination of the amine with the heme iron of the protein. In the absence of allosteric effectors, the binding is characterized by a Ks of 5 microM. In the presence of alpha-naphthoflavone or progesterone, the Ks decreases to 0.8 microM, indicating that these two compounds serve as positive effectors of the binding of 22-ABC to cytochrome P-450 3c. The antibiotic rifampicin induces cytochrome P-450 3c in rabbit liver microsomes, and the benzo(a)pyrene hydroxylase, estradiol 2-hydroxylase, and progesterone 6 beta-hydroxylase activities of these microsomes are stimulated by alpha-naphthoflavone. Moreover, the progesterone 6 beta-hydroxylase activity catalyzed by these microsomes exhibits a dependence on substrate concentration that is consistent with activation of the enzyme by the substrate, progesterone. The magnitude of the type II spectral change elicited by 22-ABC for microsomes prepared from rifampicin-treated B/J rabbits is greater than that observed for microsomes from untreated rabbits. For microsomes from rifampicin-treated rabbits, the apparent binding constant for 22-ABC was decreased 5-fold in the presence of alpha-naphthoflavone. We propose that the effects of alpha-naphthoflavone and progesterone on the binding of 22-ABC to cytochrome P-450 3c mimic the effects of the two positive effectors on the metabolism of substrates by increasing the affinity of the enzyme for substrate.