Vagal communicating branches between the facial and glossopharyngeal nerves, with references to their occurrence from the embryological point of view.

A rare and hitherto not reported case in which a branch of the vagal nerve communicated simultaneously with the facial and the glossopharyngeal nerves was encountered in the body of a Japanese male cadaver in an anatomy class. This vagofacial-vagoglossopharyngeal (X.VII-X.IX) communicating branch was found to issue from the vagal nerve truck in close association with the pharyngeal branches (rami pharyngei nervi vagi), bifurcating soon into a vagofacial (X.VII) and a vagoglossopharyngeal division (X.IX). The X.VII division coursed forward and reached the posterior belly of the digastric muscle; after entering this muscle, this division broke up into filaments to communicate with the ramus digastricus of the facial nerve which was found to play an equivalent role in making the vagofacial ansa. The X.IX division, in contrast, took its course medially to reach the stylopharyngeal muscle. After entering this muscle, the X.IX division communicated with the stylopharyngeal branch of the glossopharyngeal nerve, which was found to be the equivalent to the X.IX division; these two form together the vagoglossopharyngeal ansa. Therefore, it could be concluded that the X.VII-X.IX communicating branch constitutes the vagal moieties of the vagofacial as well as the vagoglossopharyngeal ansae. The background of the appearance of the communicating branches observed in this report is discussed in the text from the developmental viewpoint on the basis of the findings obtained in chick embryos stained in whole mounts with anti-neurofilament protein antibody.     

Gc subtypes in some population groups from Israel. Comparison between world population groups and between Jews and non-Jews of the same areas

Results of Gc subtyping on 1,222 Israelis, Arabs and Jews, are summarized and their gene frequencies are analyzed in comparison with available data on Gc subtypes in non-Jews. A discriminant and a cluster analysis demonstrated that in their Gc subtype frequencies European and non-European Jews resemble the populations of the areas where they lived before immigrating to Israel. A possible explanation for this resemblance, which is seen in some and not seen in other genetic markers in Jews, is suggested here to be connected with the function of Gc as a vitamin D-binding protein.     

Comparison of central effects of noradrenaline and dopamine injected into the lateral brain ventricle in rats.

Noradrenaline and dopamine injected into the lateral brain ventricle exerted a significant effect on the behavior of rats. Both amines caused a slight rise in the basic locomotor activity which was significantly increased in the animals with inhibited monoamine oxidase activity. Besides that, they suppressed the behavior of rats in the open-field test, inhibited the conditioned avoidance response, decreased body temperature and increased amphetamine-induced motor hyperactivity. Noradrenaline, in contrast to dopamine, changed the intensity of amphetamine-induced stereotypy and prolonged the action of hypnotics. The central action of both catecholamines (in higher doses especially) seemed to have a biphasic course: in the first phase after administration depression was observed which was more pronounced after noradrenaline administration, in the second phase a stimulating effect b     

Solubilization and partial purification of the GABA receptor from mouse brain and a binding assay for the solubilized receptor.

Abstract— The GABA receptor from mouse brain was solubilized with lysolecithin. A 56-fold overall purification and activation were achieved by discontinuous sucrose gradient centrifugation and solubilization. Activation of binding by both procedures was observed. The solubilized receptor has the following binding constants: K_D1= 3.5 _nM, K_D2= 52 _nM, B_{max 1}= 2.8 pmol/mg protein and B_{max 2}= 14 pmol/mg protein for muscimol; K_D1= 12 nM, K_D2= 470 nM, B_{max 1}= 1.4 pmol/mg protein and B_{max 2}= 17 pmol/mg protein for GABA. Specific GABA binding was inhibited by imidazoleacetic acid and bicuculline with IC₅₀ values of 250_nM and 1 _μM respectively. A rapid and sensitive filtration binding assay for the solubilized receptor has been developed. Lysolecithin was also found suitable for the solubilization of acetylcholine receptor from T. californica electroplaques.     

Structural comparisons between the soluble and the GPI-anchored forms of the Paramecium temperature-specific 156G surface antigen.

Biosynthetic labelling experiments performed on P primaurelia strain 156, expressing the temperature-specific G surface antigen, 156G SAg, demonstrated that the purified 156G SAg contained the components characteristic of a GPI-anchor. [3H]ethanolamine, [3H]myo-inositol, [32P]phosphoric acid and [3H]myristic acid could all be incorporated into the surface antigen. Myristic acid labelling was lost after treatment in vitro with Bacillus thuringiensis phosphatidylinositol-specific phospholipase C (PI-PLC). After complete digestion by pronase, a fragment containing the intact GPI-anchor of 156G surface antigen was isolated. This fragment was shown to be hydrophobic and glycosylated and to possess an epitope found specifically in the GPI component of GPI-anchored proteins. The role of the GPI-tail in anchoring the 156G surface antigen into the membrane was assessed by determining that purified 156G molecules with the GPI-anchor could be incorporated into lipid vesicles and red cell ghosts whereas the 156G molecules lacking the GPI-anchor, as result of treatment with B thuringiensis PI-PLC, could not. It has also been shown that the membrane-bound form and the soluble form, obtained after cleavage of the 156G SAg lipid moiety either by an endogenous PI-PLC or by a bacterial PI-PLC, displayed identical circular dichroic spectra.     

Systematics on the threshold of the XXI century. Traditional principles and fundamentals from today's point of view

Systematics as regarded is a purely theoretical domain of biology, and its product, system, as a specific biological theory, or a topologo-genetic model of the biota. Linnaeus was the first to introduce the idea of system and the systematic approach into the natural history. The advent of evolutionism brought new meaning to the old term "affinity", so Linnaeus' slogan of natural system got new life, and Linnaeus taxonomy assimilated the evolutionary ideology quite naturally and much easier than many other departments of biology. The difference between natural and artificial systems is remaining, and it is in their goals, as formulated by Linnaeus: heuristic of the former and cataloguing of the latter. Linnaeus' clairvoyance discovered the existence of an infrageneric level of genetic integration provable by naturalists' experience. He chose for it the designation of "species" and laid it down as primary, basic unit of his system. This is plainly evident from his own writings; the story about Linnaean species being products of a logical division of genera is a pure fiction. Modern populational model of species, by 3 important criteria, appears to be more akin to the Linneaean one than to the ideas of Lamarckism and early Darwinism. Systematic approach focuses rather on the interrelations among elements and their relative position, then on the properties and qualities of separately treated individual elements. In the development of systematics the aspect of "nexification" (study of connections) has been continuously gaining attention especially regarding the nomenclature where connotation has been totally forced out by denotation.     

Comparison of ornithine decarboxylase from rat liver, rat hepatoma and mouse kidney.

Comparisons were made of ornithine decarboxylase isolated from Morris hepatoma 7777, thioacetamide-treated rat liver and androgen-stimulated mouse kidney. The enzymes from each source were purified in parallel and their size, isoelectric point, interaction with a monoclonal antibody or a monospecific rabbit antiserum to ornithine decarboxylase, and rates of inactivation in vitro, were studied. Mouse kidney, which is a particularly rich source of ornithine decarboxylase after androgen induction, contained two distinct forms of the enzyme which differed slightly in isoelectric point, but not in Mr. Both forms had a rapid rate of turnover, and virtually all immunoreactive ornithine decarboxylase protein was lost within 4h after protein synthesis was inhibited. Only one form of ornithine decarboxylase was found in thioacetamide-treated rat liver and Morris hepatoma 7777. No differences between the rat liver and hepatoma ornithine decarboxylase protein were found, but the rat ornithine decarboxylase could be separated from the mouse kidney ornithine decarboxylase by two-dimensional gel electrophoresis. The rat protein was slightly smaller and had a slightly more acid isoelectric point. Studies of the inactivation of ornithine decarboxylase in vitro in a microsomal system [Zuretti & Gravela (1983) Biochim. Biophys. Acta 742, 269-277] showed that the enzymes from rat liver and hepatoma 7777 and mouse kidney were inactivated at the same rate. This inactivation was not due to degradation of the enzyme protein, but was probably related to the formation of inactive forms owing to the absence of thiol-reducing agents. Treatment with 1,3-diaminopropane, which is known to cause an increase in the rate of degradation of ornithine decarboxylase in vivo [Seely & Pegg (1983) Biochem. J. 216, 701-717] did not stimulate inactivation by microsomal extracts, indicating that this system does not correspond to the rate-limiting step of enzyme breakdown in vivo.     

Immunological,isoelectric, hydrophobic and molecular weight differences between soluble and ionically membrane-bound fractions of choline-o-acetyltransferase prepared from mouse and rat brain

Choline-O-acetyltransferase (EC 2.3.1.6; ChAT) was prepared from synaptosomal fractions (P₂) of mouse and rat brain in the presence of proteolytic inhibitors by the method of Gray and Whittaker (1962) as modified by (Salehmoghaddam and Collier, 1976). The P₂ fraction was hypo-osmotically shocked with glass distilled water and centrifuged to separate the cytoplasmic (S₃) and vesicle-bound (P₃) fractions. Fraction S₃ was saved for ChAT assay and compared with the ChAT fraction eluted from the P₃ by salt at a pH 7.4 or by detergent (Benishin and Carroll, 1983). These three fractions of ChAT were then compared by molecular weights, isoelectric points, immunoblotting with monoclonal or polyclonal antibodies and hydrophobicity. The results show that the S₃ fraction of ChAT has a molecular weight of 66 K_d, whereas the ionically-bound fraction of ChAT has a molecular weight of 73–78 K_d. SDS-PAGE of these two ChAT fractions followed by immunoblotting revealed the presence of two immunoreactive bands at 28–29 K_d and 50–51 K_d for the ionically bound ChAT fraction. Conversely, none of these antibodies immunostained any protein bands for the S₃ ChAT fraction even though one monoclonal antibody had been prepared against this ChAT fraction and the S₃ ChAT fraction had a similar specific activity prior to SDS-PAGE as did the salt solubilized ChAT fraction. However, anti-ChAT monoclonal antibody MB16 binds the native S₃ ChAT fraction in the co-precipitation assay.The S₃ fraction of ChAT had only one isoelectric point at pH 7.8, whereas the ionically bound and detergent soluble ChAT fractions had two isoelectric points at pH 8.1–8.15 and 7.45–7.5. The S₃ ChAT fraction also differed in hydrophobicity from the other two ChAT fractions. These differences between the S₃ and salt soluble ChAT fractions were not obviated by addition of Triton X-100 and thus could not be attributed to the association of lipids with either of the fractions. We conclude that the water soluble fraction of ChAT in central nerve terminals differs in its physical properties and its subcellular location from that which ionically binds to membranes.     

Development and characteristics of an oestrogen sulphotransferase in placenta and uterus of the pregnant mouse. Comparison between mouse and rat.

The mouse placenta possesses a soluble oestrogen sulphotransferase activity which increases markedly from at least 12 days of gestation until term. At about 16 days of gestation, a similar activity is found in the uterus. This activity also increases until term and disappears rapidly post partum. The uterine enzyme activity appears to require the presence of the foetal unit for its onset, since unoccupied horns, whether their endometrial stromal cells are differentiated to decidual cells or not, are essentially devoid of it. Uterine cytosols from non-pregnant mice are also inactive in this respect. In late gestation, the uterine sulphotransferase is confined to the decidua basalis, the areas to which the placentas are attached. The sulphotransferase(s) of placenta and uterus has an absolute requirement for 3'-phosphoadenosine 5'-phosphosulphate, and possesses little activity in the absence of exogenous thiol groups. Stimulation is also seen in the presence of Mn2+, Mg2+ or Ca2+. Oestrone and oestradiol, and to a lesser degree oestriol, are substrates for the enzyme(s), whereas testosterone, cortisol and dehydroepiandrosterone are not. Oestrone and oestradiol at higher concentrations (1.0-1.5 microM) completely inhibit the enzyme(s). These enzymes could play a role in altering tissue concentrations of active oestrogens during gestation in the mouse. Oestrogen sulphotransferase activity is low or absent in reproductive tissues of the pregnant rat.     

Interrelation between fusions in the primary dentition and agenesis in the succedaneous permanent dentition seen from an embryological point of view

The purpose of the present study was to elucidate the relationship between fusions in the primary dentition and the occurrence of agenesis in the succedaneous permanent dentition in a Danish child population and to elucidate this relationship from the recently described normal embryological development of the anterior parts of the human maxilla and mandible. The material included radiographs, either as intraoral film or as orthopantomograms from a total of 19 primary dentitions with a total of 21 fusions. Radiographs of the permanent dentition in the fusion regions were available for all 19 dentitions. Of 21 fusions, a total of 20 were in the mandible and one in the maxilla. In 15 cases, the fusions were between primary incisors and in six cases between lateral incisors and canines. Agenesis of a permanent lateral incisor always occurred when there had been fusion of a primary lateral incisor and a canine in the primary dentition. When fusion had been between primary incisors, there was only agenesis of an incisor in the permanent dentition in a few cases. The degree of fusion between the involved teeth was not related to the occurrence of agenesis. It is suggested that the intra-jaw differences are related to the recently reported prenatal developmental patterns of the alveoli of the incisors and canines. Moreover, it is suggested that neural crest developmental field differences between the developing maxilla and mandible may explain the inter-jaw differences in phenotypic abnormalities.     

Immunoprecipitation of high-affinity, guanine nucleotide-sensitive, solubilized mu-opioid receptors from rat brain: coimmunoprecipitation of the G proteins G(alpha o), G(alpha i1), and G(alpha i3)

Antibodies directed against the C-terminal and the N-terminal regions of the mu-opioid receptor were generated to identify the G proteins that coimmunoprecipitate with the mu receptor. Two fusion proteins were constructed: One contained the 50 C-terminal amino acids of the mu receptor, and the other contained 61 amino acids near the N terminus of the receptor. Antisera directed against both fusion proteins were capable of immunoprecipitating approximately 70% of solubilized rat brain mu receptors as determined by [3H][D-Ala2,N-Me-Phe4,Gly-ol5]-enkephalin ([3H]DAMGO) saturation binding. The material immunoprecipitated with both of the antisera was recognized as a broad band with a molecular mass between 60 and 75 kDa when screened in a western blot. Guanosine 5'-O-(3-thiotriphosphate) (GTPgammaS) had an EC50 of 0.4 nM in diminishing [3H]DAMGO binding to the immunoprecipitated pellet. The ratio of G proteins to mu receptors in the immunoprecipitated material was 1:1. When the material immunoprecipitated with affinity-purified antibody was screened for the presence of G protein a subunits, it was determined that G(alpha)o, G(alpha)i1, G(alpha)i3, and to a lesser extent G(alpha)i2, but not G(alpha)s or G(alpha)q11, were coimmunoprecipitated with the mu receptor. Inclusion of GTPgammaS during the immunoprecipitation process abolished the coimmunoprecipitation of G proteins.