The dopaminergic innervation of the intermediate lobe and of the neural lobe of the pituitary gland

The intermediate and the neural lobe of the pituitary gland are innervated by two, virtually independent, groups of dopaminergic neurons which, until recently, were considered as a uniform system and referred to as the "tubero-hypophyseal dopamine system". Some aspects of the separate physiological functions of these neurons in the intermediate and in the neural lobe, of their microanatomy and biochemistry as well as of dopamine release from their terminals are discussed in this review.     

Adenosine triphosphatase activity of mycoplasma membranes

Rottem, Shlomo (Hebrew University, Jerusalem, Israel), and Shmuel Razin. Adenosine triphosphatase activity of mycoplasma membranes. J. Bacteriol. 92:714-722. 1966.-Adenosine triphosphatase activity of Mycoplasma laidlawii, M. gallisepticum, and Mycoplasma sp. strain 14 was confined to the cell membrane. The enzymatic activity was dependent on magnesium, but was not activated by sodium and potassium. Ouabain did not inhibit the adenosine triphosphatase activity of the mycoplasmas, and did not interfere with the active accumulation of potassium by M. laidlawii cells. Sulfhydryl-blocking reagents and fluoride inhibited the enzymatic activity, whereas 2,4-dinitrophenol was without any effect. Membranes of M. laidlawii hydrolyzed other nucleotide triphosphates and adenosine diphosphate (ADP), but at a lower rate than adenosine triphosphate (ATP). Nucleoside-2'-(3')-phosphates, ribose-5-phosphate, glucose-6-phosphate, and pyrophosphate were not hydrolyzed by the membrane preparations. It seems that the enzyme(s) involved in ATP hydrolysis by M. laidlawii membranes is strongly bound to the membrane subunits, which would account for the failure to purify the enzyme by protein fractionation techniques. The adenosine triphosphatase activity of mycoplasma membranes resembles in its properties that of similar enzymes studied in bacteria. The mycoplasma enzyme(s) seems to differ from the adenosine triphosphatase associated with ion transport in mammalian cell membranes and from mitochondrial adenosine triphosphatase.     

Adenosine triphosphatase activity in the osmoregulatory organs of vertebrates

Studies have been made on the activity of cation- and anion-stimulated ATPases, as well as succinic dehydrogenase in homogenates and subcellular fractions from osmoregulatory organs of marine (elasmobranch and teleost) and freshwater (teleost) fishes, amphibians, reptiles, birds and mammals. The activity of Na+, K+-ATPase was found to be rather similar in almost all osmoregulatory organs of the species investigated. The highest level of Cl-stimulated ATPase was found in microsomal fraction of the kidneys from birds and mammals. Succinic dehydrogenase activity is significantly higher in the renal tissue of mammals, both in total homogenates and in mitochondrial fraction.     

Isolation and protein composition of membranes of neurosecretory vesicles and plasma membranes from the neural lobe of the bovine pituitary gland.

1. Homogenates of neural lobes of bovine pituitary glands were fractionated by differential ultracentrifugation. 2. Neurosecretory vesicles were isolated by sucrose-gradient ultracentrifugation and membranes were obtained after hypo-osmotic lysis of the particles. 3. A method is described for the isolation of a preparation of purified neuronal plasma membranes by using a fraction enriched in nerve endings as a starting material. 4. The purity of the subcellular fractions was estimated by enzyme assays and by examination with the electron microscope. 5. On the basis of the results it was estimated that neuronal plasma membranes constitute more than 30% of the protein of the nerve endings and neurosecretory vesicles more than 45% of the total amount of protein in the homogenate. 6. The proteins of membranes of neurosecretory vesicles and of plasma membranes were solubilized by means of sodium dodecyl sulphate. Polyacrylamide-gel electrophoresis of such preparations showed that both membranes contained a large number of proteins, including three glycoproteins.     

Adenosine triphosphatase activity of cutaneous nerve fibers

Summary The histochemical study of Mg⁺⁺-activated adenosine triphosphatase (Mg⁺⁺-ATPase) activity was carried out on the peripheral nerves of mouse digital skin by light and electron microscopy. Under the light microscope, the ATPase activity was clearly demonstrated on the nerve fibers as a fine network in the subepidermal regions. Under the electron microscope, the reaction product of enzyme activity was located in the interspace between axolemma and the surrounding Schwann cells of the unmyelinated nerve fibers. No reaction product was observed in the space between the axolemma and the Schwann cells associated with myelinated nerve fibers. Demonstrable activity was absent at the nodes of Ranvier as well as on the para- and internodal regions of these myelinated axons. The part of the axolemma lacking a Schwann cell sheath failed to show a reaction product. The perineural epithelial cells surrounding the nerve fibers displayed reaction product in the caveolae. These results suggest a functional difference in the axon-Schwann interface of myelinated as compared to unmyelinated nerve fibers. The function of the perineural epithelial cell would be expected to be a regulatory one in transferring materials across the epithelium to keep the proper humoral environment around nerve fibers.     

Adenosine triphosphatase activity of Tritrichomonas foetus.

Homogenates of Tritrichomonas foetus exhibited a Mg2+-dependent adenosine triphosphatase (ATPase) activity, with a pH optimum in Tris buffers of 8.2 to 8.3. The activity was not sensitive to oxygen. At high concentrations, quercetin and 4-chloro-7-nitrobenzofurazan inhibited ATPase activity in the cytoplasmic extract by 20 and 70%, respectively, whereas oligomycin, venturicidin, triethyltin, leucinostatin, dibutylchloromethyltin chloride, spegazzinine, efrapeptin, citreoviridin and sodium azide had no effect and N,N'-dicyclohexylcarbodi-imide stimulated the activity somewhat. The activity was localized in a population of small cytoplasmic particles which also contained an acid phosphatase. There was no indication of an association of ATPase with hydrogenosomes. The ATPase activity (or activities) in this aerotolerant anaerobe is different from the ATPases characteristic of mitochondria or of anaerobic bacteria.     

Adenosine triphosphatase activity in the carotid body of the cat

Summary Three kinds of nucleoside phosphatases were demonstrated histochemically in the cat carotid body with nucleoside triphosphate, nucleoside disphosphate and nucleoside monophosphate as substrates. Each of these enzyme activities exhibited the substrate specificity respectively. The nucleoside triphosphatase activity showed specific localization in association with the parenchymal cells of the carotid body.The electronmicroscopy revealed that the reaction product was located on and between the two apposing plasma membranes of type I and type II cells, of a type II cell and its wrapping axons and of the intricate basal infolding of a type II cell itself.Some possible functions of the adenosine triphosphatase in the carotid body are discussed.     

Movement of neurosecretory product through the anatomical compartments of the neural lobe of the pituitary gland

Summary Electron microscopic studies of the carotid body of the domestic fowl (Gallus gallus domesticus) have shown Type I and Type II cells combined with axons into compact groups. The many Type I cells in the depths of the organ had a body, containing the nucleus, and an elongated, flared process. Some of the Type I cells in the superficial regions tended to be spindle-shaped. Type I cells were characterised by membrane-bound, dense-cored vesicles about 120 nm in diameter. Type II cells invested the Type I cells and had axons embedded in them as in Schwann cells.The fine structure of the carotid body in the domestic fowl resembles that of the Lovebird (Uroloncha domestica) and of various amphibia and mammals. The possibility is discussed that the Type I cells may have a chemoreceptor or a general secretory function, or even both pathway for functions together. The main role of the Type II cells seems to be to provide a of these axons leading to or from Type I cells.The authors are grateful to Mr. R. P. Gould of the Department of Anatomy, Middlesex Hospital Medical School for permission to use some of his and Dr. Hodges' original material in the illustrations. Dr. Hodges also wishes to thank the A.R.C. and the University of London Central Research Fund for financial assistance. We are also most appreciative of the photographic assistance of J. Geary.     

Adenosine triphosphatase activity associated with mung bean mitochondria

The properties of the adenosine triphosphatase activity associated with tightly coupled, time-stable mung bean (Phaseolus aureus Roxb.) mitochondria resemble those of intact animal mitochondria. Induction of adenosine triphosphatase activity by 2,4-dinitrophenol was inhibited by oligomycin, oxidizable substrates, and high concentrations of sucrose. Upon sonication, high rates of endogenous adenosine triphosphate hydrolysis resulted, an absolute requirement for Mg²⁺ was manifested, stimulation by 2,4-dinitrophenol and inhibition by sucrose were eliminated, but sensitivity to oligomycin was retained.     

Immunoreactive calcitonin in the intermediate lobe of the pituitary gland.

Immunoreactive-calcitonin was observed in all cells of the intermediate lobe of the rat pituitary gland. It may thus be a fragment of the ≥31, 000 daltons precursor molecule of adrenocorticotropin and β-lipotropin.