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  • 1
    Electronic Resource
    Electronic Resource
    Effects of carvedilol on serum lipids in hypertensive and normotensive subjects (1990)
    Springer
    European journal of clinical pharmacology 38 (1990), S. S139 
    Details
    ISSN: 1432-1041
    Keywords: carvedilol ; serum lipid metabolism ; hypertension ; normotension
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary The effects of carvedilol (an α · β-blocker) on lipid metabolism were assessed in addition to its hypotensive effect. The subjects were 18 men and 18 women, 20 with hypertension and 16 normotensives with other conditions requiring carvedilol treatment. They were aged from 31 to 79 years and were given a daily dose of 5–20 mg carvedilol (average, 9.7 mg/day) for 12 weeks. Significant falls were seen in blood pressure and heart rate after 12 weeks in the hypertensive subjects (mean ± SE) (systolic: from 164 ± 2 to 141 ± 2 mm Hg,P 〈 0.001; diastolic: from 98 ± 1 to 85 ± 2 mm Hg,P 〈 0.001; heart rate: from 71 to 65 beats/min,P 〈 0.001). Smaller changes in blood pressure and heart rate were seen in the normotensive subjects, with the fall in systolic pressure being significant (from 143±3 to 135 ± 2 mm Hg,P 〈 0.01). There were no significant changes in the overall serum total cholesterol, triglycerides, high-density lipoprotein (HDL) cholesterol, and phospholipid levels. In the subgroup with a pretreatment serum triglyceride level of 〉 150 mg/dl, a significant fall of 52.1 mg/dl was seen (P 〈 0.05). Lipoprotein analysis showed a significant fall in α-lipoprotein levels (P 〈 0.05). The atherogenic index did not change significantly, and it was concluded that carvedilol was an effective antihypertensive agent that produced no adverse effects and possibly had beneficial effects on lipid metabolism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01409484
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  • 2
    Electronic Resource
    Electronic Resource
    Localization of phosphatase activities on mouse teratocarcinoma embryoid bodies
    Amsterdam : Elsevier
    Experimental Cell Research 140 (1982), S. 427-429 
    Details
    ISSN: 0014-4827
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0014-4827(82)90133-1
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  • 3
    Electronic Resource
    Electronic Resource
    Zur Ultrastruktur der Kristalloide in den Spermatogonien und Sertolizellen normaler Kinderhoden (1974)
    Springer
    Cellular and molecular life sciences 30 (1974), S. 364-366 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The fine structure of the crystalloid in spermatogonia has been studied in biopsies from 18 children and compared with the crystalloid in Sertoli cells. The crystalloid ofLubarsch can be seen already in 4-month-old children and it grows larger with age. Furthemore we have discussed the origin of spermatogonial crystalloids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01921666
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  • 4
    Electronic Resource
    Electronic Resource
    Internalization of ecto-ATPase activity in human neutrophils upon stimulation with phorbol ester or formyl peptide (1997)
    Springer
    Histochemistry and cell biology 107 (1997), S. 353-363 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  We have demonstrated the alteration of the localization of ecto-ATPase activity in human neutrophils after stimulation with phorbol myristate acetate or N-formylmethionyl-leucyl-phenylalanine using a cerium-based cytochemical method. In unstimulated cells, the enzyme activity was observed on the plasma membrane. Both the diazonium salt of sulfanilic acid and diethylpyrocarbonate inhibited the production of the reaction precipitates. Within 2–3 min of stimulation, cells developed cytoplasmic projections (ruffles). The ecto-ATPase activity on the plasma membrane of these ruffles was, however, weaker than that at the non-ruffle-forming side. The ruffle-forming side (RFS) was also the site where elongated tubular structures positive for the enzyme reaction tended to concentrate and associated with the plasma membrane. The enzyme activity was also detected in intracellular compartments, which appeared predominantly in the RFS concomitantly with the disappearance of the enzyme activity from the plasma membrane. Using a series of thick sections and computer-assisted three-dimensional reconstruction, the enzyme reaction-positive internalized membranes were visualized as a complicated mass formed by enzyme reaction-positive vesicles which gathered together and were, at least in part, interconnected. The present results indicate that the detected enzyme reaction is a product of the ecto-ATPase activity, and that RFS possibly serves the membrane flow with respect to endocytosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050121
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  • 5
    Electronic Resource
    Electronic Resource
    Intracellular dynamics of alkaline phosphatase-containing granules in electropermeabilized human neutrophils (1998)
    Springer
    Histochemistry and cell biology 110 (1998), S. 395-406 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Human neutrophils possess alkaline phosphatase-containing intracellular granules which are upregulated to the cell surface upon stimulation. The mechanism that governs the intracellular dynamics of these granules is, however, poorly understood. The aim of the present study was to investigate the possible participation of GTP-binding proteins in the reorganization and exocytosis of the alkaline phosphatase-containing granules using electropermeabilized cells. Biochemical assays using intact neutrophils showed that the alkaline phosphatase activity was upregulated and exocytosed into the extracellular space upon stimulation with AlF4 – and N-formyl peptide. This upregulation was inhibited by treatment of cells with pertussis toxin and botulinum toxin. Alkaline phosphatase activity was also upregulated in electropermeabilized cells stimulated with guanosine 5′-O-(3-thiotriphosphate) (GTPγS), but not with guanosine 5′-O-(2-thiodiphosphate) (GDPβS). Cytochemically, alkaline phosphatase-containing granules were dispersed throughout the cytoplasm in unstimulated electropermeabilized neutrophils. Upon stimulation with GTPγS, but not with GDPβS, these granules fused to form elongated tubular structures which eventually became associated with the plasma membrane. Nocodazole disturbed the reorganization of the alkaline phosphatase-containing granules in cells stimulated with GTPγS. The results from this study indicate that GTP-binding proteins participate in the reorganization and exocytosis of alkaline phosphatase-containing granules associated with the microtubules in electropermeabilized human neutrophils.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050300
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  • 6
    Electronic Resource
    Electronic Resource
    Ultracytochemical demonstration of ouabain-sensitive, K+-dependent,p-nitrophenylphosphatase (Na-K ATPase) activity in cat facial nerve (1994)
    Springer
    European archives of oto-rhino-laryngology and head & neck 251 (1994), S. 238-240 
    Details
    ISSN: 1434-4726
    Keywords: Potassium-dependent ; p-nitrophenylphosphatase ; Facial nerve ; Cerium-based-enzymology ; Ultracytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Ouabain-sensitive, K+-dependent,p-nitrophenylphosphatase (K-NPPase) is the second dephosphorylative property of the Na-K ATPase complex. Localization of its activity in the horizontal portion of the facial nerve in 11 normal cats was studied ultracytochemically using a cerium-based method. The fine granular reaction product of the K-NPPase activity was observed on the cytoplasmic side of the axolemma of the axon cylinder. Enzyme activity was also detected on the cytoplasmic side of the plasma membrane of Schmidt-Lanterman incisures and nodes of Ranvier. No reaction product was detected on the periaxonal and outermost plasma membrane of Schwann cells and in the myelin sheath. In control tissue samples, enzyme activity was almost completely inhibited by 10 mM ouabain, and no reaction was noted in medium without K+. The present findings indicate that localization of Na-K ATPase in the cat facial nerve simulates that of other peripheral and cranial nerves.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00628431
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  • 7
    Electronic Resource
    Electronic Resource
    Ultrastructural investigations of the palisade-shaped nerve fiber terminals of the normal hairs of rat's snout (1974)
    Springer
    Cell & tissue research 147 (1974), S. 259-269 
    Details
    ISSN: 1432-0878
    Keywords: Nerve endings ; Hair ; Rat ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Palisade-shaped nerve endings of the small normal hairs of the rat snout were examined with the electron microscope (fixation by perfusion). The terminals are located inside the ‘glassy membrane’ in the area of the neck of the hair root. The 10–20 radially arranged terminal axons are in direct contact with the basement membrane of the epithelium of the external root sheath. The axons are surrounded on all sides by leaf-shaped processes of the Schwann cells. The surfaces of these cell processes are marked by numerous vesicle-like invaginations (approx. 1000 Å dia.). Transverse sections from several areas of the palisadeshaped nerve endings are compared with longitudinal sections. In the upper area ‘empty’ vesicles (approx. 500–600 Å in diameter) occur, along with electron-dense vesicles (approx. 800–1100 Å in diameter); in the middle area, the axons are distended and contain accumulations of mitochondria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00582800
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