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Biomedical subjects

R Jahn

Publications and source records attributed to R Jahn.

209 records · Page 12Linked to original sources
PubMed1983

[Ring fractures of the base of the skull].

Besides complete ring fracture, also incomplete fractures open to the front, back, or side(s) are discussed on the basis of 61 ring fractures of the base of the skull. The fractures were found in casualties from traffic accidents (car passengers, cyclists and motorcyclists, pedestrians), after falls and other accidents. In traffic accidents, compression, traction, hyperextension, extreme lateral movements, and torsional forces can lead to ring fractures. In falls, compression and traction are the main forces. A fall in one plane is also capable of producing an incomplete ring fracture. Incomplete ring fractures may show lateral emphasis. The greater fracture length is found on the impact side (e.g., in falls). In contrast to complete ring fractures, incomplete ring fractures are compatible with longer survival times. Ring fractures are to be classified under direct fractures. This does not exclude the possibility that overall deformations of the skull with bursts can partly determine the course of the fracture.

Accidents, Traffic↗
PubMed1981

Phosphorylation of the same specific protein during amylase release evoked by beta-adrenergic or cholinergic agonists in rat and mouse parotid glands.

Stimulation of amylase secretion from the rat parotid gland by beta-adrenergic agonists is associated with a specific phosphorylation of three membrane-bound proteins designated as proteins I, II, and III [Jahn, R., Unger, C. & Söling, H. D. (1980) Eur. J. Biochem. 112, 345-352]. In contrast, stimuliation by carbachol induced significant phosphorylation of only protein I. This phosphorylation was low compared to isoproterenol-induced phosphorylation but corresponded to the smaller enhancement of amylase secretion. The mouse organ, however, is almost equally sensitive to beta-adrenergic and to cholinergic agonists. Incubation of mouse parotid gland slices with either 20 microM isoproterenol or 10 microM carbachol resulted in strong and comparable releases of amylase, which were accompanied by comparable phosphorylations of protein I. Proteins II and III were phosphorylated only in the presence of isoproterenol. Removal of external calcium by ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetate abolished the carbachol-induced release of amylase but not the phosphorylation of protein I. Isoproterenol-induced secretion of amylase and phosphorylation of proteins I, II, and III were not inhibited under these conditions. Amylase release stimulated by the ionophore A-23187 was accompanied by the phosphorylation of protein I. Two-dimensional electrophoresis revealed that the radioactive spot corresponding to protein I was located at the same position after cholinergic and after beta-adrenergic stimulation, indicating that both stimuli led to the phosphorylation of the same membrane-associated protein. These findings strongly support the view that the phosphorylation of protein I is an important step in the sequence of events leading from receptor activation to exocytosis.

Amylases↗
PubMed1980

Specific protein phosphorylation during stimulation of amylase secretion by beta-agonists or dibutyryl adenosine 3',5'-monophosphate in the rat parotid gland.

The present study was undertaken in order to examine the possible involvement of protein phosphorylation during beta-adrenergic stimulation in the rat parotid gland. Isolated parotid gland slices were stimulated by either isoproterenol or dibutyryl adenosine 3',5'-monophosphate (Bt2cAMP) in the presence or absence of propranolol. Amylase output was measured as a parameter for the degree of stimulation of secretion. Stimulation of secretion by either isoproterenol or Bt2AMP was associated with phosphorylation of three protein bands as revealed by sodium dodecylsulfate/polyacrylamide gel electrophoresis and autoradiography. The apparent molecular weights of the three proteins were 35,100 (protein I), 25,700 (protein II) and 20,400 (protein III). After cell fractionation by differential and gradient centrifugation, protein I was enriched in a light membrane fraction most likely corresponding to the plasma membrane as revealed by marker enzyme analysis. Proteins II and III were recovered in a denser fraction containing mainly mitochondria and rough microsomes. The effect of isoproterenol but not that of Bt2cAMP on phosphorylation of all three protein bands was completely abolished by propranolol. The different time course in the stimulation of amylase secretion by isoproterenol and Bt2cAMP respectively was reflected by corresponding differences in the time course of protein phosphorylation.

Amylases↗