Medizin - Open Access LMU - Teil 07/22 Archiv
250 Episoden
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A nuclear encoded mitochondrial heat-shock protein hsp60 is required for the assembly into oligomeric complexes of proteins imported into the mitochondrial matrix. hsp60 is a member of the 'chaperonin' class of protein factors, which include the Escherichia coli groEL protein and the Rubisco subunit-binding protein of chloroplasts
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Proteolytic degradation of receptor sites on the mitochondrial surface strongly reduces the efficiency of mitochondrial protein import. The remaining residual import still involves basic mechanisms of protein import, including: insertion of precursors into the outer membrane, requirement for ATP and a membrane potential, and translocation through contact sites between both membranes. The import of a chloroplast protein into isolated mitochondria which occurs with a low rate is not inhibited by a protease-pretreatment of mitochondria, indicating that this precursor only follows the bypass pathway. The low efficiency of bypass import suggests that this unspecific import does not disturb the uniqueness of mitochondrial protein composition. We conclude that mitochondrial protein import involves a series of steps in which receptor sites appear to be responsible for the specificity of protein uptake.
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GR43175, a selective 5-HT1-like agonist, was administered as oral dispersible tablets in an open, uncontrolled dose-ranging study to assess its efficacy as an agent for acute migraine. Nine patients, all with well established attacks, were assessed for changes in severity of headache and associated symptoms over 2 h. Drug absorption was compared during and between attacks in five patients. Doses of 140 mg and 280 mg resulted in complete relief of all symptoms within 2 h. Treatment was well tolerated in all patients.
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