Erratic deposition of agrin during the formation of Xenopus neuromuscular junctions in culture
Article Abstract:
The molecules which organize synapses were studied. The results indicated that agrin deposits on muscle fibers came mainly from remote cells through extracellular fluids. Agrins appeared to be regulatory proteins contributing to the normal elaboration of the extracellular matrices (ECM) near various cell types. Agrin deposition does not seem always to be required for neuromuscular junctions to form. Agrin appears to be a protease inhibitor. Muscle ECM elaboration may just depend on several endogenous ECM-binding protease inhibitors being available. A Xenopus culture was used in the study.
Publication Name: Developmental Biology
Subject: Biological sciences
ISSN: 0012-1606
Year: 1995
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Former neuritic pathways containing endogenous neural agrin have high synaptogenic activity
Article Abstract:
A study of the efficiency of former neuritic pathways in inducing variations in the normal acetylcholine receptor (AChR) and cholinesterase (ChE) distribution during nerve-muscle synaptogenesis in Xenopus reveals that the preferential positioning of AChR and ChE on embryonic muscle cells is favored by the pathways that are agrin-positive, while the agrin-negative pathways do not stimulate the preferential positioning. The restricted potential of muscle cells to accumulate AChR is indicated by the saturation process that determines the length of AChR accumulation along the agrin pathway.
Publication Name: Developmental Biology
Subject: Biological sciences
ISSN: 0012-1606
Year: 1995
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Brefeldin A provokes indirect activation of cdc2 kinase (MPF) in Xenopus oocytes, resulting in meiotic cell division
Article Abstract:
Brefeldin A is a fungal metabolite which acts on cell cycle regulatory elements. It indirectly activates cdc2 protein kinase in Xenopus oocytes and meiosis progresses till metaphase II. The amount of Cdc2 protein kinase, M-phase factor, cyclic B, MAP kinase and changes in the protein synthesis in oocytes treated with brefeldin A are similar to that in progesterone-induced oocytes. The maturation effect of brefeldin A is affected by drugs which affect cAMP metabolism. Brefeldin A disrupts the Golgi apparatus' protein transport.
Publication Name: Developmental Biology
Subject: Biological sciences
ISSN: 0012-1606
Year: 1995
User Contributions:
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