Article Abstract:
A study was conducted on nonmuscle myosin heavy chain isoform expression in several mice tissues during development using anti-human platelet myosin antibodies, anti-peptide IIA and anti-peptide IIB. Results revealed that tissue-specific changes occurred in the tissues' relative isoform concentrations. A single band (MIIB2) was found to be stained by anti-peptide IIB antibodies. This band, however, migrated more slowly compared with the band stained by anti-platelet myosin antibodies and anti-peptide IIA. MIIB2 was also found to decrease after birth in the thymus and to disappear rapidly in the liver, together with macrophage-type isoforms.
User Contributions:
Comment about this article or add new information about this topic:
Article Abstract:
Immunoblot analysis and immunocytochemistry techniques show that expression of myosin-IA (MIA) and myosin-IB (MIB) from Drosophila melanogaster is correlated with brush border cytoskeleton within the alimentary canal. In the larval gut, MIA is localized to the subapical terminal web domain whereas MIB is localized to the apical microvillar domain. In the adult gut, MIA also becomes predominant in the apical position in addition to its position in the web domain, while MIB attains a position in the egg chambers of the somatic follicle cells.
User Contributions:
Comment about this article or add new information about this topic:
Article Abstract:
Increased activity of proteolytic enzymes and excess laminin production are responsible for the defect in cerebellar development seen in the weaver mouse mutant. The weaver mouse mutant contains a mutation on chromosome 16 that causes abnormal cerebellar development because the granule neurons fail to migrate. Increased degradation of laminin produces an accumulation of the B2 chain of laminin, which is neurotoxic at high levels.
User Contributions:
Comment about this article or add new information about this topic: