» Articles » PMID: 23558932

Myosin Va is Developmentally Regulated and Expressed in the Human Cerebellum from Birth to Old Age

Overview
Date 2013 Apr 6
PMID 23558932
Authors
Affiliations
Soon will be listed here.
Abstract

Myosin Va functions as a processive, actin-based motor molecule highly enriched in the nervous system, which transports and/or tethers organelles, vesicles, and mRNA and protein translation machinery. Mutation of myosin Va leads to Griscelli disease that is associated with severe neurological deficits and a short life span. Despite playing a critical role in development, the expression of myosin Va in the central nervous system throughout the human life span has not been reported. To address this issue, the cerebellar expression of myosin Va from newborns to elderly humans was studied by immunohistochemistry using an affinity-purified anti-myosin Va antibody. Myosin Va was expressed at all ages from the 10th postnatal day to the 98 th year of life, in molecular, Purkinje and granular cerebellar layers. Cerebellar myosin Va expression did not differ essentially in localization or intensity from childhood to old age, except during the postnatal developmental period. Structures resembling granules and climbing fibers in Purkinje cells were deeply stained. In dentate neurons, long processes were deeply stained by anti-myosin Va, as were punctate nuclear structures. During the first postnatal year, myosin Va was differentially expressed in the external granular layer (EGL). In the EGL, proliferating prospective granule cells were not stained by anti-myosin Va antibody. In contrast, premigratory granule cells in the EGL stained moderately. Granule cells exhibiting a migratory profile in the molecular layer were also moderately stained. In conclusion, neuronal myosin Va is developmentally regulated, and appears to be required for cerebellar function from early postnatal life to senescence.

References
1.
Espindola F, Espreafico E, COELHO M, Martins A, Costa F, Mooseker M . Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: a novel calmodulin-binding myosin. J Cell Biol. 1992; 118(2):359-68. PMC: 2290054. DOI: 10.1083/jcb.118.2.359. View

2.
Rivas R, Hatten M . Motility and cytoskeletal organization of migrating cerebellar granule neurons. J Neurosci. 1995; 15(2):981-9. PMC: 6577828. View

3.
Pastural E, Ersoy F, Yalman N, Wulffraat N, Grillo E, Ozkinay F . Two genes are responsible for Griscelli syndrome at the same 15q21 locus. Genomics. 2000; 63(3):299-306. DOI: 10.1006/geno.1999.6081. View

4.
Hayasaka S, Takagishi Y, Oda S, Wakasugi N, Mikoshiba K, Inouye M . Endoplasmic reticulum is missing in dendritic spines of Purkinje cells of the ataxic mutant rat. Brain Res. 1996; 714(1-2):226-30. DOI: 10.1016/0006-8993(95)01560-4. View

5.
Trybus K . Myosin V from head to tail. Cell Mol Life Sci. 2008; 65(9):1378-89. PMC: 2613318. DOI: 10.1007/s00018-008-7507-6. View