Developmental regulation of Thy 1.2 rate of synthesis in the mouse cerebellum
Thy 1.2 is a well‐known major cell surface glycoprotein of the central nervous system (CNS). However, the regulation of the expression of this molecule as well as its function are yet to be determined. To approach these problems we studied the synthesis of the molecule in the developing cerebellum o...
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1995
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03604012_v42_n2_p220_Radrizzani http://hdl.handle.net/20.500.12110/paper_03604012_v42_n2_p220_Radrizzani |
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paper:paper_03604012_v42_n2_p220_Radrizzani2023-06-08T15:34:45Z Developmental regulation of Thy 1.2 rate of synthesis in the mouse cerebellum Radrizzani Helguera, Martín Carminatti, Héctor Purkinje cell staggerer mutant synaptogenesis synthesis Thy 1 glycoprotein methionine monoclonal antibody sepharose thy 1 antigen animal cell article cerebellum dendritic spine development mouse mutation newborn nonhuman priority journal protein synthesis purkinje cell synaptogenesis synaptosome Animal Antigens, Thy-1 Cerebellum Gene Expression Regulation, Developmental Mannose Methionine Mice Mice, Inbred C57BL Mice, Neurologic Mutants Nerve Tissue Proteins Organ Culture Purkinje Cells Subcellular Fractions Synaptosomes Translation, Genetic Thy 1.2 is a well‐known major cell surface glycoprotein of the central nervous system (CNS). However, the regulation of the expression of this molecule as well as its function are yet to be determined. To approach these problems we studied the synthesis of the molecule in the developing cerebellum of wild‐type and staggerer mutant mice. We found the appearance of a [35S]‐methionine‐labeled band detected with specific Sepharose 4B‐bound monoclonal antibodies (Mabs). The Thy 1.2 activity increases progressively from postnatal day 9 (P9), reaching the highest rate at P12, subsequently decreasing sharply at P13, and remaining relatively low up to P16 in the wild type. Comparison of these data to the rates of total protein synthesis reveals a selective developmental regulation of Thy 1.2 expression, at least at the translational level. This correlates quite well with the timing of synaptic stabilization between parallel fibers and Purkinje cell dendritic spines. Furthermore, at P12 Thy 1.2 protein is preferentially located in the synaptosomal fraction. The parallel fiber:Purkinje cell synapsis is not stabilized in the staggerer mutant mouse. At P12 Thy 1.2 synthesis is 30% of the wild type, indicating that the translational regulation of Thy 1.2 is altered in the staggerer mutation. © 1995 Wiley‐Liss, Inc. Copyright © 1995 Wiley‐Liss, Inc. Fil:Radrizzani, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Carminatti, H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1995 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03604012_v42_n2_p220_Radrizzani http://hdl.handle.net/20.500.12110/paper_03604012_v42_n2_p220_Radrizzani |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Purkinje cell staggerer mutant synaptogenesis synthesis Thy 1 glycoprotein methionine monoclonal antibody sepharose thy 1 antigen animal cell article cerebellum dendritic spine development mouse mutation newborn nonhuman priority journal protein synthesis purkinje cell synaptogenesis synaptosome Animal Antigens, Thy-1 Cerebellum Gene Expression Regulation, Developmental Mannose Methionine Mice Mice, Inbred C57BL Mice, Neurologic Mutants Nerve Tissue Proteins Organ Culture Purkinje Cells Subcellular Fractions Synaptosomes Translation, Genetic |
| spellingShingle |
Purkinje cell staggerer mutant synaptogenesis synthesis Thy 1 glycoprotein methionine monoclonal antibody sepharose thy 1 antigen animal cell article cerebellum dendritic spine development mouse mutation newborn nonhuman priority journal protein synthesis purkinje cell synaptogenesis synaptosome Animal Antigens, Thy-1 Cerebellum Gene Expression Regulation, Developmental Mannose Methionine Mice Mice, Inbred C57BL Mice, Neurologic Mutants Nerve Tissue Proteins Organ Culture Purkinje Cells Subcellular Fractions Synaptosomes Translation, Genetic Radrizzani Helguera, Martín Carminatti, Héctor Developmental regulation of Thy 1.2 rate of synthesis in the mouse cerebellum |
| topic_facet |
Purkinje cell staggerer mutant synaptogenesis synthesis Thy 1 glycoprotein methionine monoclonal antibody sepharose thy 1 antigen animal cell article cerebellum dendritic spine development mouse mutation newborn nonhuman priority journal protein synthesis purkinje cell synaptogenesis synaptosome Animal Antigens, Thy-1 Cerebellum Gene Expression Regulation, Developmental Mannose Methionine Mice Mice, Inbred C57BL Mice, Neurologic Mutants Nerve Tissue Proteins Organ Culture Purkinje Cells Subcellular Fractions Synaptosomes Translation, Genetic |
| description |
Thy 1.2 is a well‐known major cell surface glycoprotein of the central nervous system (CNS). However, the regulation of the expression of this molecule as well as its function are yet to be determined. To approach these problems we studied the synthesis of the molecule in the developing cerebellum of wild‐type and staggerer mutant mice. We found the appearance of a [35S]‐methionine‐labeled band detected with specific Sepharose 4B‐bound monoclonal antibodies (Mabs). The Thy 1.2 activity increases progressively from postnatal day 9 (P9), reaching the highest rate at P12, subsequently decreasing sharply at P13, and remaining relatively low up to P16 in the wild type. Comparison of these data to the rates of total protein synthesis reveals a selective developmental regulation of Thy 1.2 expression, at least at the translational level. This correlates quite well with the timing of synaptic stabilization between parallel fibers and Purkinje cell dendritic spines. Furthermore, at P12 Thy 1.2 protein is preferentially located in the synaptosomal fraction. The parallel fiber:Purkinje cell synapsis is not stabilized in the staggerer mutant mouse. At P12 Thy 1.2 synthesis is 30% of the wild type, indicating that the translational regulation of Thy 1.2 is altered in the staggerer mutation. © 1995 Wiley‐Liss, Inc. Copyright © 1995 Wiley‐Liss, Inc. |
| author |
Radrizzani Helguera, Martín Carminatti, Héctor |
| author_facet |
Radrizzani Helguera, Martín Carminatti, Héctor |
| author_sort |
Radrizzani Helguera, Martín |
| title |
Developmental regulation of Thy 1.2 rate of synthesis in the mouse cerebellum |
| title_short |
Developmental regulation of Thy 1.2 rate of synthesis in the mouse cerebellum |
| title_full |
Developmental regulation of Thy 1.2 rate of synthesis in the mouse cerebellum |
| title_fullStr |
Developmental regulation of Thy 1.2 rate of synthesis in the mouse cerebellum |
| title_full_unstemmed |
Developmental regulation of Thy 1.2 rate of synthesis in the mouse cerebellum |
| title_sort |
developmental regulation of thy 1.2 rate of synthesis in the mouse cerebellum |
| publishDate |
1995 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03604012_v42_n2_p220_Radrizzani http://hdl.handle.net/20.500.12110/paper_03604012_v42_n2_p220_Radrizzani |
| work_keys_str_mv |
AT radrizzanihelgueramartin developmentalregulationofthy12rateofsynthesisinthemousecerebellum AT carminattihector developmentalregulationofthy12rateofsynthesisinthemousecerebellum |
| _version_ |
1768545419266097152 |