Abstract
The levels of three different microtubule-associated proteins (MAP1, -2, and -3) in brain were found to undergo large changes during postnatal development. MAP1 was barely detectable at birth but thereafter steadily increased, reaching adult levels by postnatal day 20 (P20). Both MAP2 and MAP3 showed differential expression patterns of their component peptides. At birth, MAP2 was represented by the smaller of two Mr 280,000 peptides (MAP2b) and three antigenically related Mr 70,000 peptides. The larger of the Mr 280,000 peptides (MAP2a) first appeared between P10 and P20, and the Mr 70,000 components disappeared at the same time. Of the two MAP3 peptides, the larger (MAP3a) was present in the late embryo, several days before MAP3b appeared. Between P10 and P20, both MAP3 components underwent a striking decrease in abundance (a factor of 10), which correlated with their disappearance from all neuronal compartments except neurofilament-containing axons. These developmental changes in expression are different and characteristic for each of the three MAPs, yet in each case they are detectable in brain homogenates, indicating that they occur concurrently throughout the brain.
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- Bernhardt R., Huber G., Matus A. Differences in the developmental patterns of three microtubule-associated proteins in the rat cerebellum. J Neurosci. 1985 Apr;5(4):977–991. doi: 10.1523/JNEUROSCI.05-04-00977.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bernhardt R., Matus A. Light and electron microscopic studies of the distribution of microtubule-associated protein 2 in rat brain: a difference between dendritic and axonal cytoskeletons. J Comp Neurol. 1984 Jun 20;226(2):203–221. doi: 10.1002/cne.902260205. [DOI] [PubMed] [Google Scholar]
- Binder L. I., Frankfurter A., Kim H., Caceres A., Payne M. R., Rebhun L. I. Heterogeneity of microtubule-associated protein 2 during rat brain development. Proc Natl Acad Sci U S A. 1984 Sep;81(17):5613–5617. doi: 10.1073/pnas.81.17.5613. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bloom G. S., Schoenfeld T. A., Vallee R. B. Widespread distribution of the major polypeptide component of MAP 1 (microtubule-associated protein 1) in the nervous system. J Cell Biol. 1984 Jan;98(1):320–330. doi: 10.1083/jcb.98.1.320. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Burgoyne R. D., Cumming R. Ontogeny of microtubule-associated protein 2 in rat cerebellum: differential expression of the doublet polypeptides. Neuroscience. 1984 Jan;11(1):156–167. doi: 10.1016/0306-4522(84)90220-3. [DOI] [PubMed] [Google Scholar]
- Caceres A., Binder L. I., Payne M. R., Bender P., Rebhun L., Steward O. Differential subcellular localization of tubulin and the microtubule-associated protein MAP2 in brain tissue as revealed by immunocytochemistry with monoclonal hybridoma antibodies. J Neurosci. 1984 Feb;4(2):394–410. doi: 10.1523/JNEUROSCI.04-02-00394.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Daniels M. P. Colchicine inhibition of nerve fiber formation in vitro. J Cell Biol. 1972 Apr;53(1):164–176. doi: 10.1083/jcb.53.1.164. [DOI] [PMC free article] [PubMed] [Google Scholar]
- De Camilli P., Miller P. E., Navone F., Theurkauf W. E., Vallee R. B. Distribution of microtubule-associated protein 2 in the nervous system of the rat studied by immunofluorescence. Neuroscience. 1984 Apr;11(4):817–846. [PubMed] [Google Scholar]
- Dentler W. L., Granett S., Rosenbaum J. L. Ultrastructural localization of the high molecular weight proteins associated with in vitro-assembled brain microtubules. J Cell Biol. 1975 Apr;65(1):237–241. doi: 10.1083/jcb.65.1.237. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fellous A., Francon J., Lennon A. M., Nunez J. Microtubule assembly in vitro. Purification of assembly-promoting factors. Eur J Biochem. 1977 Aug 15;78(1):167–174. doi: 10.1111/j.1432-1033.1977.tb11726.x. [DOI] [PubMed] [Google Scholar]
- Hawkes R., Niday E., Gordon J. A dot-immunobinding assay for monoclonal and other antibodies. Anal Biochem. 1982 Jan 1;119(1):142–147. doi: 10.1016/0003-2697(82)90677-7. [DOI] [PubMed] [Google Scholar]
- Herzog W., Weber K. Fractionation of brain microtubule-associated proteins. Isolation of two different proteins which stimulate tubulin polymerization in vitro. Eur J Biochem. 1978 Dec 1;92(1):1–8. doi: 10.1111/j.1432-1033.1978.tb12716.x. [DOI] [PubMed] [Google Scholar]
- Huber G., Alaimo-Beuret D., Matus A. MAP3: characterization of a novel microtubule-associated protein. J Cell Biol. 1985 Feb;100(2):496–507. doi: 10.1083/jcb.100.2.496. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Huber G., Matus A. Differences in the cellular distributions of two microtubule-associated proteins, MAP1 and MAP2, in rat brain. J Neurosci. 1984 Jan;4(1):151–160. doi: 10.1523/JNEUROSCI.04-01-00151.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Huber G., Matus A. Immunocytochemical localization of microtubule-associated protein 1 in rat cerebellum using monoclonal antibodies. J Cell Biol. 1984 Feb;98(2):777–781. doi: 10.1083/jcb.98.2.777. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Karr T. L., White H. D., Purich D. L. Characterization of brain microtubule proteins prepared by selective removal of mitochondrial and synaptosomal components. J Biol Chem. 1979 Jul 10;254(13):6107–6111. [PubMed] [Google Scholar]
- Matus A., Huber G., Bernhardt R. Neuronal microdifferentiation. Cold Spring Harb Symp Quant Biol. 1983;48(Pt 2):775–782. doi: 10.1101/sqb.1983.048.01.079. [DOI] [PubMed] [Google Scholar]
- Matus A., Pehling G., Ackermann M., Maeder J. Brain postsynaptic densities: the relationship to glial and neuronal filaments. J Cell Biol. 1980 Nov;87(2 Pt 1):346–359. doi: 10.1083/jcb.87.2.346. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Murphy D. B., Borisy G. G. Association of high-molecular-weight proteins with microtubules and their role in microtubule assembly in vitro. Proc Natl Acad Sci U S A. 1975 Jul;72(7):2696–2700. doi: 10.1073/pnas.72.7.2696. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Seeds N. W., Gilman A. G., Amano T., Nirenberg M. W. Regulation of axon formation by clonal lines of a neural tumor. Proc Natl Acad Sci U S A. 1970 May;66(1):160–167. doi: 10.1073/pnas.66.1.160. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sloboda R. D., Rudolph S. A., Rosenbaum J. L., Greengard P. Cyclic AMP-dependent endogenous phosphorylation of a microtubule-associated protein. Proc Natl Acad Sci U S A. 1975 Jan;72(1):177–181. doi: 10.1073/pnas.72.1.177. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Towbin H., Gordon J. Immunoblotting and dot immunobinding--current status and outlook. J Immunol Methods. 1984 Sep 4;72(2):313–340. doi: 10.1016/0022-1759(84)90001-2. [DOI] [PubMed] [Google Scholar]
- Weingarten M. D., Lockwood A. H., Hwo S. Y., Kirschner M. W. A protein factor essential for microtubule assembly. Proc Natl Acad Sci U S A. 1975 May;72(5):1858–1862. doi: 10.1073/pnas.72.5.1858. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wiche G., Briones E., Hirt H., Krepler R., Artlieb U., Denk H. Differential distribution of microtubule-associated proteins MAP-1 and MAP-2 in neurons of rat brain and association of MAP-1 with microtubules of neuroblastoma cells (clone N2A). EMBO J. 1983;2(11):1915–1920. doi: 10.1002/j.1460-2075.1983.tb01679.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yamada K. M., Spooner B. S., Wessells N. K. Axon growth: roles of microfilaments and microtubules. Proc Natl Acad Sci U S A. 1970 Aug;66(4):1206–1212. doi: 10.1073/pnas.66.4.1206. [DOI] [PMC free article] [PubMed] [Google Scholar]