scholarly journals Studies on the expression of the microtubule-associated protein, tau, during mouse brain development, with newly isolated complementary DNA probes.

1984 ◽  
Vol 98 (3) ◽  
pp. 1090-1097 ◽  
Author(s):  
D G Drubin ◽  
D Caput ◽  
M W Kirschner
Keyword(s):  
Brain Development ◽  
Mouse Brain ◽  
Tau Protein ◽  
Bovine Brain ◽  
In Vitro Translation ◽  
Embryonic Mouse ◽  
Complementary Dna ◽  
Mouse Brain Development

Tau protein is a collection of closely related polypeptides that associate with microtubules in vivo and stimulate their assembly in vitro. Using an affinity-purified antiserum against bovine brain tau protein, we found that the number and amount of tau polypeptides changes dramatically during mouse brain development. The different forms appear to result from changes in tau mRNA since in vitro translation products reflect the qualitative and quantitative changes found in vivo. To study the mRNA and genomic complexity of tau protein, we used tau mRNA, purified from polysomes with tau antiserum, to isolate embryonic mouse tau complementary DNA clones. With these probes we have determined that embryonic tau protein is translated from a 6-kb mRNA that persists throughout brain development.

scholarly journals A chronological expression profile of gene activity during embryonic mouse brain development

2013 ◽  
Vol 24 (11-12) ◽  
pp. 459-472 ◽  
Author(s):  
P. Goggolidou ◽  
S. Soneji ◽  
N. Powles-Glover ◽  
D. Williams ◽  
S. Sethi ◽  
...  
Keyword(s):  
Brain Development ◽  
Mouse Brain ◽  
Expression Profile ◽  
Gene Activity ◽  
Embryonic Mouse ◽  
Mouse Brain Development

Transcriptome and proteome analysis of early embryonic mouse brain development

PROTEOMICS ◽  
2008 ◽  
Vol 8 (6) ◽  
pp. 1257-1265 ◽  
Author(s):  
Daniela Hartl ◽  
Martin Irmler ◽  
Irmgard Römer ◽  
Michael T. Mader ◽  
Lei Mao ◽  
...  
Keyword(s):  
Brain Development ◽  
Mouse Brain ◽  
Proteome Analysis ◽  
Embryonic Mouse ◽  
Mouse Brain Development

scholarly journals Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains.

1989 ◽  
Vol 9 (4) ◽  
pp. 1381-1388 ◽  
Author(s):  
A Himmler ◽  
D Drechsel ◽  
M W Kirschner ◽  
D W Martin
Keyword(s):  
Polyclonal Antibodies ◽  
Bovine Brain ◽  
Tau Proteins ◽  
In Vitro Translation ◽  
Cdna Clones ◽  
Terminal Domain ◽  
Binding Domains ◽  
Terminal Domains

Tau proteins consist of a family of proteins, heterogeneous in size, which associate with microtubules in vivo and are induced during neurite outgrowth. In humans, tau is one of the major components of the pathognomonic neurofibrillary tangles in Alzheimer's disease brain. Screening of a cDNA library prepared from bovine brain led to the isolation of several cDNA clones encoding tau proteins with different N termini and differing by insertions or deletions, suggesting differential splicing of the tau transcripts. One of the N-terminal domains and the repeated C-terminal domain of the encoded tau proteins are recognized by polyclonal antibodies to bovine tau. The bovine tau proteins are highly homologous to murine and human tau, especially within the repeated C-terminal domain. Compared with murine and human tau, bovine tau contains the insertion of three longer segments, one of which is an additional characteristic repeat. Portions of tau proteins generated by in vitro translation were used to show that these repeats represent tubulin-binding domains, two of which are sufficient to bind to microtubules assembled from purified tubulin in the presence of taxol.

scholarly journals High-Throughput, High-Frequency 3-D Ultrasound for in Utero Analysis of Embryonic Mouse Brain Development

2013 ◽  
Vol 39 (12) ◽  
pp. 2321-2332 ◽  
Author(s):  
Orlando Aristizábal ◽  
Jonathan Mamou ◽  
Jeffrey A. Ketterling ◽  
Daniel H. Turnbull
Keyword(s):  
Brain Development ◽  
Mouse Brain ◽  
High Throughput ◽  
High Frequency ◽  
In Utero ◽  
Embryonic Mouse ◽  
Mouse Brain Development

Tau consists of a set of proteins with repeated C-terminal microtubule-binding domains and variable N-terminal domains

1989 ◽  
Vol 9 (4) ◽  
pp. 1381-1388
Author(s):  
A Himmler ◽  
D Drechsel ◽  
M W Kirschner ◽  
D W Martin
Keyword(s):  
Polyclonal Antibodies ◽  
Bovine Brain ◽  
Tau Proteins ◽  
In Vitro Translation ◽  
Cdna Clones ◽  
Terminal Domain ◽  
Binding Domains ◽  
Terminal Domains

Tau proteins consist of a family of proteins, heterogeneous in size, which associate with microtubules in vivo and are induced during neurite outgrowth. In humans, tau is one of the major components of the pathognomonic neurofibrillary tangles in Alzheimer's disease brain. Screening of a cDNA library prepared from bovine brain led to the isolation of several cDNA clones encoding tau proteins with different N termini and differing by insertions or deletions, suggesting differential splicing of the tau transcripts. One of the N-terminal domains and the repeated C-terminal domain of the encoded tau proteins are recognized by polyclonal antibodies to bovine tau. The bovine tau proteins are highly homologous to murine and human tau, especially within the repeated C-terminal domain. Compared with murine and human tau, bovine tau contains the insertion of three longer segments, one of which is an additional characteristic repeat. Portions of tau proteins generated by in vitro translation were used to show that these repeats represent tubulin-binding domains, two of which are sufficient to bind to microtubules assembled from purified tubulin in the presence of taxol.

scholarly journals Studies on myelin-basic-protein methylation during mouse brain development

1986 ◽  
Vol 240 (2) ◽  
pp. 471-479 ◽  
Author(s):  
L P Chanderkar ◽  
W K Paik ◽  
S Kim
Keyword(s):  
Brain Development ◽  
Myelin Basic Protein ◽  
Mouse Brain ◽  
Basic Protein ◽  
Relative Rate ◽  
Polyacrylamide Gel Electrophoresis ◽  
High Ratio ◽  
Major Species ◽  
Mouse Brain Development

The synthesis and methylation in vivo of myelin basic protein (MBP) during the mouse brain development has been investigated. When mice ranging in age from 13 to 60 days were injected intracerebrally with L-[methyl-3H]methionine, the incorporation of radioactivity into MBP isolated from youngest brain was found to be the highest and declined progressively in mature brains. This pattern of radioactivity incorporation was inversely correlated with the total amount of MBP in the brains, suggesting a higher ratio of MBP methylation to synthesis in younger brain. To differentiate the relative rate of protein synthesis and methylation, animals were given intracerebral injections of a L-[methyl-3H]methionine and L-[35S]methionine mixture and the ratio of 3H/35S (methylation index) was determined. The ratios in the isolated MBP fractions were higher than those of ‘acid extracts’ and ‘breakthrough’ fractions, with a maximal ratio in the youngest brain. This high ratio was well correlated with the higher protein methylase I (PMI) activity in younger brains. The MBP fractions were further separated on SDS/polyacrylamide-gel electrophoresis into several species with apparent Mr ranging from 32,400 to 14,500. The results indicated that each protein species accumulated at a characteristic rate as a function of age. The high-Mr (32,400) species was predominant in younger brain, whereas the smaller MBP was the major species in older brain tissue. The importance of this developmental pattern of MBP synthesis and methylation is discussed in relation to PMI activity.

XLF/Cernunnos Loss Impairs Mouse Brain Development by Altering Symmetric Proliferative Divisions of Neural Progenitors

2020 ◽  
Author(s):  
Amandine Bery ◽  
Olivier Etienne ◽  
Laura Mouton ◽  
Sofiane Mokrani ◽  
Christine Granotier-Beckers ◽  
...  
Keyword(s):  
Brain Development ◽  
Mouse Brain ◽  
Neural Progenitors ◽  
Mouse Brain Development

Targeting Tau Hyperphosphorylation via Kinase Inhibition: Strategy to Address Alzheimer's Disease

2020 ◽  
Vol 20 (12) ◽  
pp. 1059-1073 ◽  
Author(s):  
Ahmad Abu Turab Naqvi ◽  
Gulam Mustafa Hasan ◽  
Md. Imtaiyaz Hassan
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Tau Protein ◽  
Glycogen Synthase ◽  
Paired Helical Filaments ◽  
Tau Hyperphosphorylation ◽  
Microtubule Stabilization ◽  
Extracellular Signal

Microtubule-associated protein tau is involved in the tubulin binding leading to microtubule stabilization in neuronal cells which is essential for stabilization of neuron cytoskeleton. The regulation of tau activity is accommodated by several kinases which phosphorylate tau protein on specific sites. In pathological conditions, abnormal activity of tau kinases such as glycogen synthase kinase-3 β (GSK3β), cyclin-dependent kinase 5 (CDK5), c-Jun N-terminal kinases (JNKs), extracellular signal-regulated kinase 1 and 2 (ERK1/2) and microtubule affinity regulating kinase (MARK) lead to tau hyperphosphorylation. Hyperphosphorylation of tau protein leads to aggregation of tau into paired helical filaments like structures which are major constituents of neurofibrillary tangles, a hallmark of Alzheimer’s disease. In this review, we discuss various tau protein kinases and their association with tau hyperphosphorylation. We also discuss various strategies and the advancements made in the area of Alzheimer's disease drug development by designing effective and specific inhibitors for such kinases using traditional in vitro/in vivo methods and state of the art in silico techniques.

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