Distribution of phosphoneuroprotein 14 (PNP 14) in vertebrates: its levels as determined by enzyme immunoassay

Tsukada, K.; Kameyama, Hiroshi; Furuyama, Yasuo; Nakaya, Kazuyasu

doi:10.1016/s0006-8993(96)00914-6

Cited by 24 publications

(14 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…5, B and C). The concentration of ␣-synuclein in brain homogenate was high at 0.03% of total brain protein, largely consistent with published literature (47). We then extrapolated the synaptic ␣-synuclein protein concentration by Western blotting purified synaptosomes for ␣-synuclein and approximating the volume of synapses at 0.12ϫ of the total brain volume (assuming a uniform distribution of proteins in the brain).…”

Section: And Ref 12)supporting

confidence: 81%

Monomeric Synucleins Generate Membrane Curvature

Westphal

Chandra

2013

Journal of Biological Chemistry

171

177

View full text Add to dashboard Cite

Section: And Ref 12)supporting

confidence: 81%

Monomeric Synucleins Generate Membrane Curvature

Westphal

Chandra

2013

Journal of Biological Chemistry

171

177

View full text Add to dashboard Cite

“…In addition, we have found that this function is greatly altered when ␣-synuclein includes A30P, a mutation associated with autosomal dominant forms of PD. In all our experiments, the concentrations of ␣-synucleins used were analogous to the average levels of the protein in the brain (Shibayama-Imazu et al, 1993;Nakajo et al, 1996) and lower than those existing in at least some synapses (Fortin et al, 2005;Tao-Cheng, 2006). Our results therefore cannot depend on excess of the protein, rather, they demonstrate that the ␣-synuclein/actin interaction can have an important role in both the physiology and the pathology of the brain.…”

Section: Discussionmentioning

confidence: 56%

“…N2A cells express very low levels of endogenous ␣-synuclein, hardly appreciable by either Western blotting or immunocytochemistry (Figure 3, A-D). In these cells, concentrations of ␣-synucleins comparable to those existing in the brain (Shibayama-Imazu et al, 1993;Nakajo et al, 1996) were reached by either delivery of recombinant wt or A30P ␣-synucleins or transfection of the corresponding cDNAs. The concentration of exogenous ␣-synucleins in the cells loaded by SLO permeabilization (Walev et al, 2001) followed by Ca 2ϩ -dependent membrane resealing was ϳ5 M, as revealed by Western blotting (Figure 3A).…”

Section: A30p ␣-Synuclein Induces Cytoskeleton Disruption In N2a Cellsmentioning

confidence: 99%

α-Synuclein and Its A30P Mutant Affect Actin Cytoskeletal Structure and Dynamics

Sousa

Bellani

Giannandrea

et al. 2009

MBoC

107

View full text Add to dashboard Cite

The function of ␣-synuclein, a soluble protein abundant in the brain and concentrated at presynaptic terminals, is still undefined. Yet, ␣-synuclein overexpression and the expression of its A30P mutant are associated with familial Parkinson's disease. Working in cell-free conditions, in two cell lines as well as in primary neurons we demonstrate that ␣-synuclein and its A30P mutant have different effects on actin polymerization. Wild-type ␣-synuclein binds actin, slows down its polymerization and accelerates its depolymerization, probably by monomer sequestration; A30P mutant ␣-synuclein increases the rate of actin polymerization and disrupts the cytoskeleton during reassembly of actin filaments. Consequently, in cells expressing mutant ␣-synuclein, cytoskeleton-dependent processes, such as cell migration, are inhibited, while exo-and endocytic traffic is altered. In hippocampal neurons from mice carrying a deletion of the ␣-synuclein gene, electroporation of wild-type ␣-synuclein increases actin instability during remodeling, with growth of lamellipodia-like structures and apparent cell enlargement, whereas A30P ␣-synuclein induces discrete actin-rich foci during cytoskeleton reassembly. In conclusion, ␣-synuclein appears to play a major role in actin cytoskeletal dynamics and various aspects of microfilament function. Actin cytoskeletal disruption induced by the A30P mutant might alter various cellular processes and thereby play a role in the pathogenesis of neurodegeneration.

show abstract

“…This protein, like α-synuclein, is expressed predominantly in the brain, however, in contrast to α-synuclein, β-synuclein is distributed more uniformly throughout the brain [181,182]. Besides the central nervous system β-Synuclein was also found in Sertoli cells of the testis [183,184], whereas α-synuclein was found in platelets [185].…”

Section: β-And γ-Synucleinsmentioning

confidence: 99%

Amyloidogenesis of Natively Unfolded Proteins

Uversky

2008

CAR

174

152

View full text Add to dashboard Cite

Aggregation and subsequent development of protein deposition diseases originate from conformational changes in corresponding amyloidogenic proteins. The accumulated data support the model where protein fibrillogenesis proceeds via the formation of a relatively unfolded amyloidogenic conformation, which shares many structural properties with the pre-molten globule state, a partially folded intermediate first found during the equilibrium and kinetic (un)folding studies of several globular proteins and later described as one of the structural forms of natively unfolded proteins. The flexibility of this structural form is essential for the conformational rearrangements driving the formation of the core cross-beta structure of the amyloid fibril. Obviously, molecular mechanisms describing amyloidogenesis of ordered and natively unfolded proteins are different. For ordered protein to fibrillate, its unique and rigid structure has to be destabilized and partially unfolded. On the other hand, fibrillogenesis of a natively unfolded protein involves the formation of partially folded conformation; i.e., partial folding rather than unfolding. In this review recent findings are surveyed to illustrate some unique features of the natively unfolded proteins amyloidogenesis.

show abstract

Distribution of phosphoneuroprotein 14 (PNP 14) in vertebrates: its levels as determined by enzyme immunoassay

Cited by 24 publications

References 14 publications

Monomeric Synucleins Generate Membrane Curvature

Monomeric Synucleins Generate Membrane Curvature

α-Synuclein and Its A30P Mutant Affect Actin Cytoskeletal Structure and Dynamics

Amyloidogenesis of Natively Unfolded Proteins

Contact Info

Product

Resources

About