scholarly journals Arginine-rich proteins in spherical inclusions of human locus coeruleus neurons demonstrated by benzil modification.

1984 ◽  
Vol 32 (11) ◽  
pp. 1192-1196 ◽  
Author(s):  
M T Panayotacopoulou ◽  
M R Issidorides
Keyword(s):  
Bromphenol Blue ◽  
Complex Structures ◽  
Green Fluorescence ◽  
Cytoplasmic Inclusions ◽  
Spherical Inclusions ◽  
Normal Human ◽  
Acidic Nature ◽  
Human Brains ◽  
Arginyl Residues ◽  
Formalin Fixed

Previous studies have shown that aminergic neurons in the normal human brain contain acidophilic cytoplasmic inclusions--called protein bodies (PBs)--that are reduced or absent in parkinsonism and disrupted in depression. The purpose of the present study was to elucidate the constitution of PBs in five formalin-fixed normal human brains using histochemical methods specific for histones, protamines, and the amino acid arginine. PBs were revealed with alkaline fast green and bromphenol blue, exhibiting a high content in histones and in protamines. They developed blue metachromasia with phosphotungstic acid-hematoxylin and green fluorescence with phenanthrenequinone, which established the presence of arginyl residues. Using benzil, which selectively modifies the guanido group of arginine, staining was blocked for each of the above two methods. The application of Mallory's trichrome procedure after benzil differentiated the PBs into an unstained core and a still fuchsinophilic rim. Since the fuchsinophilia of the rim was shown to persist after acetylation as well, we suggest that this rim probably contains acidic macromolecules that attach to the basic charges of the amphoteric acid fuchsin. We conclude that the PB are complex structures consisting of a core segregating arginine-rich proteins and a rim which probably contains macromolecules of an acidic nature.

scholarly journals Your Brain Is Not an Onion With a Tiny Reptile Inside

2020 ◽  
Vol 29 (3) ◽  
pp. 255-260
Author(s):  
Joseph Cesario ◽  
David J. Johnson ◽  
Heather L. Eisthen
Keyword(s):  
Nervous System ◽  
Behavioral Flexibility ◽  
Brain Structures ◽  
Introductory Psychology ◽  
Complex Structures ◽  
Accurate Model ◽  
Nervous System Evolution ◽  
Neural Evolution ◽  
Human Brains ◽  
Unanimous Agreement

A widespread misconception in much of psychology is that (a) as vertebrate animals evolved, “newer” brain structures were added over existing “older” brain structures, and (b) these newer, more complex structures endowed animals with newer and more complex psychological functions, behavioral flexibility, and language. This belief, although widely shared in introductory psychology textbooks, has long been discredited among neurobiologists and stands in contrast to the clear and unanimous agreement on these issues among those studying nervous-system evolution. We bring psychologists up to date on this issue by describing the more accurate model of neural evolution, and we provide examples of how this inaccurate view may have impeded progress in psychology. We urge psychologists to abandon this mistaken view of human brains.

ADP-induced inhibition of von Willebrand factor-mediated platelet agglutination

1976 ◽  
Vol 230 (5) ◽  
pp. 1406-1410 ◽  
Author(s):  
RA Grant ◽  
MB Zucker ◽  
J McPherson
Keyword(s):  
Human Plasma ◽  
Von Willebrand Factor ◽  
Prostaglandin E1 ◽  
Platelet Rich Plasma ◽  
Shape Change ◽  
Normal Human ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Formalin Fixed ◽  
Platelet Shape

Human plasma von Willebrand factor (vWF) plus the antibiotic ristocetin, or bovine or porcine vWF alone, agglutinates platelets in either normal human ethylenediaminetetraacetate (EDTA)-treated citrated platelet-rich plasma (PRP) or citrated PRP from patients with the congenital platelet defect thrombasthenia. The prior addition of 1-10 muM ADP, which causes platelet shape change but not aggregation under these conditions, inhibited vWF-mediated agglutination. Inhibition was prevented by 200 muM ATP. Addition of ADP caused prompt reversal of established vWF-mediated agglutination, which resumed when the ADP was enzymatically removed. EDTA-treated, Formalin-fixed, washed normal platelets also underwent vWF-mediated agglutination. ADP was inhibitory only when added before fixation. Epinephrine (40 muM), prostaglandin E1 (7 muM), or serotonin (2 muM) added before fixation caused slight to moderate inhibition but always less than ADP. Platelets from blood chilled before fixation were fully active. Platelets fixed in freshly prepared PRP did not agglutinate as well as those fixed after incubation of PRP, probably because centrifugation exposes the platelets to ADP. It concluded that ADP causes a reversible decrease in the accessibility of the membrane receptor to vWF.

Quantitative Electrophoresis of Serum Proteins on Paper

1956 ◽  
Vol 2 (5) ◽  
pp. 303-319 ◽  
Author(s):  
Moses Wurm ◽  
Frederick H Epstein
Keyword(s):  
Protein Concentration ◽  
Moving Boundary ◽  
Serum Proteins ◽  
Paper Electrophoresis ◽  
Bromphenol Blue ◽  
Good Resolution ◽  
Confidence Limits ◽  
Protein Patterns ◽  
Electrophoretic Patterns ◽  
Normal Human

Abstract 1. A procedure for paper electrophoresis has been described which gives highly reproducible protein patterns with good resolution and freedom from distortions. 2. Densitometry of protein bands on paper stained with bromphenol blue or Amidoschwarz 10B reveals that the logarithm of protein concentration is proportional to optical density and that Beer's law does not apply. Electrophoretic patterns of normal human serum evaluated in this manner give values in close agreement with those obtained by moving-boundary electrophoresis. 3. Confidence limits were determined for both methods.

Three-Dimensional Topographic Fiber Tract Anatomy of the Cerebrum

2015 ◽  
Vol 11 (2) ◽  
pp. 274-305 ◽  
Author(s):  
Kaan Yagmurlu ◽  
Alexander L Vlasak ◽  
Albert L Rhoton
Keyword(s):  
Three Dimensional ◽  
Central Core ◽  
3 Dimensional ◽  
Fiber Tracts ◽  
Nuclear Masses ◽  
Fiber Dissection ◽  
Dissection Technique ◽  
Human Brains ◽  
The Brain ◽  
Formalin Fixed

Abstract BACKGROUND The fiber tracts of the cerebrum may be a more important determinant of resection limits than the cortex. Better knowledge of the 3-dimensional (3-D) anatomic organization of the fiber pathways is important in planning safe and accurate surgery for lesions within the cerebrum. OBJECTIVE To examine the topographic anatomy of fiber tracts and subcortical gray matter of the human cerebrum and their relationships with consistent cortical, ventricular, and nuclear landmarks. METHODS Twenty-five formalin-fixed human brains and 4 whole cadaveric heads were examined by fiber dissection technique and ×6 to ×40 magnification. The fiber tracts and central core structures, including the insula and basal ganglia, were examined and their relationships captured in 3-D photography. The depth between the surface of the cortical gyri and selected fiber tracts was measured. RESULTS The topographic relationships of the important association, projection, and commissural fasciculi within the cerebrum and superficial cortical landmarks were identified. Important landmarks with consistent relationships to the fiber tracts were the cortical gyri and sulci, limiting sulci of the insula, nuclear masses in the central core, and lateral ventricles. The fiber tracts were also organized in a consistent pattern in relation to each other. The anatomic findings are briefly compared with functional data from clinicoradiological analysis and intraoperative stimulation of fiber tracts. CONCLUSION An understanding of the 3-D anatomic organization of the fiber tracts of the brain is essential in planning safe and accurate cerebral surgery.

scholarly journals Is Multiple System Atrophy a Prion-like Disorder?

2021 ◽  
Vol 22 (18) ◽  
pp. 10093
Author(s):  
Kurt A. Jellinger ◽  
Gregor K. Wenning ◽  
Nadia Stefanova
Keyword(s):  
Multiple System Atrophy ◽  
Prion Disease ◽  
Scientific Evidence ◽  
Motor Impairment ◽  
Lewy Bodies ◽  
Convincing Evidence ◽  
Cytoplasmic Inclusions ◽  
Primary Astrocyte ◽  
Disease Causation ◽  
Human Brains

Multiple system atrophy (MSA) is a rapidly progressive, fatal neurodegenerative disease of uncertain aetiology that belongs to the family of α-synucleinopathies. It clinically presents with parkinsonism, cerebellar, autonomic, and motor impairment in variable combinations. Pathological hallmarks are fibrillary α-synuclein (αSyn)-rich glial cytoplasmic inclusions (GCIs) mainly involving oligodendroglia and to a lesser extent neurons, inducing a multisystem neurodegeneration, glial activation, and widespread demyelinization. The neuronal αSyn pathology of MSA has molecular properties different from Lewy bodies in Parkinson’s disease (PD), both of which could serve as a pool of αSyn (prion) seeds that could initiate and drive the pathogenesis of synucleinopathies. The molecular cascade leading to the “prion-like” transfer of “strains” of aggregated αSyn contributing to the progression of the disease is poorly understood, while some presented evidence that MSA is a prion disease. However, this hypothesis is difficult to reconcile with postmortem analysis of human brains and the fact that MSA-like pathology was induced by intracerebral inoculation of human MSA brain homogenates only in homozygous mutant 53T mice, without production of disease-specific GCIs, or with replication of MSA prions in primary astrocyte cultures from transgenic mice expressing human αSyn. Whereas recent intrastriatal injection of Lewy body-derived or synthetic human αSyn fibrils induced PD-like pathology including neuronal αSyn aggregates in macaques, no such transmission of αSyn pathology in non-human primates by MSA brain lysate has been reported until now. Given the similarities between αSyn and prions, there is a considerable debate whether they should be referred to as “prions”, “prion-like”, “prionoids”, or something else. Here, the findings supporting the proposed nature of αSyn as a prion and its self-propagation through seeding as well as the transmissibility of neurodegenerative disorders are discussed. The proof of disease causation rests on the concordance of scientific evidence, none of which has provided convincing evidence for the classification of MSA as a prion disease or its human transmission until now.

Age-related neurofilament phosphorylation in normal human brains

1989 ◽  
Vol 10 (3) ◽  
pp. 253-258 ◽  
Author(s):  
Barbara J. Blanchard ◽  
Vernom M. Ingram
Keyword(s):  
Age Related ◽  
Neurofilament Phosphorylation ◽  
Normal Human ◽  
Human Brains

scholarly journals STAINING OF BASIC NUCLEOPROTEINS BY AN EXTRACT OF THE BLACK RASPBERRY

1974 ◽  
Vol 22 (10) ◽  
pp. 976-980
Author(s):  
LAWRENCE KASS
Keyword(s):  
Bone Marrow ◽  
Peripheral Blood ◽  
Bone Marrow Cells ◽  
Human Peripheral Blood ◽  
Black Raspberry ◽  
Methanolic Extracts ◽  
Naturally Occurring ◽  
Normal Human ◽  
Normal Human Peripheral Blood ◽  
Formalin Fixed

Methanolic extracts of the black raspberry (Rubrus occidentalis) were found to stain nuclei of normal human peripheral blood and bone marrow cells. Using filter paper spot tests, staining of both purified deoxyribonucleic acid and histone occurred at pH 4.1, but at pH 9.3 only histone was stained. Histone staining diminished above pH 9.3 and disappeared at pH 10.0. Using formalin-fixed cover slips of peripheral blood and bone marrow, methanol-raspberry staining at pH 9.3 demonstrated orange-brown staining nuclei. This study suggests that the anthocyanin group of naturally occurring dyes is capable of staining basic nucleoproteins at alkaline pH.

Congenital brain anomalies and chromosomal aberrations from the Zagreb Collection of human brains

2014 ◽  
Vol 5 (4) ◽  
Author(s):  
Božo Krušlin ◽  
Tihana Džombeta ◽  
Miran Bezjak ◽  
Goran Sedmak ◽  
Zdravko Petanjek ◽  
...  
Keyword(s):  
Down Syndrome ◽  
Human Brain ◽  
Brain Development ◽  
Chromosomal Aberrations ◽  
Developmental Stages ◽  
Human Brain Development ◽  
Patau Syndrome ◽  
Edwards Syndrome ◽  
Normal Human ◽  
Human Brains

AbstractThe Zagreb Collection of developing and adult human brains consists of approximately 1,300 brains of fetuses, children and adults that were collected following routine autopsies in the period from 1974 to 2014. The collection comprises brains of different normal developmental stages that may serve for investigation of normal human brain development. Previous studies on this material have led to several important contributions on human cortical development, such as the discovery of the transient fetal subplate zone. The Zagreb Collection, however, also contains approximately 100 brains with different anomalies including chromosomal aberrations such as Down syndrome. We have analyzed all the available material from the Zagreb Collection and identified 44 brains of fetuses and children with Down syndrome, 10 with Patau syndrome, 6 with Edwards syndrome as well as 7 holoprosencephalic, 7 hydrocephalic and 4 microcephalic brains. The largest part of the Collection is available for further research using modern genetic, immunocytochemical and imaging methods, especially magnetic resonance imaging. Furthermore, the histological slides from the Zagreb Collection are currently being digitally scanned and made available as virtual slides to general scientific audience. The Zagreb Collection represents unique and versatile resource for the future study of normal and abnormal human brain development.

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