Immunocytochemical study of ballooned neurons in cortical degeneration with neuronal achromasia.

We studied the immunocytochemical characteristics of the ballooned neurons (BN) in three patients with cortical degeneration with neuronal achromasia (CDNA) using antibodies to phosphorylated neurofilaments (PNF), tau, Alz-50, ubiquitin, beta (A4) amyloid, and glial fibrillary acidic protein. All BN exhibited intense perikaryal staining for PNF protein. Most BN and some normal-appearing neurons also stained for ubiquitin and Alz-50. The BN did not immunostain for tau protein, and none of the cases had tau-reactive neocortical neurofibrillary tangles or Pick bodies. One case had occasional senile plaques that stained for beta amyloid; no case had amyloid angiopathy. Our findings suggest that the pathophysiologic basis of the cortical degeneration in CDNA involves an alteration of neuronal cytoskeletal metabolism affecting neurofilament and possibly microtubular proteins in conjunction with activation of the ubiquitin proteolytic system.     

Clinical utility of PTSD,resilience, sleep,and blast as risk factors to predict poor neurobehavioral functioning following traumatic brain injury: A longitudinal study in U.S. military service members

Quality of Life Research - This study examined the clinical utility of post-traumatic stress disorder (PTSD), low resilience, poor sleep, and lifetime blast exposure as risk factors for predicting...     

Enhancement of 3H-diazepam binding by SQ 65,396: a novel anti-anxiety agent.

SQ 65,396, a clinically active anti-anxiety agent, enhanced the binding of 3H-diazepam at 1.5 nM. This effect was due to an increase in the affinity for the ligand, without a change in the number of 3H-diazepam binding sites. This action of SQ 65,396 may mediate its anti-anxiety effects by affecting the action of an endogenous modulator of the "benzodiazepine receptor." Several other substances and treatments increase the affinity of 3H-diazepam for its receptors by mechanisms which may be related to the effect produced by SQ 65,396.     

Anatomie et tendinopathie patellaire : un malentendu

The anatomical structure linking the patella and the tibia is called the “patellar ligament” in the international nomenclature. This term is well accepted yet can be a source of confusion for non-specialists. This is because the priority role of this structure is not to maintain joint stability, the primary role of the cruciate ligaments and the collateral ligaments, but rather to prolong the mechanical action of the quadriceps muscle onto the leg skeleton beyond the “patellar sesmoid”. Patellar tendon injuries are a common observation in sports medicine. The proximal third of the tendon below the patella is most generally involved. This highly frequent tendinopathy sometimes termed an “insertion” tendiopathy. Based on 100 consecutive magnetic resonance imaging studies and cadaveric dissection, we confirm that the insertion of the patellar tendon is situated on the anterior aspect of the patella and not the tip. We describe two anatomical variants of the healthy patellar tendon (type 1 and 2) that should not be confused with a site of tendinopathy. The anatomical limits between tendinous tissue and infrapatellar adipose body (the Hoffa adipose ligament), notably on the upper third is still debated and merits further work.     

A synthetic non-benzodiazepine ligand for benzodiazepine receptors: A probe for investigating neuronal substrates of anxiety

CL 218,872 is the first non-benzodiazepine to selectively displace brain specific ³H-diazepam binding with a potency comparable to that of the benzodiazepines. Like the benzodiazepines, CL 218,872 increased punished responding in a conflict situation and protected against the convulsions induced by pentylenetetrazole. These three pharmacological properties are highly predictive of anxiolytic activity. Unlike the benzodiazepines, however, CL 218,872 was relatively inactive in tests designed to measure effects on neuronal systems which utilize GABA, glycine and serotonin as transmitters. Furthermore, CL 218,872 was relatively free of the ataxic and depressant side effects commonly associated with the benzodiazepines. Because of this high degree of selectivity, CL 218,872 may represent a new probe for investigating neuronal substrates of anxiety.     

Relationship between benzodiazepine receptors and experimental anxiety in rats.

The in vitro and in vivo ability of benzodiazepines to inhibit specific 3H-diazepam binding correlated with their ability to increase punished responding in a conflict situation. Conflict and foot shock, the punishing stimulus used in most conflict procedures, also altered 3H-diazepam binding. These data implicate 3H-diazepam binding sites in mediating at least some of the anxiolytic properties of benzodiazepines and suggest the existence of some endogenous substance which might be involved in the etiology of anxiety.     

Lewy bodies in the amygdala: increase of alpha-synuclein aggregates in neurodegenerative diseases with tau-based inclusions

BACKGROUND: Increased attention has been given to alpha-synuclein aggregation in nonsynucleinopathies because alpha-synuclein-containing Lewy bodies (LBs) influence symptoms. However, the spectrum of disorders in which secondary inclusions are likely to occur has not been defined. Amygdala neurons commonly develop large numbers of secondary LBs, making it a practical region for studying this phenomenon. OBJECTIVE: To characterize the spectrum of diseases associated with LB formation in the amygdala of neurodegenerative disease and control cases. DESIGN: An autopsy series of 101 neurodegenerative disease and 34 aged control cases. Using immunohistochemistry studies, we examined the amygdala for alpha-synuclein aggregates. RESULTS: Lewy bodies were often abundant in classic Pick disease, argyrophilic grain disease, Alzheimer disease, and dementia with LBs but not in cases with amygdala degeneration lacking tau-based inclusions, control cases, preclinical disease carriers, or degenerative diseases lacking pathologic involvement of the amygdala. The exposed alpha-synuclein epitopes were similar in all cases containing LBs. CONCLUSIONS: Abnormal alpha-synuclein aggregation in the amygdala is disease selective, but not restricted to disorders of alpha-synuclein and beta-amyloid. Our data are compatible with the notion that tau aggregates predispose neurons to develop secondary LBs.