Number Of A1 Research Articles

NREM sleep alterations in narcolepsy/cataplexy

Objective NREM sleep patterns of narcoleptic patients with cataplexy were studied, focusing on their sleep ‘microstructure’, by analyzing the cyclic alternating pattern (CAP). Methods Forty-nine HLA DQB1*0602-positive patients with narcolepsy/cataplexy (32 men and 17 women, aged 18–46 years) were included together with 37 age-matched normal controls. Each subject underwent one polysomnographic night recording after an adaptation night. Sleep stages were scored following standard criteria and CAP A phases were detected and classified into 3 subtypes (A1, A2, and A3). Power spectra for frequencies between 0.5 and 25 Hz were obtained for each CAP condition, separately in sleep stage 2 and SWS. Results Narcoleptic patients displayed reduced total CAP rate. A selective reduction in the number of A1 subtypes/hour and a reduced A3 index were found in narcoleptics who had also a smaller average number of CAP sequences. Narcoleptic patients had higher power spectra for fast frequencies mostly during SWS, while REM sleep power spectra showed significantly higher power density for frequency bins 0.5–1.5, 8.5–9.5, and 17.5–25 Hz. Similarly, CAP A1 subtypes and NCAP epochs during SWS displayed significantly higher power density for fast frequency bins. Conclusions The main finding of this study is that the occurrence of the A1 CAP subtypes is impaired during NREM sleep in narcoleptic patients. Thus, narcolepsy seems to be accompanied not only by alterations of REM but also NREM sleep which is subtly but significantly impaired, as reflected by CAP and the corresponding EEG spectral analysis. Significance Our findings might indicate that in narcolepsy very-slow oscillation processes less effective than normal might be present, with a subtly impaired capability of grouping the other sleep EEG activities; this aspect deserves further insight in order to obtain a better understanding of its functional meaning.

The relationship of daily sperm production with number of Sertoli cells and testicular size in adult horses: role of primitive spermatogonia

The number of Sertoli cells is important in spermatogenesis as noted by significant correlations between the number of Sertoli cells and the number of germ cells observed as early as type B2 spermatogonia in the horse. However, the stage within spermatocytogenesis at which these relationships first occur is unclear. The relationships between the number of Sertoli cells and parenchymal weight and the number of germ cells during the mitosis of spermatogenesis were determined in 184 adult horses to identify the developmental stage (that is, the earliest germ cell) at which significant relationships are established. The total numbers of all types of A spermatogonia and of specific subtypes (A1, A2, A3, B1 or B2) of spermatogonia were correlated with the number of Sertoli cells and with parenchymal weight. The number of each cell type was calculated using stereology. The number of Sertoli cells was correlated (P < 0.01) with parenchymal weight (r = 0.85) and with daily sperm production (r = 0.83), and parenchymal weight was correlated (P < 0.01) with daily sperm production (r = 0.89). The number of Sertoli cells was correlated (P < 0.01) with the number of type A (r = 0.81) and A1 (r = 0.74) spermatogonia. Parenchymal weight was correlated with the number of type A (r = 0.80) spermatogonia and with the number of A1 (r = 0.67) spermatogonia.(ABSTRACT TRUNCATED AT 250 WORDS)

Seasonal Differences in Equine Spermatocytogenesis1

Spermatocytogenesis plays a pivotal role in regulation of spermatogenesis; however, its details remain relatively obscure in nonrodent species. The equine testis contains approximately 100% more spermatogonia in summer than in winter and appears to be a good model to identify the flexible components of spermatocytogenesis that cause seasonal changes in daily sperm production. Testes were taken from horses in the winter (n = 47) and in summer (n = 43). Tissues were fixed by glutaraldehyde-perfusion and submission in osmium, embedded in Epon or methacrylate, sectioned at 0.5 micron or 5 microns, stained with toluidine blue, and observed using bright-field microscopy. The combined total number of A1, A2, A3, and B1 (A plus B1) spermatogonia/testis and the numbers of B2 spermatogonia or early primary spermatocytes were determined by stereology of Epon sections involving testicular volume density and volume of spermatogonial nuclei. In a subset of horses, different spermatogonial subtypes (A1, A2, A3, and B1) were counted per 100 Sertoli cells in each of the 8 spermatogenic stages and expressed as percentage of all A plus B1 spermatogonia. The number of each spermatogonial subtype/testis for the large series of horses was calculated by multiplying the number of A plus B1 spermatogonia/testis (determined for each horse) by the percentage of that given spermatogonial subtype. Season did not significantly affect the number of any given subtype per 100 Sertoli cells in any stage or percentages of different subtypes of spermatogonia. Numbers of A1 (p less than 0.05), A2, A3, B1, or B2 spermatogonia (p less than 0.01) were greater in the breeding season.(ABSTRACT TRUNCATED AT 250 WORDS)

Characterization of the human T lymphocyte adenosine receptor: comparison of normal and systemic lupus erythematosus cells

To determine whether a defect in the T cell response to adenosine exists at the level of the adenosine receptor in systemic lupus erythematosus (SLE) we measured the binding affinity and maximum binding of T cell membranes from both normal and SLE T cells by utilizing radiolabeled adenosine ligands. Normal T lymphocyte membranes possess a single class of [3H]5-N-ethylcarboxamide adenosine binding sites with a Kd of 0.61 microM, a Bmax of 23.5 pmol/mg protein, and a Hill coefficient of 0.98, which indicates the presence of noncooperative sites. In contrast, T cell membranes do not bind significant amounts of either [3H]cyclohexyladenosine or [3H]phenylisopropyladenosine. These data indicate that T lymphocyte membranes have only A2, and not A1, adenosine receptors. Similarly, T cells from both active and inactive SLE subjects also express only A2 receptors with a Kd of 0.93 microM, a Bmax of 20.4 pmol/mg protein, and a Hill coefficient of 0.85, which is consistent with the presence of noncooperative sites. There is no difference in the on-rate, affinity, or density of T cell A2 receptors from active SLE patients, inactive SLE patients, or healthy controls. We conclude that T lymphocytes from both healthy and SLE subjects express A2, but not A1, receptors. Thus, the inability of SLE T cells to respond to adenosine does not reflect a decreased density of A2 (stimulatory) receptors, diminished A2 receptor binding, or an increased affinity or number of A1 (inhibitory) adenosine receptors. These observations support the conclusion that the defect in the T cell cAMP-dependent pathway may occur at a point distal to the adenosine receptor.