Indicate the presence of numerical data in the abstract (whether numerical data plays a key role in medical records), solely using the information from the abstract.
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Question: Abstract: Surgically prepared cryptorchid mouse testes containing only type A spermatogonia were cultured with (Bu)2cAMP in combination with vitamin A (retinol). Treatment with (Bu)2cAMP and retinol for 12-24 h and with basal medium for an additional 8 days stimulated mitotic activity in type A spermatogonia and induced differentiation of germ cells. However, (Bu)2cAMP alone did not induce differentiation of type A spermatogonia. Moreover, when cryptorchid testes were treated with (Bu)2cAMP for longer than 3 days in the presence or absence of retinol, differentiation of type A spermatogonia did not take place; disintegration of the seminiferous tubules occurred instead. When the cryptorchid testes were cultured for 24 h in a medium containing a fixed concentration of retinol and varying concentrations of (Bu)2cAMP from 0.001-0.4 mM, there was a dose-dependent increase in the number of differentiated and mitotic germ cells and type A spermatogonia. Likewise, at a fixed dose of (Bu)2cAMP and increasing concentrations of retinol, a dose-dependent increase in the number of differentiated and mitotic germ cells occurred. However, the number of type A spermatogonia was decreased. The addition of puromycin, cycloheximide, and actinomycin D to the medium completely blocked retinol-(Bu)2cAMP-induced differentiation of the germ cells. The present results suggest that cAMP and retinol trigger biochemical events promoting the synthesis of specific macromolecules involved in the proliferation and differentiation of type A spermatogonia.
Question: Does the abstract contain any numerical data?

Answer: Yes

Question: Abstract: Guiding surgical therapy of ventricular tachycardia by preoperative endocardial catheter mapping necessitates improvement of the accuracy of localization of the arrhythmogenic site. We therefore used a new mathematical cineradiographic method during catheter mapping to compute the position of left ventricular arrhythmogenic sites relative to three anatomic reference points: the centers of aortic and mitral valve ostia and the left ventricular apex. To enable the surgeon to identify the position of the computed sites, a wire skeleton (one for each patient) representing a single or multiple arrhythmogenic site(s) relative to the anatomic reference points was constructed. This wire skeleton was inserted into the left ventricular cavity during surgery. Side branches of the device indicated preoperatively localized arrhythmogenic sites. Results in eight consecutive patients were compared with those of intraoperative simultaneous mapping of 64 endocardial sites. Sixteen morphologically distinct monomorphic ventricular tachycardias were mapped by catheter and 15 by intraoperative mapping. In 12 ventricular tachycardias an identical morphology was recorded during both techniques. The distance between arrhythmogenic sites localized with both methods was 1 cm or less in 11 of these 12 ventricular tachycardias and 2 cm in one ventricular tachycardia. These results indicate that endocardial catheter mapping combined with wire skeleton representation of computed positions of arrhythmogenic sites is reliable for guiding surgical therapy of ventricular tachycardia and since some of the ventricular tachycardias were inducible only during either preoperative or intraoperative mapping, both techniques have an additive value. In addition, the wire skeleton proved convenient during surgery by identifying the arrhythmogenic sites.
Question: Does the abstract contain any numerical data?

Answer: Yes

Question: Abstract: During liquid preservation under blood bank conditions, red cell membranes inexorably undergo damage that decreases erythrocyte survival after transfusion. Accordingly, we have surveyed membrane skeletal protein interactions during storage. We uncovered a decrease in the in vitro formation of spectrin-actin complex in the absence (50%) or presence (60%) of protein 4.1. Actual formation of the spectrin-actin-protein 4.1 complex fell in a linear fashion during the storage period. This fall in spectrin-actin interaction tightly correlated with the decline in total red cell phospholipid (R = 0.9932) measured simultaneously. This decrement of spectrin-actin association could be restored to greater than 70% of normal values by preincubation of stored spectrin with 50 mM dithiothreitol. This storage injury to spectrin-actin interaction might weaken the membrane skeleton and lead to decreased red cell survival. In vitro reversibility of the damage by reducing agents suggests a possible new direction for prolonging the shelf life of stored blood.
Question: Does the abstract contain any numerical data?

Answer:
Yes