Rejuvenation of irradiated AS-1 red cells.

BACKGROUND: Gamma irradiation of blood components is used to prevent transfusion-associated graft-versus-host disease. The demand for irradiated blood components is increasing because of the increase in directed donation by family members. Irradiated units currently have a recommended maximum storage life of 28 days. Since in vivo recovery is related to red cell ATP levels, rejuvenation of stored irradiated units using a pyruvate-inosine phosphate-adenine additive was explored. STUDY DESIGN AND METHODS: Units of AS-1 red cells from 16 volunteer donors were divided into two equal volumes and one split unit from each was irradiated with 25 Gy. Ten units were irradiated on Day 5, 6, or 7 of 4 degrees C storage and 6 units were irradiated on Day 1 of 4 degrees C storage. All units were rejuvenated for 1 hour at 37 degrees C using a pyruvate-inosine-phosphate-adenine additive on Day 42 of 4 degrees C storage. Units were assayed for ATP, 2, 3 DPG and supernatant sodium, potassium, and glucose. RESULTS: ATP and 2, 3 DPG levels were restored equally well in irradiated and non-irradiated units. The previously reported irradiation-induced red cell potassium-sodium shift was demonstrated. Supernatant potassium and sodium levels did not reverse 1 hour after rejuvenation was completed. There was no significant difference in results between units irradiated on Day 1 or Day 5, 6, or 7. CONCLUSION: Red cell ATP and 2, 3 DPG levels were restored in irradiated AS-1 units stored at 4 degrees C for 42 days using a pyruvate-inosine-phosphate-adenine rejuvenation additive.

Fine needle aspiration cytology of acinar cell carcinoma of the pancreas: a report of two cases.

BACKGROUND: Fine needle aspiration in lieu of needle biopsy is widely used for the diagnosis of pancreatic neoplasms. The cytologic features of ductal carcinomas are well characterized, but the appearances of less common pancreatic neoplasms, such as acinar cell carcinoma (ACC), are not well described. CASES: We present the cytologic, histologic, immunocytochemical and ultrastructural features of two cases of ACC. The tumors occurred in a 36-year-old woman and 43-year-old man. The aspirate from one case contained neoplastic cells with smooth-contoured nuclei containing one or two prominent nucleoli. The aspirated material from the second case was necrotic, with numerous neutrophils and scattered nests of tumor cells similar to those present in the first case. Histologically, both tumors manifested solid and acinar patterns, and each contained some cells with periodic acid-Schiff-positive granules that were resistant to diastase. The neoplasms were immunochemically positive for trypsin and negative for neuroendocrine markers. Ultrastructurally, the aspirate from one case demonstrated apical microvilli, zymogenlike granules and abundant rough endoplasmic reticulum. CONCLUSION: Uncommon pancreatic neoplasms may be difficult to diagnose due to their cytologic and histologic subtleties. Supplemental studies including immunocytochemistry, cytochemistry and electron microscopy are important in facilitating their identification.

The relationship between the morphology of cell organelles and kinetics of the secretory process in male sex accessory glands of mice.

Two male sex accessory glands of the mouse, seminal vesicle and coagulating gland, were compared with the aim of relating differences in the morphology of organelles to the kinetics of the secretory process. The epithelial cells of the two glands were assessed by morphometric analysis, cytochemical staining, and electron-microscopic autoradiography after administration of a labeled amino acid. The rough endoplasmic reticulum of the seminal vesicle comprised narrow parallel cisternae, while that of the coagulating gland was greatly distended and occupied a much larger percentage of the cytoplasmic volume. Radioactively labeled products were secreted much more rapidly in the seminal vesicle than in the coagulating gland. The primary point of difference in kinetics of intracellular transport between the two glands was in exit of material from the rough endoplasmic reticulum. The more rapid drainage of the rough endoplasmic reticulum may be related to its relatively greater membrane surface density and lesser internal volume. In contrast, similarities in size and cytochemical staining in the Golgi apparatus of the two glands were accompanied by similar kinetics of intracellular transport of secretory protein through this organelle.

Intracellular pathway and kinetics of protein secretion in the coagulating gland of the mouse.

The coagulating gland of male rodents is part of the prostatic complex. Various mechanisms of secretion have been postulated, in part because organelles commonly involved in the secretory process possess unusual features, such as extreme distension of the rough endoplasmic reticulum. In the present study, the pathway, kinetics, and mode of secretion in the coagulating gland of the mouse were studied by electron microscope autoradiography at intervals between 5 min and 8 h after administration of 3H-threonine. The percentage of grains associated with the rough endoplasmic reticulum was initially high and generally decreased throughout the experiment, while a pronounced rise in the proportion of grains associated with the Golgi apparatus and secretory granules was observed 6 h after injection of precursor. In addition, there was a smaller elevation in the percentage of grains over the Golgi apparatus and secretory granules between 1 and 4 h, and radioactive material first reached the lumen of the gland 4 h after injection of the precursor. Although the general pathway of intracellular transport of secretory protein resembles that in other cells, the results indicate that there are several unusual aspects to the secretory process in the coagulating gland. First, the rate of transport was markedly slower than in most other exocrine gland cells, since the bulk of the labeled protein did not reach the Golgi apparatus and secretory granules until 6 h after administration of precursor. This reflected prolonged retention of secretory products in the endoplasmic reticulum. Second, in addition to the major bolus of labeled material that traversed the cells at about 6 h, a smaller wave of radioactivity appeared to pass through the Golgi apparatus and secretory granules and reach the lumen earlier, within the first few hours after the injection. Finally, the primary mode of secretion in the coagulating gland appears to be merocrine because the secretory granules contained much labeled protein.

Incorporation of 3H-fucose and the secretion of glycoproteins in the coagulating gland of the mouse.

The coagulating gland of rodents, which is part of the prostatic complex, secretes components of semen. Although possessing some ultrastructural features of other exocrine glands, the mechanism of secretion by these cells has been problematic. In the present study the pathway, kinetics, and mode of secretion in the coagulating gland of the mouse were studied by light and electron microscope autoradiography at intervals between 10 minutes and 3 hours after injection of 3H-fucose. The majority of silver grains overlay the Golgi apparatus at the initial interval, but in addition, more than a third of the grains were associated with extremely distended cisternae of the rough endoplasmic reticulum. At later intervals, radioactivity of the Golgi apparatus and the endoplasmic reticulum declined, while labeling of secretory granules increased greatly. Luminal contents became labeled 1 hour after administration of precursor. The results indicate that the pathway for secretion of glycoproteins proceeds through the Golgi apparatus to secretory granules and the glandular lumen, as in many other cells. In particular, heavy labeling of secretory granules at later intervals indicates that merocrine secretion is the most likely mechanism in the coagulating gland. However, the unusual observation that a significant proportion of grains overlay the rough endoplasmic reticulum at the initial interval raises the possibility that some fucose is incorporated into glycoproteins in the endoplasmic reticulum, as has been reported for other cell types with similarly configured endoplasmic reticulum.