Levels of serum Span-1, a new tumor marker for pancreatic cancer, were assayed in 64 patients with pancreatic cancer, 90 with nonpancreatic cancer, and 254 with nonmalignancies, involving 55 healthy controls. Furthermore, Span-1 was compared with other tumor markers (CA19-9, carcinoembryonic antigen [CEA], and DU-PAN-2). Frequency of elevated Span-1 levels was 81.3% in pancreatic cancer. False-positive elevations of serum Span-1 levels were rather common in liver cirrhosis (53.8%) and chronic hepatitis (26.3%). The sensitivity, specificity, and efficiency of this assay for pancreatic cancer, was 81.3%, 75.6%, and 76.5% against all subjects without pancreatic cancer, respectively. In comparison with other markers, sensitivity of Span-1 tended to be highest with similar specificity to those of CA19-9 and CEA. The Span-1 assay has a high sensitivity and specificity for pancreatic cancer. It is almost equivalent to CA19-9 assay. However, this assay is not specific for chronic liver diseases.
125I-guanylin was injected intravenously into rats, and their kidney and intestinal tract were processed for light microscopic radioautography using semithin sections to examine the binding sites. Various doses of unlabeled guanylin were also injected to examine the morphological effects of guanylin on the kidney. Dense labeling of silver grains due to 125I-guanylin were observed only in the kidney. In the cortex, silver grains were localized on the luminal side of the proximal tubules at 5-30 min. In the medulla, silver grains appeared at the basal side of the collecting ducts, capillaries and loops of Henle after 5 min. Silver grains then accumulated in the cytoplasm of the collecting ducts after 10 min, and disappeared after 30 min. The cell height of the inner medullary collecting ducts (IMCD) decreased and their luminal spaces increased dose-dependently 5 min after the injection of both labeled and unlabeled guanylin. These structural changes returned to control levels within 30 min. These results indicate a high density localization of guanylin receptors on the luminal surface of proximal tubules in the renal cortex and also rapid excretion of guanylin through the IMCD. The morphological changes of the IMCD suggest a diuretic effect of guanylin.
Guanylin, structurally related to the heat-stable enterotoxin of E. coli, is a 15-amino-acid peptide isolated from rat small intestine. We investigated the morphological effects of an intravenous injection of rat and human guanylin upon the rat intestine. Various doses of rat guanylin were injected intravenously in anesthetized rats. After 5, 10 and 30 min, rats were killed by intracardiac perfusion with aldehyde fixative, and specimens of the intestine were then prepared for light and electron microscopy. Intravenously injected rat guanylin rapidly induced mucus secretion from crypt goblet cells in the duodenum. About half of the crypt goblet cells secreted mucous granules by compound exocytosis within 5 min. The villus goblet cells, in contrast, were not sensitive to guanylin. Goblet cells in the jejunum were less responsive than those in the duodenum. This secretory response was rare in the ileum and colon. Human guanylin produced similar results. The mucus secretion induced by guanylin was inhibited by a prior-injection of atropine, but not hexamethonium. Moreover, guanylin induced intense edema in the mucosa and submucosa of the small intestine 5 min after the injection, which disappeared after 30 min. A prior-injection of atropine did not block the appearance of edema. In conclusion, the intravenous injection of guanylin induces two phenomena related to water movement: (1) compound exocytosis of mucous granules from crypt goblet cells in the rat duodenum and jejunum; (2) perineural, inter-epithelial and intra-epithelial edema in the rat small intestine.
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