Yoichi Matsubara

Intestinal fatty acid-binding protein as a sensitive marker of intestinal ischemia.

Determination of the serum level of intestinal fatty acid-binding protein has been used to detect rat intestinal ischemia following ligation or 30-min occlusion of the superior mesenteric artery. The normal values were under the minimal detectable level of less than 2 ng/ml in all the 10 rats. The serum fatty acid-binding protein level increased rapidly, to 340.7±54.6, 438.5±40.1, 388.1±37.4, and 292.2±95.7 ng/ml (P<0.01) at 1, 2, 4, and 8 hr after ligation respectively. It also increased, to 347.2±127.7 ng/ml (P<0.01) at 1 hr, after a 30-min transient occlusion and then returned to a normal level. Histological studies showed destruction of the villi, disappearance of the mucosa, and transmural necrosis with the progress of time after ligation, while no remoarkable morphological change was observed following 30-min transieent occlusion. These observations strongly suggest that the intestinal fatty acid-binding protein is a useful biochemical marker for intestinal ischemia, particularly in the early reversible phase.

Met-enkephalin-immunoreactive and gastrin-immunoreactive cells in the human and canine pyloric antrum

Abstract Localization of met-enkephalin and gastrin-immunoreactive cells in the human and canine pyloric antrum was studied by an indirect immunofluorescence technique using anti-met-enkephalin and anti-gastrin antisera. The met-enkephalin immunoreactive cells were identical to gastrin immunoreactive ones, and these cells were located in the neck portion of the human and canine pyloric glands. Since immunocytological cross-reactions between met-enkephalin and anti-gastrin antiserum and between gastrin and anti-met-enkephalin antiserum were not detected, the coexistence of met-enkephalin and gastrin in one and the same cell of pyloric antrum is most likely.

Possible role of rat fatty acid-binding proteins in the intestine as carriers of phenol and phthalate derivatives

Fatty acid-binding proteins of hepatic and intestinal type and gastrotropin-like protein (GTLP) were purified from rat intestinal cytosol by Sephadex G-75 gel filtration and DEAE-cellulose, CM-cellulose, and hydroxylapatite chromatographies. In addition to fatty acids, butylated hydroxytoluene (BHT), phthalate dibutyl, and di(2-ethylhexyl) esters (DBP and DEHP) were identified by gas liquid chromatography and mass spectrometry as endogenous ligands from the extract of either fatty acid-binding protein superfamily. These protein families in the intestine may have an important role as carriers in the initial step of arresting these exogenous pollutants.

Does somatostatin in the gut inhibit the GLI release locally

SummaryBased on the assumption that somatostatin may inhibit peptide release through junctional complexes or through local circulation, an immunofluorescent technique for somatostatin and GLI in the gut was applied in order to investigate whether suppression of GLI release by i.v. administration of somatostatin was a physiological effect of somatostatin or not. Somatostatin-immunoreactive cells (GIF-cells) in the human and canine intestine had no direct cellular contacts with GLI-immunoreactive cells (GLI-cells). This finding suggests that somatostatin in the intestine does not inhibit GLI release through junctional complexes between GIF- and GLI-cells. As to the local circulation, most of GIF-cells in the canine intestine were distributed in the deeper portion of the intestinal gland which corresponds to the upstream sides of the local blood supply of the intestinal gland, as reported byReynold et al. The ratio of GIF-cells to total cells (GIF-cells + GLI-cells) was 68% in the duodenum and 25% in the ileum. In contrast, a limited number of GIF-cells was found in the human duodenum where a few GLI-cells were distributed and a few GIF-cells were seen in the human ileum where a large number of GLI-cells were located. Findings in the dog suggest the possibility that somatostatin inhibits GLI release from GLI-cells through the local circulation system of intestinal glands. However, findings in humans suggest that the same possibility does not apply to the human gut. Differences of population density of intestinal GIF-cells between humans and dogs indicate that the functional meaning of GIF-cells may vary from one species to another.