The cellular changes that take place as the intestinal cell migrates from crypt to villus are morphologically and biochemically remarkable. It is fortunate that many of these phenomena can be delineated by following enzymic activities. Sucrase-isomaltase is a particularly fascinating enzyme complex because it is a marker of the differentiated cell. Sucrase is inducible with steroids and protected by the substrate sucrose. Purified enzyme can be used to stimulate production of specific antibodies in goats; these antibodies have been used as probes to locate enzymically active and inactive antigen in the cells of the crypt and villus respectively. Further examination of the enzyme has indicated a molecular weight of 200 000--350 000. These higher molecular weight components are located in the brush border of the enterocytes. Lower molecular weight subunits are antigenically active and are in the cytosol. It is assumed that these smaller components are enzymically inactive pre-combination subunits of the sucrase-isomaltase complex and that the sucrase-isomaltase of the brush border is an aggregate of these subunits. The California sea lion, which is deficient in intestinal sucrase activity, does have isomaltase activity. This finding supports the concept that there are different gene complexes for sucrase and for isomaltase.

Aging↗

PubMedDate not supplied

Development of glutaminase along the villus-crypt axis in the jejunum of rat.

The activity of glutaminase (E.C. 3.5.1.2), the entry enzyme for oxidation of glutamine, was measured in enterocytes isolated along the villus-crypt axis from rat jejunum. Specific activity of glutaminase was 5.05 +/- 0.24 mumol glutamate/mg protein/h in villus cells (fully differentiated cells) and 4.16 +/- 0.30 in the deep crypt (undifferentiated cells). Activity of glutaminase was significantly (p less than 0.05) increased in cells isolated from the villus-crypt junction (differentiating cells) compared to the activity of the enzyme in both the villus and crypt at 6.21 +/- 0.45. A similar pattern of activity of glutaminase was observed when the cells of the villus-crypt gradient were separated by sequential horizontal sectioning with a cryostat. Oxidation of L-[U-14C]glutamine to 14CO2 was also significantly (p less than 0.01) higher in cells isolated from the villus-crypt junction compared to both villus or deep crypt cells. The quantity of glutaminase protein was determined by a dot immunobinding assay using an antibody to purified glutaminase. Immunoreactive glutaminase protein relative to total cellular protein was 6.06 +/- 0.40 cpm/microgram homogenate protein in the villus cells, 3.01 +/- 0.24 (p less than 0.05) at the villus-crypt junction, and 4.49 +/- 0.57 (p less than 0.05) in the deep crypt. Thus, the highest activity of glutaminase present in the villus-crypt junction is the result of an increase in activity of the enzyme rather than an increase in the enzyme protein.

Animals↗

PubMedDate not supplied

Some aspects of urea and pyrimidine metabolism during development.

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Animals↗