Developmental changes in the mechanisms of duodenal calcium transport in the rat

Am J Physiol. 1983 Jan;244(1):G20-6. doi: 10.1152/ajpgi.1983.244.1.G20.

Abstract

Duodenal calcium transport was resolved into a saturable and a nonsaturable process by means of an in situ ligated loop procedure applied to Wistar rats at 3, 12, 19, 24, 30, 40, 60, 110, and 150 days of age. All postweaning animals were males that had been placed on a 1.5% calcium, 1.5% phosphorus semisynthetic diet. Duodenal calcium-binding protein (CaBP) levels were determined at all ages. The newborn rat had no saturable transport component and no CaBP. Its nonsaturable component was very high. With increasing age the saturable component and CaBP varied biphasically, increasing steeply until the animals were about 35 days old; thereafter, each decreased to low but detectable values. The nonsaturable component, on the other hand, decreased in near-linear fashion in the first 35 days; in animals beyond that age it remained invariant. The difference in age dependence between the saturable and nonsaturable components may be considered to constitute additional evidence for the existence of the two transport processes. CaBP and the saturable transport process were highly correlated, further proof that both are vitamin D dependent. Histological studies have revealed the presence of many vacuoles in the intestinal cells of the very young rats; these vacuoles were absent in rats older than 35 days. It is suggested that these vacuoles may be implicated in a pinocytosislike nonsaturable transport that is superimposed on the nonsaturable, non-vitamin D-dependent calcium transport found in all enterocytes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aging*
  • Animals
  • Biological Transport
  • Calcium / metabolism*
  • Calcium-Binding Proteins / metabolism*
  • Duodenum / metabolism*
  • Duodenum / ultrastructure
  • Female
  • Intestinal Absorption
  • Male
  • Rats
  • Rats, Inbred Strains
  • Vacuoles / ultrastructure

Substances

  • Calcium-Binding Proteins
  • Calcium