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Science 15 April 1994:
Vol. 264. no. 5157, pp. 430 - 433
DOI: 10.1126/science.8153632
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Articles

Science, Vol 264, Issue 5157, 430-433
Copyright © 1994 by American Association for the Advancement of Science

articles

Association of intestinal peptide transport with a protein related to the cadherin superfamily

AH Dantzig, JA Hoskins, LB Tabas, S Bright, RL Shepard, IL Jenkins, DC Duckworth, Sportsman JR, D Mackensen, PR Rosteck Jr, and al. et

Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN 46285.

The first step in oral absorption of many medically important peptide-based drugs is mediated by an intestinal proton-dependent peptide transporter. This transporter facilitates the oral absorption of beta-lactam antibiotics and angiotensin-converting enzyme inhibitors from the intestine into enterocytes lining the luminal wall. A monoclonal antibody that blocked uptake of cephalexin was used to identify and clone a gene that encodes an approximately 92-kilodalton membrane protein that was associated with the acquisition of peptide transport activity by transport-deficient cells. The amino acid sequence deduced from the complementary DNA sequence of the cloned gene indicated that this transport-associated protein shares several conserved structural elements with the cadherin superfamily of calcium-dependent, cell-cell adhesion proteins.


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