Brush border, intestinal

Mooseker, M.S. (1985). Organization, chemistry, and assembly of the cytoskeletal apparatus of the intestinal brush border. Ann. Rev. Cell Biol. 1, 209-241. 

Sodium/glucose cotransporter (rabbit intestinal brush borders)1641 Stearylcoenzyme A desaturase (rat liver microsomal)[651 Subtilopeptidase amylosacchariticus[661 Succinate dehydrogenase (mitochondrial)1671... 

Proulx, P., Structure-function relationships in intestinal brush border membranes, Biochim. Biophys. Acta 1071, 255-271 (1991). 

H Yuasa, D Fleisher, GL Amidon. Noncompetitive inhibition of cephradine uptake by enalapril in rabbit intestinal brush-border membrane vesicles An enalapril specific inhibitory binding site on the peptide carrier. J Pharmacol Exp Ther 269 1107-1111, 1994. 

Aminopeptidase A is another brush border membrane enzyme which has been the subject of various studies [79,81,83-86], It has been found in the intestinal brush border membrane of humans, rabbits, rats, and pigs and is active against peptides with acidic amino acids at the amino terminus. Its activity against dipeptides is more limited. Shoaf et al., isolated three rat brush border aminopeptidases with distinct but somewhat overlapping substrate specificities. These enzymes had preference for dipeptides containing methionine, arginine, or aspartic acid and glycine. The optimal pH for activity of aminopeptidase was reported to be 7-8. 

N Triadou, J Bataille, J Schmitz. Longitudinal study of the human intestinal brush border membrane proteins. Distribution of the main disaccharidases and peptidases. Gastroenterology 85 1326-1332, 1983. 

EJ Brophy, YS Kim. Effect of amino acids on purified rat intestinal brush-border membrane aminooligopeptidase. Gastroenterology 78 82-87, 1979. 

N Tobey, W Heizer, R Yeh, T Huang, C Hoffner. Human intestinal brush border peptidases. Gastroentrology 88 913-926, 1985. 

M Yoshioka, RH Erickson, YS Kim. Digestion and assimilation of proline-con-taining peptide by rat intestinal brush border membrane carboxypeptidases. Role... 

M Yoshioka, RH Erikson, JF Woodly, R Gulb, D Guam, YS Kim. Role of rat intestinal brush-border membrane angiotensin-converting enzyme in dietary protein digestion. Am J Physiol 253 G-781-G-786, 1987. 

Di- and tripeptides Aminopeptidases Hydrolyze di- and tripeptides into amino acids Absorptive cells of small intestine Brush border of absorptive cells... 

Poschet, J. F., S. M. Hammond, and P. D. Fairclough. Characterisation of penicillin-G uptake in rabbit small-intestinal brush-border membrane vesicles. Biochim. Biophys. Acta 1996, 1278, 233-240. 

Kitagawa, S., J. Takeda, and S. Sato. pH-dependent inhibitory effects of angiotensin-converting enzyme inhibitors on cefroxadine uptake by rabbit small intestinal brush-border membrane vesicles and their relationship with hydrophobicity and the ratio of zwitterionic species. Biol. Pharm. Bull. 1999, 22, 721-724. 

Hashimoto, N., et al. Renin inhibitor transport mechanism in rat small intestinal brush-border membrane vesicles. Pharm. Res. 1994, 11, 1448— 1451. 

Takano, M., et al. Bestatin transport in rabbit intestinal brush-border membrane vesicles. Biochem. Pharmacol. 1994, 47, 1089-1090. 

Inui, K., et al. H+ coupled active transport of bestatin via the dipeptide transport system in rabbit intestinal brush-border membranes. J. Pharmacol. Exp. Ther. 1992, 260, 482-486. 

Patil, S. D. and J. D. Unadkat. Sodium-dependent nucleoside transport in the human intestinal brush-border membrane. Am. J. Physiol. 

Takanaga, H., et al. Nicotinic acid transport mediated by pH-dependent anion antiporter and proton cotransporter in rabbit intestinal brush-border membrane. J. Pharm. Pharmacol. 1996, 48, 1073-1077. 

Tsuji, A. and I. Tamai. Na+ and pH dependent transport of foscamet via the phosphate carrier system across intestinal brush-border membrane. Biochem. Pharmacol 1989, 38, 1019— 1022. 

Ishizawa, T., et al. Sodium and pH dependent carrier-mediated transport of antibiotic, fosfomydn, in the rat intestinal brush-border membrane. J. Pharmacobiodyn. 1990, 13, 292—300. 

Riepe S, Goldstein J, Alpers DH Effect of secreted Bacteroides proteases on human intestinal brush border hydrolases. J Clin Invest 1980 66 314-322. 

Fig. 6.11. Peptide prodrugs (6.20, 6.21, and 6.22) for the intestine-selective delivery of 5-aminosalicylic acid (6.23). The prodrugs undergo selective activation by intestinal brush border enzymes, namely aminopeptidase A and/or carboxypeptidases [39].

Fructose is found in honey and fruit and as part of the disaccharide sucrose (common table sugar). Sucrose is hydrolyzed by intestinal brush border sucrase, and the resulting monosaccharides, glucose and fructose, are absorbed into the portal blood. The liver phosphorylates frurtose and cleaves it into glyceraldehyde and DHAP. Smaller amounts are metabolized in renal proximal tubules. The pathway is shown in Figure 1-12-7 important enzymes to remember are ... 

Kobayashi, M., Suruga, S., Takeuchi, H., Sugawara, M., Iseki, K., and Miyazaki, K. A structure-relationship study of the uptake of aliphatic polyamine compounds by rat intestinal brush-border membrane vesicles, / Pharm. Pharmacol., 49(5) 511-515, 1997. 

Choudhury BR, Poddar MK. (1985) Andrographolide and Kalmegh (Andrographis paniculata) extract Effect on intestinal brush-border membrane bound hydrolases. Methods Find Exp Clin Pharmacol 7 617-621. 

These zinc-dependent endopeptidases (meprin A [EC 3.4.24.18] and meprin B [EC 3.4.24.63] ) are members of the peptidase family M12A. They catalyze the hydrolysis of peptide bonds in proteins and peptide substrates. Meprin A, a membrane-bound enzyme that has been isolated from mouse and rat kidney and intestinal brush borders as well as salivary ducts, acts preferentially on carboxyl side of hydrophobic amino acyl residues. Meprin A and B are insensitive to inhibition by phosphora-midon and thiorphan. 

Orally administered drugs partition into the lipid bilayer in the process of diffusing across the apical and basolateral membranes of the intestinal brush border cells into the blood, as illustrated in Figure 2. About 1800 such drugs are commercially available. A small surface area of the polar parts of the drug molecule generally favors entry into the hydrophobic interior of... 

In general, ethanol in low to moderate amounts, is relatively benign to most body systems. A moderate amount of ethanol causes peripheral vasodilation, especially of cutaneous vessels, and stimulates the secretion of salivary and gastric fluids the latter action may aid digestion. On the other hand, ethanol consumption in high concentrations, as found in undiluted spirits, can induce hemorrhagic lesions in the duodenum, inhibit intestinal brush border enzymes, inhibit the uptake of amino acids, and limit the absorption of vitamins and minerals. In addition, ethanol can reduce blood testosterone levels, resulting in sexual dysfunction. 

Insulin secretion stimulation. Oil, administered orally to young suckling rabbits, quickened and strengthened the rise of immunoreactive serum insulin ". Intestinal brush border membrane. Oil, administered orally to rats at a dose of 10% for 5 weeks, produced an increase in level of saturated fatty acids in the brush border membrane from coconut oil-fed animals. Membrane fluidity was as follows coconut oil less than commercial pellet diet less than corn oil less than fish oil. The membrane hexose content was high in the coconut-fed rats. Hexamines were elevated in coconut-treated rat brush borders. The activities of alkaline phosphatase, sucrase, and lactase were increased "". 

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