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The Secretion and Action of Brush Border Enzymes in the Mammalian Small Intestine

  • Diane Hooton
  • Roger LentleEmail author
  • John Monro
  • Martin Wickham
  • Robert Simpson
Part of the Reviews of Physiology, Biochemistry and Pharmacology book series (REVIEWS, volume 168)

Abstract

Microvilli are conventionally regarded as an extension of the small intestinal absorptive surface, but they are also, as latterly discovered, a launching pad for brush border digestive enzymes. Recent work has demonstrated that motor elements of the microvillus cytoskeleton operate to displace the apical membrane toward the apex of the microvillus, where it vesiculates and is shed into the periapical space. Catalytically active brush border digestive enzymes remain incorporated within the membranes of these vesicles, which shifts the site of BB digestion from the surface of the enterocyte to the periapical space. This process enables nutrient hydrolysis to occur adjacent to the membrane in a pre-absorptive step. The characterization of BB digestive enzymes is influenced by the way in which these enzymes are anchored to the apical membranes of microvilli, their subsequent shedding in membrane vesicles, and their differing susceptibilities to cleavage from the component membranes. In addition, the presence of active intracellular components of these enzymes complicates their quantitative assay and the elucidation of their dynamics. This review summarizes the ontogeny and regulation of BB digestive enzymes and what is known of their kinetics and their action in the peripheral and axial regions of the small intestinal lumen.

Keywords

Digestion Enterocyte Membrane Microvillus Vesicles 

Abbreviations

ACE

Angiotensin-converting enzyme

ALP

Alkaline phosphatase

APA

Aminopeptidase A

APN

Aminopeptidase N

APP

Aminopeptidase P

AS

Alkaline sphingomyelinase

BB

Brush border

BBMV

Brush border membrane vesicle

BSAL

Bile salt-activated lipase

CPA

Carboxypeptidase A

CPB

Carboxypeptidase B

DP1

Dipeptidase 1

DPPIV

Dipeptidylpeptidase IV

GGT

γ-Glutamyl transpeptidase

GPI

Glycophosphatidylinositol

LPH

Lactase–phlorizin hydrolase

MEP

Meprin A subunit β

MGAM

Maltase–glucoamylase

NC

Neutral ceramidase

NEP

Neprilysin

NTC

Sodium taurocholate

PLA2

Phospholipase A2

PLB1

Phospholipase B1

PTL

Pancreatic triacylglycerol lipase

PTL

Pancreatic triacylglycerol lipase

RER

Rough endoplasmic reticulum

SC

Soluble cytosolic

SI

Sucrase–isomaltase

Notes

Acknowledgments

We would like to extend a special thank-you to Peter Butterworth (Kings College, London, United Kingdom) for reviewing the manuscript; Juliet Ansell, Christine Butts (Plant and Food Research, Palmerston North, New Zealand), and Kevin Sutton (Plant and Food Research, Lincoln, New Zealand) for proof reading the manuscript; Tony Corbett (Plant and Food Research, Hawkes Bay) for the graphics; and Doug Hopcroft and Jianyu Chen from the Manawatu Microscopy and Imaging Centre, Massey University, Palmerston North, for the transmission electron microscope images of the BBMV.

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Copyright information

© Springer International Publishing Switzerland 2015

Authors and Affiliations

  • Diane Hooton
    • 1
    • 2
  • Roger Lentle
    • 1
    Email author
  • John Monro
    • 2
  • Martin Wickham
    • 3
  • Robert Simpson
    • 2
  1. 1.Institute of Food Nutrition and Human HealthMassey UniversityPalmerston NorthNew Zealand
  2. 2.The New Zealand Institute for Plant & Food Research Limited, Food Industry Science CentrePalmerston NorthNew Zealand
  3. 3.Reacta Biotech LimitedManchesterUK

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