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

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Reviews of Physiology, Biochemistry and Pharmacology

Part of the book series: Reviews of Physiology, Biochemistry and Pharmacology ((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.

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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

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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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Authors and Affiliations

  1. Institute of Food Nutrition and Human Health, Massey University, Private Bag 121222, Palmerston North, New Zealand

    Diane Hooton & Roger Lentle

  2. The New Zealand Institute for Plant & Food Research Limited, Food Industry Science Centre, Batchelar Road, Palmerston North, 4474, New Zealand

    Diane Hooton, John Monro & Robert Simpson

  3. Reacta Biotech Limited, Manchester, UK

    Martin Wickham

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Editors and Affiliations

  1. KU Leuven, Leuven, Belgium

    Bernd Nilius

  2. Klinikum der Universität München Abteilung, München, Bayern, Germany

    Thomas Gudermann

  3. Max-Planck-Inst for Biophysical Chemistr, Göttingen, Niedersachsen, Germany

    Reinhard Jahn

  4. University of Marburg, Marburg, Hessen, Germany

    Roland Lill

  5. Cardiff School of Biosciences, Cardiff University, Cardiff, United Kingdom

    Ole H. Petersen

  6. Dept. of Cell and Molec. Physiology, Loyola University Chicago, MAYWOOD, Illinois, USA

    Pieter P. de Tombe

Declaration of Interest

Declaration of Interest

This paper was funded by a Ministry for Business Innovation and Employment (MBIE) grant.

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© 2015 Springer International Publishing Switzerland

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Hooton, D., Lentle, R., Monro, J., Wickham, M., Simpson, R. (2015). The Secretion and Action of Brush Border Enzymes in the Mammalian Small Intestine. In: Nilius, B., Gudermann, T., Jahn, R., Lill, R., Petersen, O., de Tombe, P. (eds) Reviews of Physiology, Biochemistry and Pharmacology. Reviews of Physiology, Biochemistry and Pharmacology, vol 168. Springer, Cham. https://doi.org/10.1007/112_2015_24

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