Mosaic expression of membrane peptidases by confluent cultures of Caco‐2 cells

FEBS Letters

Brewis, Ian A.¹  Hooper, Nigel M.¹  Turner, Anthony J.¹  Howell, Steven¹  Kenny, A.John¹ 

[1] Department of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, UK

关键词: Membrane peptidase;    Immunofluorescent staining;    Caco-2 cell;    ACE;    angiotensin converting enzyme;    AP-N;    aminopeptidase N;    AP-W;    aminopeptidase W;    DPPIV;    dipeptidylpeptidase IV;    E-24.11;    endopeptidase-24.11;    FITC;    fluorescein isothiocyanate;    PBS;    phosphate-buffered saline;   

DOI  :  10.1016/0014-5793(93)81502-Q

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The cell-surface expression of endopeptidase-24.11 (EC 3.4.24.11) on Caco-2 cells cultured to confluency is markedly heterogeneous unlike that of dipeptidylpeptidase IV (EC 3.4.14.5). Here we have investigated the cell-surface expression of three other ectopeptidases: angiotensin converting enzyme (EC 3.4.15.1), aminopeptidase N (EC 3.4.11.2) and aminopeptidase W (EC 3.4.11.16). We show by indirect immunofluorescent staining that these three enzymes are present on the surface of some cells but not on others. However, these enzymes were detected in the majority of detergent-permeabilised Caco-2 cells indicating the presence of intracellular pools of these enzymes. This suggests that there may either be differential regulation of apical transport for these peptidases or that they recycle at different rates.

【 授权许可】

Unknown