Modulation of the endosomal and lysosomal distribution of cathepsins B, L and S in human monocytes/macrophages

被引:18
作者
Schmid, H
Sauerbrei, R
Schwarz, G
Weber, E
Kalbacher, H
Driessen, C
机构
[1] Univ Klinikum Tubingen, Inst Pathol, D-72076 Tubingen, Germany
[2] Univ Tubingen, Inst Physiol Chem, D-72076 Tubingen, Germany
[3] Univ Tubingen, Med Nat Wissensch Forschungszentrum, D-72074 Tubingen, Germany
[4] Univ Halle Wittenberg, Inst Physiol Chem, D-06097 Halle Saale, Germany
[5] Univ Klinikum Tubingen, Innere Med Abt 2, D-72076 Tubingen, Germany
关键词
antigen presentation; enzyme secretion; limited proteolysis; major histocompatibility complex class II; maturation; phagocytosis;
D O I
10.1515/BC.2002.143
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Endosomal and lysosomal fractions of human monocytes/ macrophages prepared from buffy coats were analyzed for activities of cathepsins B, L and S, and expression of cathepsin proteins along with major histocompatibility complex class I and class II molecules under control and immunomodulatory conditions. While the total activity of cathepsins B, L, and S together remained unchanged in lysates of control cells during culture for 72 h, the subcellular distribution of cathepsin activities underwent a shift from a predominantly endosomal localization in freshly isolated cells to a lysosomal pattern after 72 h of culture. Interferon[gamma] treatment for 72 h resulted in an upregulation of both major histocompatibility complex proteins and cathepsins with differential changes in cathepsin B, L and S activities in endosomes versus lysosomes. These changes suggest a remodeling of the endocytic machinery and imply different functions of cathepsins B, L and S during monocyte differentiation.
引用
收藏
页码:1277 / 1283
页数:7
相关论文
共 39 条
[1]  
ABRAHAMSON M, 1994, METHOD ENZYMOL, V244, P685
[2]   Splice variants of human cathepsin L mRNA show different expression rates [J].
Abudula, A ;
Rommerskirch, W ;
Weber, E ;
Günther, D ;
Wiederanders, B .
BIOLOGICAL CHEMISTRY, 2001, 382 (11) :1583-1591
[3]   Endosomal proteolysis of internalized proteins [J].
Authier, F ;
Posner, BI ;
Bergeron, JJM .
FEBS LETTERS, 1996, 389 (01) :55-60
[4]  
Beck H, 2001, EUR J IMMUNOL, V31, P3726, DOI 10.1002/1521-4141(200112)31:12<3726::AID-IMMU3726>3.0.CO
[5]  
2-O
[6]   PHYSIOLOGICAL FUNCTIONS OF ENDOSOMAL PROTEOLYSIS [J].
BERG, T ;
GJOEN, T ;
BAKKE, O .
BIOCHEMICAL JOURNAL, 1995, 307 :313-326
[7]   Major histocompatibility complex class II-associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L [J].
Bevec, T ;
Stoka, V ;
Pungercic, G ;
Dolenc, I ;
Turk, V .
JOURNAL OF EXPERIMENTAL MEDICINE, 1996, 183 (04) :1331-1338
[8]   Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs [J].
Bogyo, M ;
Verhelst, S ;
Bellingard-Dubouchaud, V ;
Toba, S ;
Greenbaum, D .
CHEMISTRY & BIOLOGY, 2000, 7 (01) :27-38
[9]   PROTEASES AND PROTEOLYSIS IN THE LYSOSOME [J].
BOHLEY, P ;
SEGLEN, PO .
EXPERIENTIA, 1992, 48 (02) :151-157
[10]  
Boyum A, 1968, SCAND J CLIN LAB I S, P9777