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Vol 49, No 4 (2011)
Review paper
Submitted: 2012-01-16
Published online: 2012-01-16
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Cathepsin E (EC 3.4.23.34) — a review

Michał Chlabicz, Marek Gacko, Anna Worowska, Radosław Łapiński
DOI: 10.5603/FHC.2011.0078
·
Folia Histochem Cytobiol 2011;49(4):547-557.

open access

Vol 49, No 4 (2011)
REVIEW
Submitted: 2012-01-16
Published online: 2012-01-16

Abstract

Cathepsin E belongs to the third class of enzymes — hydrolases, a subclass of peptide bond hydrolases and a sub-subclass of endopeptidases with aspartic catalytic sites. Cathepsin E is an endopeptidase with substrate specificity similar to that of cathepsin D. In a human organism, cathepsin E occurs in: erythrocytes, thymus, dendritic cells, epithelial M cells, microglia cells, Langerhans cells, lymphocytes, epithelium of gastrointestinal tract, urinary bladder, lungs, osteoclasts, spleen and lymphatic nodes. In human cells, loci of the gene of pre-procathepsin E are located on chromosome 1 in the region 1231-32. The catalytic site of cathepsin E is two residues of aspartic acid — Asp96 and Asn281, occurring in amino acid triads with sequences DTG96-98 and DTG281-283. To date, no particular role of cathepsin E in the metabolism of proteins in normal tissues has been found. However, it is known that there are many documented pathological conditions in which overexpression of cathepsin E occurs. (Folia Histochemica et Cytobiologica 2011; Vol. 49, No. 4, pp. 547–557)

Abstract

Cathepsin E belongs to the third class of enzymes — hydrolases, a subclass of peptide bond hydrolases and a sub-subclass of endopeptidases with aspartic catalytic sites. Cathepsin E is an endopeptidase with substrate specificity similar to that of cathepsin D. In a human organism, cathepsin E occurs in: erythrocytes, thymus, dendritic cells, epithelial M cells, microglia cells, Langerhans cells, lymphocytes, epithelium of gastrointestinal tract, urinary bladder, lungs, osteoclasts, spleen and lymphatic nodes. In human cells, loci of the gene of pre-procathepsin E are located on chromosome 1 in the region 1231-32. The catalytic site of cathepsin E is two residues of aspartic acid — Asp96 and Asn281, occurring in amino acid triads with sequences DTG96-98 and DTG281-283. To date, no particular role of cathepsin E in the metabolism of proteins in normal tissues has been found. However, it is known that there are many documented pathological conditions in which overexpression of cathepsin E occurs. (Folia Histochemica et Cytobiologica 2011; Vol. 49, No. 4, pp. 547–557)

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Keywords

cathepsin E; cathepsin D

About this article
Title

Cathepsin E (EC 3.4.23.34) — a review

Journal

Folia Histochemica et Cytobiologica

Issue

Vol 49, No 4 (2011)

Article type

Review paper

Pages

547-557

Published online

2012-01-16

Page views

2426

Article views/downloads

3538

DOI

10.5603/FHC.2011.0078

Bibliographic record

Folia Histochem Cytobiol 2011;49(4):547-557.

Keywords

cathepsin E
cathepsin D

Authors

Michał Chlabicz
Marek Gacko
Anna Worowska
Radosław Łapiński

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