Authors: Tsukuba, Takayuki¹; Yanagawa, Michiyo²; Okamoto, Kuniaki¹; Okamoto, Yoshiko³; Yasuda, Yoshiyuki⁴; Nakayama, Keiichi I.⁵; Kadowaki, Tomoko⁶; Yamamoto, Kenji⁷

Source: The Journal of Biochemistry, Volume 145, Number 5, 27 May 2009 , pp. 565-573(9)

Publisher: Oxford University Press

Abstract:

Cathepsin E is an endo-lysosomal aspartic proteinase exclusively present in immune system cells. Previous studies have shown that cathepsin E-deficient (CatE^-/-) mice display aberrant immune responses such as atopic dermatitis and higher susceptibility to bacterial infection. However, the mechanisms underlying abnormal immune responses induced by cathepsin E deficiency are still unclear. In this study, we found that the cell-surface levels of chemotactic receptors, including chemokine receptor (CCR)-2 and N-formyl peptide receptors (FPRs), were clearly diminished in CatE^-/-macrophages compared with those in wild-type cells. Consistently, chemotaxis of CatE^-/-macrophages to MCP-1 and N-formyl-methionyl-leucyl-phenylalanine was also decreased. Similar to the chemotactic receptors, the surface expressions of the adhesion receptors CD18 (integrin β₂) and CD 29 (integrin β₁) in CatE^-/- macrophages were significantly decreased, thereby reducing cell attachment of CatE^-/- macrophages. These results indicate that the defects in chemotaxis and cell adhesion are likely to be involved in the imperfect function of CatE^-/-macrophages.

Keywords: aspartic proteinase; cathepsin E; knockout; macrophages; chemotaxis; cell adhesion

Document Type: Regular paper

DOI: http://dx.doi.org/10.1093/jb/mvp016

Affiliations: 1: Department of Dental Pharmacology, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki 852-8588; , 2: Department of Fixed Prosthodontics, Graduate School of Dental Science, Kyushu University, Fukuoka 812-8582; , 3: Department of Biochemistry, Daiichi University College of Pharmaceutical Sciences, Fukuoka 815-8511; , 4: Division of Clinical Cariology and Endodontology, Department of Oral Rehabilitation, School of Dentistry, Health Sciences University of Hokkaido, Hokkaido, 061-0293; , 5: Department of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582; , 6: Pharmacology, Graduate School of Dental Science, Kyushu University, Fukuoka 812-8582; and , 7: Proteolysis Research Laboratory, Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka 812-8582, Japan,

Publication date: 2009-05-27

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