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Inhibitor of DASH proteases affects expression of adhesion molecules in osteoclasts and reduces myeloma growth and bone disease.

Authors :
Pennisi A
Li X
Ling W
Khan S
Gaddy D
Suva LJ
Barlogie B
Shaughnessy JD
Aziz N
Yaccoby S
Source :
British journal of haematology [Br J Haematol] 2009 Jun; Vol. 145 (6), pp. 775-87. Date of Electronic Publication: 2009 Apr 08.
Publication Year :
2009

Abstract

Dipeptidyl peptidase (DPP) IV activity and/or structure homologues (DASH) are serine proteases implicated in tumourigenesis. We previously found that a DASH protease, fibroblast activation protein (FAP), was involved in osteoclast-induced myeloma growth. Here we further demonstrated expression of various adhesion molecules in osteoclasts cultured alone or cocultured with myeloma cells, and tested the effects of DASH inhibitor, PT-100, on myeloma cell growth, bone disease, osteoclast differentiation and activity, and expression of adhesion molecules in osteoclasts. PT-100 had no direct effects on viability of myeloma cells or mature osteoclasts, but significantly reduced survival of myeloma cells cocultured with osteoclasts. Real-time PCR array for 85 adhesion molecules revealed upregulation of 17 genes in osteoclasts after coculture with myeloma cells. Treatment of myeloma/osteoclast cocultures with PT-100 significantly downregulated 18 of 85 tested genes in osteoclasts, some of which are known to play roles in tumourigenesis and osteoclastogenesis. PT-100 also inhibited osteoclast differentiation and subsequent pit formation. Resorption activity of mature osteoclasts and differentiation of osteoblasts were not affected by PT-100. In primary myelomatous severe combined immunodeficient (SCID)-hu mice PT-100 reduced osteoclast activity, bone resorption and tumour burden. These data demonstrated that DASH proteases are involved in myeloma bone disease and tumour growth.

Details

Language :
English
ISSN :
1365-2141
Volume :
145
Issue :
6
Database :
MEDLINE
Journal :
British journal of haematology
Publication Type :
Academic Journal
Accession number :
19388929
Full Text :
https://doi.org/10.1111/j.1365-2141.2009.07696.x