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Expression of glutamyl aminopeptidase by osteogenic induction in rat bone marrow stromal cells
Author(s) -
Wu Yao,
Xiao Jingang,
Wu Ling,
Tian Weidong,
Liu Lei
Publication year - 2008
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1016/j.cellbi.2008.02.006
Subject(s) - alkaline phosphatase , stromal cell , microbiology and biotechnology , in vitro , chemistry , bone marrow , biology , biochemistry , enzyme , immunology , cancer research
Glutamyl aminopeptidase (GluAP, EC 3.4.11.7, ENPEP) is a 130‐kDa homodimeric zinc metallopeptidase which specifically cleaves the N‐terminal glutamate or aspartate residue of peptidic substrates such as cholecystokinin‐8 or angiotensin (Ang) II, in vitro . We used a DNA microarray hybridization (Genechip Rat Expression Array 230A, Affymetrix Inc., Santa Clara, CA, USA) to demonstrate that GluAP was upregulated in osteogenic induced rat bone marrow stromal cells (BMSCs). To compare the expression of GluAP in the osteogenic differentiation and non‐osteogenic differentiation of rat BMSCs in vitro , the cells were osteogenic induced in vitro . We also performed an MTT assay, alkaline phosphatase assay, alizarin red staining, and an immunohistochemical analysis to determine the osteogenic differentiation of BMSCs. The expression of GluAP was examined by real‐time polymerase chain reaction (PCR). The real‐time PCR results showed that GluAP was upregulated in osteogenic differentiated BMSCs in vitro , suggesting that GluAP may be correlated with the osteogenic differentiation of BMSCs.