Bone marrow stem/progenitor cell mobilization in C57BL/6J and BALB/c mice.
- Author:
Hakmo LEE
1
;
Jeong Hwan CHE
;
Ju Eun OH
;
Sung Soo CHUNG
;
Hye Seung JUNG
;
Kyong Soo PARK
Author Information
- Publication Type:In Vitro ; Original Article
- Keywords: Bone marrow stem/progenitor cells; Mobilization; AMD3100; G-CSF; Host-related factors
- MeSH: Animals; Bone Marrow*; Ectoderm; Endoderm; Granulocyte Colony-Stimulating Factor; Granulocytes; Humans; Mesoderm; Mice*; Receptors, Lysosphingolipid; Tissue Donors; Fingolimod Hydrochloride
- From:Laboratory Animal Research 2014;30(1):14-20
- CountryRepublic of Korea
- Language:English
- Abstract: Bone marrow (BM) has been considered as a reservoir of stem/progenitor cells which are able to differentiate into ectodermal, endodermal, and mesodermal origins in vitro as well as in vivo. Following adequate stimulation, such as granulocyte stimulating factor (G-CSF) or AMD3100, BM resident stem/progenitor cells (BMSPCs) can be mobilized to peripheral blood. Several host-related factors are known to participate in this mobilization process. In fact, a significant number of donors are resistant to G-CSF induced mobilization protocols. AMD3100 is currently used in combination with G-CSF. However, information regarding host-related factors which may influence the AMD3100 directed mobilization is extremely limited. In this study, we were to get some more knowledge on the host-related factors that affect the efficiency of AMD3100 induced mobilization by employing in vivo mobilization experiments. As a result, we found that C57BL/6J mice are more sensitive to AMD3100 but less sensitive to G-CSF which promotes the proliferation of BMSPCs. We excluded S1P as one of the host related factor which influences AMD3100 directed mobilization because pre-treatment of S1P receptor antagonist FTY720 did not inhibit BMSPC mobilization. Further in vitro experiments revealed that BALB/c mice, compared to C57BL/6J mice, have less BMSPCs which migrate in response to host related factors such as sphingosine-1-phosphate (S1P) and to CXCL12. We conclude that AMD3100-directed mobilization depends on the number of BMSPCs rather than on the host-related factors. These results suggest that the combination of AMD3100 and G-CSF is co-operative and is optimal for the mobilization of BMSPCs.
