- Authors: Mikaelsson, E., Osterborg, A., Jeddi-Tehrani, M., Kokhaei, P., Ostadkarampour, M., Hadavi, R., Gholamin, M., Akhondi, M., Shokri, F., Rabbani, H., Mellstedt, H.
- Year: 2013
- Journal: PLoS One 8 e67601
- Applications: in vitro / DNA / jetPEI
- Cell type: Sp2/0-Ag14
Description: Mouse plasma myeloma cells.
Known as: SP2/0-Ag14; SP2/0-AG14; SP2/0-ag14; Sp2/O-Ag14; SP2/O-Ag14; Sp2/0-Ag-14; SP2-0-Ag14; SP2/0 Ag-14; SP-2/0-AG14; Sp 2/0-Ag 14; Sp2/0; SP2/0; Sp2/O; SP2/O; SP-2; SP2; GM03569; GM03569B; GM3569.
Proline/arginine-rich end leucine-rich repeat protein (PRELP) belongs to the small leucine-rich proteoglycan (SLRP) family, normally expressed in extracellular matrix of collagen-rich tissues. We have previously reported on another SLRP, fibromodulin (FMOD) in patients with chronic lymphocytic leukemia (CLL). PRELP is structurally similar to FMOD with adjacent localization on chromosome 1 (1q32.1). As cluster-upregulation of genes may occur in malignancies, the aim of our study was to analyze PRELP expression in CLL. PRELP was expressed (RT-PCR) in all CLL patients (30/30), as well as in some patients with mantle cell lymphoma (3/5), but not in healthy donor leukocytes (0/20) or tumor samples from other hematological malignancies (0/35). PRELP was also detected in CLL cell-lines (4/4) but not in cell-lines from other hematological tumors (0/9). PRELP protein was detected in all CLL samples but not in normal leukocytes. Deglycosylation experiments revealed a CLL-unique 38 kDa core protein, with an intact signal peptide. This 38 kDa protein was, in contrast to the normal 55 kDa size, not detected in serum which, in combination with the uncleaved signal peptide, suggests cellular retention. The unique expression of a 38 kDa PRELP in CLL cells may suggest involvement in the pathobiology of CLL and merits further studies.