Expression of a 70-kDa Immunoreactive Form of Bile Salt-Dependent Lipase by Human Pancreatic Tumoral Mia PaCa-2 Cells

摘要: Abstract This work describes the characterization of an immunoreactive form bile salt-dependent lipase (BSDL) expressed by human pancreatic tumoral Mia PaCa-2 cell line. BSDL-related protein, which has M r 70 kDa, is enzymatically active and poorly secreted. Furthermore, a protein with same electrophoretic migration can also be immunoprecipitated polyclonal antibodies specific for BSDL after in vitro translation RNA isolated from cells. These data indicated that this might poorly, or not, glycosylated. Reverse transcription amplification extracted cells using primers able to specifically amplify full-length mRNA resulted detectable 1.8-kb cDNA product, shorter than (2.2 kb). The sequence transcript corresponds codes mature BSDL. However, deletion 330 bp located within 3′-domain cDNA. Therefore allowed us conclude 70-kDa 612 amino acid length represents truncated 110 acids occurs C-terminal region encompasses 6 tandemly repeated sequences instead 16 normally present Because feto-acinar (FAPP), oncofetal counterpart BSDL, C-terminally isoform it suggested MiaPaCa-2 could representative moiety FAPP.