Identification of bile canalicular cell surface antigen HAM.4 as dipeptidyl peptidase IV (DPPIV) and characterization of its role in hepatic regeneration after partial hepatectomy in rats
M. Tsugiki et al., Identification of bile canalicular cell surface antigen HAM.4 as dipeptidyl peptidase IV (DPPIV) and characterization of its role in hepatic regeneration after partial hepatectomy in rats, DIG DIS SCI, 43(12), 1998, pp. 2591-2600
Dipeptidyl peptidase IV (DPPIV) has been implicated in the control of cell
growth and differentiation. A rat hepatocyte membrane antigen recognized by
a monoclonal antibody (HAM.4) has now been shown to be identical to DPPIV
by immunoblot analysis and amino acid sequencing. The amounts of DPPIV immu
noreactive protein and enzymatic activity in serum increased in a manner in
dependent of de novo protein synthesis, and without any biochemical or immu
nohistochemical changes in hepatic DPPIV, during liver regeneration after p
artial hepatectomy in rats. DPPIV purified from serum by HAM.4 antibody-bas
ed affinity chromatography lacked the NH2-terminal 36 amino acids of the me
mbrane-bound enzyme, suggesting that proteolytic cleavage may mediate the r
elease of DPPIV into serum. No significant differences in the restoration o
f liver mass or in hepatic DNA synthesis were apparent between DPPIV-defici
ent and normal rats after partial hepatectomy, suggesting that DPPIV may no
t be essential for hepatic regeneration.