Human apolipoprotein (apo) B plays an obligatory role in the assembly and secretion of hepatic triglyceride-rich lipoproteins. Investigation of the truncated human apoB variants associated with hypobetalipoproteinemia has suggested that both size and secretion of apoB-containing lipoproteins may be reduced by carboxyl-terminal truncation. To examine the role of the carboxyl terminus of apoB in the assembly and secretion of hepatic lipoproteins, we have generated rat hepatoma McA-RH7777 cells that synthesize and secrete the full-length human apoB100 and the truncated forms B94, B88, B80, B72, and B60. In the resulting lipoproteins, particle density was inversely related to the logarithm of apoB length, ranging from 1.019 g/ml for apoB100 to 1.06 g/ml for B60. Furthermore, particle diameter (as determined by non-denaturing gel electrophoresis) was directly correlated with apoB length, ranging from 21.4 nm for apoB100 to 17.7 nm for B60. The relationship between apoB length and particle geometry was best defined by a linear correlation between length and core volume; a 10% decrease in apoB length resulted in an approximately 13% decrease in core volume. These observations, which are in agreement with the observations of aberrant lipoproteins in hypobetalipoproteinemia, suggest that lipid recruitment by apoB is progressively reduced by carboxyl-terminal truncation. However, pulse-chase studies indicated that carboxyl-terminal truncation did not impair apoB secretion. The recombinant human apoB forms were secreted as efficiently as endogenous rat apoB100; approximately 20% of total newly synthesized apoB72, B80, or B100 was secreted at the end of the chase. Intracellular degradation of newly synthesized apoB was observed for both the truncated human and the endogenous rat proteins. These data suggest that the low apoB levels in hypobetalipoproteinemia might not be caused by impaired secretion of the truncated apoB proteins.