cDNAs encoding major plasma apolipoproteins (apo) were cloned from the eel
Anguilla japonica liver and their nucleotide sequences determined. Sodium d
odecyl sulfate-polyacrylamide gel electrophoresis revealed that eel lipopro
teins contain apolipoproteins of 28 kDa and 14 kDa as major components. Eac
h of the two apolipoproteins showed two isoforms having different isoelectr
ic points as demonstrated by two-dimensional electrophoresis. The two 28 kD
a components had different N-terminal amino acid sequences, whereas the two
14 kDa components had an identical one. Then cDNA clones encoding these ap
olipoproteins were isolated from a cDNA library constructed from the eel li
ver. An acidic 28 kDa component (28 kDa-1) consisted of 259 amino acids inc
luding a putative signal peptide of 27 residues, whereas a basic 28 kDa com
ponent (28 kDa-2) was composed of 260 amino acids containing a putative sig
nal peptide of 23 residues. The tandem repeating units, which are character
istic of apolipoproteins, for 28 kDa-l showed 27.8% identity to that of por
cine apoA-IV, although mammalian apoA-IV is about 40 kDa and much larger th
an 28 kDa-l. However, the repeating units of 28 kDa-2 showed 52.5% identity
to that of Atlantic salmon apoA-I. The 14 kDa apolipoprotein consisted of
142 amino acids containing a putative signal peptide of 20 residues. It has
a novel sequence differing from apolipoproteins of other vertebrates. The
transcriptional expressions of 28 kDa-l, 28 kDa-2., and 14 kDa components w
ere all restricted to the liver, except for the transcripts of 28 kDa-2 whi
ch were also slightly expressed in the intestine. (C) 2001 Elsevier Science
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