M. Nakamuta et al., MOUSE MICROSOMAL TRIGLYCERIDE TRANSFER PROTEIN LARGE SUBUNIT - CDNA CLONING, TISSUE-SPECIFIC EXPRESSION, AND CHROMOSOMAL LOCALIZATION, Genomics, 33(2), 1996, pp. 313-316
Microsomal triglyceride transfer protein (MTP) catalyzes the transfer
of triglyceride, cholesteryl ester, and phospholipid between membranes
. It is essential for the secretion of apolipoprotein B from the cell.
Mutations in MTP are a major cause of abetalipoproteinemia. The mouse
is a popular animal model for lipoprotein metabolism. We have cloned
and sequenced mouse MTP cDNA. The DNA-deduced amino acid sequence indi
cates that mouse MTP contains 894 amino acids; the mouse protein shows
93, 86, and 83% sequence identity to the hamster, human, and bovine s
equences, respectively. Northern blot analysis indicates that mouse MT
P mRNA is expressed at high levels in the small intestine and at subst
antially lower levels in the liver and that it is not detectable in si
x other tissues examined. The mouse MTP gene has been localized to the
distal region of chromosome 3 by Southern blots of interspecific back
cross panels using progeny derived from matings of (C57BL/BJ x SPRET/E
i)F1 x SPRET/Ei. Comparison of MTP sequences from human, bovine, hamst
er, and mouse indicates that the C-terminal region of MTP is better co
nserved than its N-terminal region, (C) 1996 Academic Press, Inc.