Graduate Thesis Or Dissertation
 

Characterization of a cDNA encoding a procine adipocyte membrane protein

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  • In recent years, the general public has recognized the dangers of a high fat diet and are demanding meat with lower fat content. This demand has stimulated research in the growth and regulation of adipocytes. However, despite much effort, no adipocyte-specific plasma membrane markers from any species are available as an aid to accurately distinguish adipocytes from non-adipocytes. One potential candidate for such a marker in porcine adipocytes has been identified by Killefer and Hu (1990b). Characterization of the cDNA for this protein, designated porcine adipocyte membrane protein (PAMP), is presented here. Sequence for the 910 by clone is 80% similar to an internal region of a rat prostaglandin F[subscript 2α] receptor regulator protein (FPRP) described by Orlickey (1996). Western blot analysis suggests that the pig protein is a homotetramer held together with disulfide bonds which form very close to the transmembrane region making the tetramer extremely difficult to reduce to monomeric units. Oligonucleotide primers were designed to amplify a genomic fragment by the polymerase chain reaction (PCR) and for a reverse transcriptase PCR (RT-PCR) assay to study the expression of the mRNA. A 2114 bp genomic clone revealed one intron in the coding region. A serum-free primary cell culture system was used to study the expression of the mRNA. Although message was detected every day over a ten day period, it appeared to peak between 6 to 8 days after plating. The PAMP protein is clearly of the same family as the rat FPRP but its size and conformation are quite different so it is not clear what function it performs in porcine adipocytes. Further experiments should focus on attaining full length cDNA's, confirming the molecular conformation of the protein, and assessing its function in a serum-free primary cell culture system.
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