2013م - 1444هـ
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The nervous system is composed of a diverse population of cells selectively

expressing different genes which ultimately determine the type of neurotransmitters and neuropeptides produced and released. Neuropeptide tyrosine (NPY)

is one of the most abundant and widely expressed peptides in the mammalian

nervous system (1). It was originally isolated by virtue of a chemical assay that

detects the presence of a carboxyl-terminal amide in proteins (2); a hallmark of

potential hormonal function. Its widespread expression in the central and

peripheral nervous systems, in addition to the carboxyl-terminal amide, suggested that NPY could be a critical neurotransmitter in a variety of neuronal

processes. We were therefore interested in obtaining the cDNA for human NPY

in order to study NPY gene expression and screen for the NPY gene (3,4). The

only available information was the amino acid sequence of porcine NPY and

the amino acid sequences of two related peptides, pancreatic polypeptide and

peptide YY (5,6). These experiments were performed in the early 1980s before

the advent of genome sequencing and polymerase chain reaction (PCR) technology. Today, experiments to obtain cDNAs for proteins for which only amino

acid sequence is available are designed very differently and include computer

searches of nucleotide databases and/or various PCR strategies. The experiments described in this chapter represent the classical way by which cDNAs

were cloned from corresponding protein sequence.