B. Ottesen et al., EXPRESSION AND CHARACTERIZATION OF PREPROVIP DERIVED PEPTIDES IN THE HUMAN MALE UROGENITAL TRACT, Neuropeptides, 28(4), 1995, pp. 227-236
Expression of the gene sequence encoding vasoactive intestinal polypep
tide (VIP) leads to the synthesis of a 170 amino acid precursor molecu
le which can be processed to five fragments: preproVIP 22-79, peptide
histidine methionine (PHM), or peptide histidine valine (PHV), preproV
IP 111-122, VIP and preproVIP 156-170. Using region specific radioimmu
noassays and antisera against the functional domains of the VIP precur
sor in combination with immunocytochemistry and chromatography, the lo
calization, distribution and identity of the preproVIP derived peptide
s within the human male urogenital tract were investigated. Postmortem
as well as fresh tissue specimens were used. All the preproVIP derive
d peptides were expressed and could be demonstrated in nerve fibres th
roughout the urogenital tract in close relation to the epithelial lini
ng and in vascular as well as non-vascular smooth muscle. The VIP-rela
ted peptide containing fibres were most abundant in the prostate paren
chyma and the seminal vesicle. Using double immunostaining, co-localiz
ation of the various preproVIP derived peptides could be evidenced. Th
e fact that all preproVIP derived peptides are present in the urogenit
al tract, should be taken into consideration when the regulatory aspec
ts of neuropeptides in physiological and pathophysiological functions
are discussed.