Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-3-26
pubmed:databankReference
pubmed:abstractText
Human cDNAs encoding the precursor to pituitary adenylate cyclase activating polypeptide (PACAP) were cloned from human testis and cerebral cortex cDNA libraries. Nucleotide sequencing revealed that cDNA from the testis library encoded the entire precursor for PACAP, while cDNA from the brain library represented only the carboxy-terminal half of the precursor. The predicted human PACAP precursor consisted of 176 amino acid residues and was very similar to the ovine one (82%). Both human and ovine precursors contained both PACAP and another peptide, PACAP-related peptide (PRP), having 29 amino acids. PACAP and PRP were preceded and followed by paired basic amino acids, recognized as important for post-translational processing. The PACAP precursor resembles the vasoactive intestinal peptide (VIP) precursor, which contains VIP and peptide histidine methionine/isoleucine amide (PHM/PHI). Structurally, PRP had some similarity to PHM/PHI, growth hormone-releasing hormone (GRH) and PACAP. Northern blot analysis indicated that a 3.0-kb transcript was expressed in the ovine hypothalamus. Tissue distribution of PACAP mRNA was also clarified in the rat. Southern blot analysis of human genomic DNA gives single bands with six restriction enzymes, indicating that a single copy of the PACAP gene is contained in a haploid genome. The cDNA for human PACAP precursor was expressed using COS-7 and Chinese hamster ovary (CHO) cells. Immunoreactive PACAP was secreted into the culture media of both transfected cell lines.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1044-5498
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21-30
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed-meshheading:1739432-Amino Acid Sequence, pubmed-meshheading:1739432-Animals, pubmed-meshheading:1739432-Base Sequence, pubmed-meshheading:1739432-Blotting, Northern, pubmed-meshheading:1739432-Blotting, Southern, pubmed-meshheading:1739432-DNA, pubmed-meshheading:1739432-Humans, pubmed-meshheading:1739432-Hypothalamus, pubmed-meshheading:1739432-Male, pubmed-meshheading:1739432-Molecular Sequence Data, pubmed-meshheading:1739432-Neuropeptides, pubmed-meshheading:1739432-Peptide Fragments, pubmed-meshheading:1739432-Peptides, pubmed-meshheading:1739432-Pituitary Adenylate Cyclase-Activating Polypeptide, pubmed-meshheading:1739432-Protein Precursors, pubmed-meshheading:1739432-RNA, Messenger, pubmed-meshheading:1739432-Rats, pubmed-meshheading:1739432-Sheep, pubmed-meshheading:1739432-Testis
pubmed:articleTitle
Primary structure and characterization of the precursor to human pituitary adenylate cyclase activating polypeptide.
pubmed:affiliation
Tsukuba Research Laboratories, Takeda Chemical Industries, Ibaraki, Japan.
pubmed:publicationType
Journal Article