Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-8-12
pubmed:databankReference
pubmed:abstractText
Five protein families are needed to encompass the diversity of cyclic-AMP (cAMP) phosphodiesterases (PDE). Family IV PDEs (PDE IV) specifically hydrolyze cAMP with a low Km, and are selectively inhibited by rolipram (Rp) and related drugs. Cloned cDNAs from rat (r) suggest that the PDE IV family comprises four distinct members, designated A, B, C and D. Using RN from a human lymphocytic B-cell line (43D-Cl2), we have isolated a 3.8-kb cDNA by low-stringency screening using a rat PDE IV member B (r-PDE IVB) probe. Expression of the human (h) cDNA in Escherichia coli results in cAMP-specific PDE activity that is Rp sensitive. A single large open reading frame (ORF) predicts a 564-amino-acid protein with 92.9% identity to r-PDE IVB; at the nucleotide level the identity is 86.3%. This h-PDE IVB clone, HPB106, differs from a related cDNA clone isolated by others from h-monocytes [Livi et al., Mol. Cell. Biol. 10 (1990) 2678-2686]. Our analysis identifies the monocyte clone with r-PDE IVA. Southern blots using a 1.2-kb h-PDE IVB probe at low stringency suggest the presence of additional uncloned human PDE IV family members. Analysis of genomic Southern blots using short specific probes from the h-PDE IVA and h-PDE IVB cDNAs indicates that distinct genes encode these two PDE IV family members. RNA from fractionated normal human leukocytes shows major specific messages of 3.0 and 4.6 kb for h-PDE IVA and 3.7 kb for h-PDE IVB.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
129
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
239-47
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:8392015-3',5'-Cyclic-AMP Phosphodiesterases, pubmed-meshheading:8392015-Alternative Splicing, pubmed-meshheading:8392015-Amino Acid Sequence, pubmed-meshheading:8392015-Animals, pubmed-meshheading:8392015-B-Lymphocytes, pubmed-meshheading:8392015-Base Sequence, pubmed-meshheading:8392015-Binding Sites, pubmed-meshheading:8392015-Blotting, Northern, pubmed-meshheading:8392015-Blotting, Southern, pubmed-meshheading:8392015-Cell Line, pubmed-meshheading:8392015-DNA, Recombinant, pubmed-meshheading:8392015-Escherichia coli, pubmed-meshheading:8392015-Genetic Variation, pubmed-meshheading:8392015-Humans, pubmed-meshheading:8392015-Isoenzymes, pubmed-meshheading:8392015-Molecular Sequence Data, pubmed-meshheading:8392015-Multigene Family, pubmed-meshheading:8392015-Polymerase Chain Reaction, pubmed-meshheading:8392015-Protein Processing, Post-Translational, pubmed-meshheading:8392015-Pyrrolidinones, pubmed-meshheading:8392015-RNA, Messenger, pubmed-meshheading:8392015-Rats, pubmed-meshheading:8392015-Recombinant Fusion Proteins, pubmed-meshheading:8392015-Rolipram, pubmed-meshheading:8392015-Sequence Analysis, DNA, pubmed-meshheading:8392015-Sequence Homology, Amino Acid
pubmed:year
1993
pubmed:articleTitle
The cDNA of a human lymphocyte cyclic-AMP phosphodiesterase (PDE IV) reveals a multigene family.
pubmed:affiliation
Syntex Discovery Research, Institute of Bio-Organic Chemistry, Palo Alto, CA 94304.
pubmed:publicationType
Journal Article