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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0007586,
umls-concept:C0009017,
umls-concept:C0017262,
umls-concept:C0040287,
umls-concept:C0084688,
umls-concept:C0162801,
umls-concept:C0185117,
umls-concept:C0205314,
umls-concept:C0220927,
umls-concept:C0679622,
umls-concept:C1550548,
umls-concept:C1555714,
umls-concept:C1705654,
umls-concept:C2003905,
umls-concept:C2911684
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pubmed:issue |
1
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pubmed:dateCreated |
1998-2-3
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pubmed:databankReference | |
pubmed:abstractText |
Suppressin (SPN) is an inhibitor of cell proliferation that was originally identified and purified to homogeneity from bovine pituitaries (LeBoeuf, R. D., Burns, J. N., Bost, K. L., and Blalock, J. E. (1990) J. Biol. Chem. 265, 158-165). In this report we have cloned the full-length cDNA encoding rat SPN and have identified the tissue distribution of SPN expression. The cDNA of SPN is 1882 nucleotides with a 1488-base coding region and 55 and 339 nucleotides of 5'- and 3'-untranslated sequences, respectively. Northern gel analysis of rat pituitary mRNA showed a single hybridizing species at approximately 2 kilobases. Sequence analyses showed that the nucleotide and deduced amino acid sequences of SPN are novel and unrelated to any known vertebrate inhibitors of proliferation. However, the deduced amino acid sequence of SPN contains two domains that have extensive sequence identity with a recently cloned transcription activator in Drosophila, deformed epidermal autoregulatory factor-1 (DEAF-1, see Gross, C. T., and McGinnis, W. (1996) EMBO J. 15, 1961-1970) suggesting that SPN represents a vertebrate cognate of deformed epidermal autoregulatory factor-1. Reverse transcriptase-polymerase chain reaction and immunohistochemical analyses showed that the SPN mRNA and the SPN protein are expressed in every tissue examined including testis, spleen, skeletal muscle, liver, kidney, heart, and brain suggesting that SPN may be involved in the control of proliferation in a variety of cell types.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
361-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9417089-Amino Acid Sequence,
pubmed-meshheading:9417089-Animals,
pubmed-meshheading:9417089-Base Sequence,
pubmed-meshheading:9417089-Cattle,
pubmed-meshheading:9417089-Cell Cycle,
pubmed-meshheading:9417089-Cloning, Molecular,
pubmed-meshheading:9417089-DNA, Complementary,
pubmed-meshheading:9417089-Male,
pubmed-meshheading:9417089-Molecular Sequence Data,
pubmed-meshheading:9417089-Pituitary Gland,
pubmed-meshheading:9417089-Rats,
pubmed-meshheading:9417089-Rats, Sprague-Dawley,
pubmed-meshheading:9417089-Recombinant Proteins,
pubmed-meshheading:9417089-Sequence Homology, Amino Acid,
pubmed-meshheading:9417089-Structure-Activity Relationship,
pubmed-meshheading:9417089-Thymus Hormones
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pubmed:year |
1998
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pubmed:articleTitle |
Molecular cloning, sequence analysis, expression, and tissue distribution of suppressin, a novel suppressor of cell cycle entry.
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pubmed:affiliation |
Department of Physiology and Biophysics, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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