Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
1992-6-11
|
pubmed:abstractText |
The possible role of second messenger systems in androgen-dependent smooth muscle proliferation was investigated. Focusing on the hormone-sensitive guinea pig seminal vesicle, we analyzed changes in protein kinase C (PKC) and cAMP-dependent type I and II protein kinases during the androgen-dependent smooth muscle proliferation of puberty, as well as in the transition to the nonproliferative state of the adult. The androgenic sensitivity of the cAMP-dependent type I and II protein kinases and the cAMP-dependent phosphorylations of soluble muscle proteins did not correlate with the qualitative change in the androgenic sensitivity of the prepubertal vs. adult animals. In contrast to the cAMP-dependent protein kinases, regulation of the soluble and particulate forms of PKC corresponded to the androgen-induced smooth muscle proliferation. That is, in the seminal vesicle muscle of prepubertal castrated animals, androgen treatment reduced both the soluble and particulate forms of PKC during the increase in smooth muscle DNA synthesis, and in adult seminal vesicle smooth muscle, which was resistant to androgen-induced proliferation, both forms of the enzyme were resistant to androgenic stimulation. It is concluded that PKC may be a component of an autocrine mitogenic mechanism involved in the coupling and uncoupling of androgen-induced smooth muscle proliferation.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Androgens,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Thymidine,
http://linkedlifedata.com/resource/pubmed/chemical/Tritium
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0006-3363
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
46
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
551-60
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:1315580-Androgens,
pubmed-meshheading:1315580-Animals,
pubmed-meshheading:1315580-Cell Division,
pubmed-meshheading:1315580-Cyclic AMP,
pubmed-meshheading:1315580-DNA,
pubmed-meshheading:1315580-Genitalia, Male,
pubmed-meshheading:1315580-Guinea Pigs,
pubmed-meshheading:1315580-Male,
pubmed-meshheading:1315580-Muscle, Smooth,
pubmed-meshheading:1315580-Phosphorylation,
pubmed-meshheading:1315580-Protein Kinases,
pubmed-meshheading:1315580-Second Messenger Systems,
pubmed-meshheading:1315580-Seminal Vesicles,
pubmed-meshheading:1315580-Thymidine,
pubmed-meshheading:1315580-Tritium
|
pubmed:year |
1992
|
pubmed:articleTitle |
Protein kinases and the androgen-induced proliferation of accessory sex organ smooth muscle.
|
pubmed:affiliation |
Department of Periodontology, JHMHC, University of Florida, Gainesville 32610.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|