Linked Life Data

6146265

Source:http://linkedlifedata.com/resource/pubmed/id/6146265

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1 Pt 1
pubmed:dateCreated
1984-8-20
pubmed:abstractText
The binding of 125I-[Tyr11]somatostatin to guinea pig pancreatic acini was saturable and temperature, protein, and radioligand concentration dependent. Dissociation rate was very slow (t1/2 = 193 +/- 24 min). Scatchard analysis revealed a single class of binding sites with a Kd of 0.28 +/- 0.02 nM and a maximal binding capacity of 72 +/- 10.6 fmol/mg prot. There was a strong correlation between binding capacity and extracellular calcium concentration. Incubating acini in EGTA-containing medium with no added Ca2+ caused a 50% decrease in maximal binding capacity with a decrease in receptor affinity. Furthermore, in the absence of calcium, bound somatostatin was rapidly released (t1/2 = 14 +/- 1 min). Subcellular fractionation studies and acid treatment of acini incubated with the tracer showed that most of the somatostatin binding sites were located on the cell surface. Agents that altered cellular calcium in pancreatic acini, such as analogues of cholecystokinin and cholinergic agents, also inhibited the binding of 125I-[Tyr11]somatostatin by a calcium-dependent process. We conclude that somatostatin binds to specific plasma membrane receptors to form a slowly reversible complex that is highly reactive with calcium. Cell calcium-mobilizing agents decrease the affinity of acinar somatostatin receptors for somatostatin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0002-9513
pubmed:author
pubmed:issnType
Print
pubmed:volume
247
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
G62-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Binding of somatostatin to pancreatic acinar cells.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't