Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-8-6
pubmed:abstractText
Treatment of rice cells with an endogenous mitogenic peptide, phytosulfokine-alpha (PSK-alpha), results in cell proliferation. In the present study, [3H]PSK-alpha prepared by catalytic reduction of a PSK-alpha analog containing tetradehydroisoleucine was employed to identify putative PSK-alpha target molecules on rice plasma membranes. Membrane binding of the ligand was found to be saturable, reversible and pH dependent. Scatchard analysis demonstrated the existence of both high- and low-affinity binding sites with Kd values of 1.4 nM and 27 nM, respectively. Competition studies with [3H]PSK-alpha and several PSK-alpha analogs showed that displacing activity closely corresponds to the ability to induce cell proliferation. The properties of the binding sites distributed on plasma membranes are consistent with the function of PSK-alpha receptors in activating a cascade of molecular events involved in plant cell proliferation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
262
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
666-71
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Characterization of specific binding sites for a mitogenic sulfated peptide, phytosulfokine-alpha, in the plasma-membrane fraction derived from Oryza sativa L.
pubmed:affiliation
Laboratory of Bioactive Natural Products Chemistry, Graduate School of Bioagricultural Sciences, Nagoya University, Chkusa, Japan. matsu@agr.nagoya-u.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't