Linked Life Data

15504731

Source:http://linkedlifedata.com/resource/pubmed/id/15504731

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2004-12-31
pubmed:abstractText
Peptide YY (PYY) and neuropeptide Y (NPY) are regulatory peptides synthesized in the intestine and brain, respectively, that modify physiological functions affecting nutrient assimilation and feeding behavior. Because PYY and NPY also alter the expression of intestine-specific differentiation marker proteins and the tetraspanin CD63, which is involved in cell adhesion, we investigated whether intestinal cell differentiation could be linked to mucosal cell adhesion and migration through these peptides. PYY and NPY significantly decreased cell adhesion and increased cell migration in a dose-dependent manner prior to cell confluency in our model system, non-tumorigenic small intestinal hBRIE 380i cells. Both peptides reduced CD63 expression and CD63-dependent cell adhesion. CD63 overexpression increased and antisense CD63 cDNA decreased intestinal cell adhesion. In parallel, both PYY and NPY increased expression of matrix metalloproteinase-3 (MMP-3) to a level sufficient to induce cell migration by activating the Rho GTPase Cdc42. The effects of both peptides on cell migration were blocked in cells constitutively overexpressing dominant-negative Cdc42. PYY and NPY also significantly induced the expression of the differentiation marker villin, which could be eliminated by an MMP inhibitor at a concentration that inhibits cell migration. Increased MMP-3 activity, which enhanced cell migration, also induced villin mRNA levels. Therefore, these data indicate that the alteration of adhesion and migration by PYY and NPY occurs in part by synchronous modulation of three proteins that are involved in extracellular matrix-basolateral membrane interactions, CD63, MMP-3 and Cdc42, and that PYY/NPY regulation of expression of mucosal proteins such as villin is linked to the process of cell migration and adhesion.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
125-36
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:15504731-Animals, pubmed-meshheading:15504731-Antigens, CD, pubmed-meshheading:15504731-Antigens, CD63, pubmed-meshheading:15504731-Cell Adhesion, pubmed-meshheading:15504731-Cell Differentiation, pubmed-meshheading:15504731-Cell Line, pubmed-meshheading:15504731-Cell Movement, pubmed-meshheading:15504731-Dose-Response Relationship, Drug, pubmed-meshheading:15504731-Gene Expression Regulation, pubmed-meshheading:15504731-Intestine, Small, pubmed-meshheading:15504731-Matrix Metalloproteinase 3, pubmed-meshheading:15504731-Membrane Proteins, pubmed-meshheading:15504731-Microfilament Proteins, pubmed-meshheading:15504731-Neuropeptide Y, pubmed-meshheading:15504731-Peptide YY, pubmed-meshheading:15504731-Platelet Membrane Glycoproteins, pubmed-meshheading:15504731-Rats, pubmed-meshheading:15504731-Signal Transduction, pubmed-meshheading:15504731-cdc42 GTP-Binding Protein
pubmed:year
2005
pubmed:articleTitle
Peptide YY and neuropeptide Y induce villin expression, reduce adhesion, and enhance migration in small intestinal cells through the regulation of CD63, matrix metalloproteinase-3, and Cdc42 activity.
pubmed:affiliation
Department of Nutritional Sciences and Toxicology, University of California, Berkeley, California 94720-3104, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, N.I.H., Extramural