PMID- 15504731
OWN - NLM
STAT- MEDLINE
DCOM- 20050721
LR  - 20210206
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 280
IP  - 1
DP  - 2005 Jan 7
TI  - 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.
PG  - 125-36
AB  - 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.
FAU - Lee, Mike
AU  - Lee M
AD  - Department of Nutritional Sciences and Toxicology, University of California, 
      Berkeley, California 94720-3104, USA.
FAU - Hadi, Margono
AU  - Hadi M
FAU - Hallden, Gunnel
AU  - Hallden G
FAU - Aponte, Gregory W
AU  - Aponte GW
LA  - eng
GR  - DK58592/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, U.S. Gov't, P.H.S.
DEP - 20041025
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antigens, CD)
RN  - 0 (Cd63 protein, rat)
RN  - 0 (Membrane Proteins)
RN  - 0 (Microfilament Proteins)
RN  - 0 (Neuropeptide Y)
RN  - 0 (Platelet Membrane Glycoproteins)
RN  - 0 (Tetraspanin 30)
RN  - 0 (Vil1 protein, rat)
RN  - 106388-42-5 (Peptide YY)
RN  - EC 3.4.24.17 (Matrix Metalloproteinase 3)
RN  - EC 3.6.5.2 (cdc42 GTP-Binding Protein)
SB  - IM
MH  - Animals
MH  - Antigens, CD/physiology
MH  - Cell Adhesion/drug effects/physiology
MH  - Cell Differentiation/drug effects/physiology
MH  - Cell Line
MH  - Cell Movement/drug effects/*physiology
MH  - Dose-Response Relationship, Drug
MH  - Gene Expression Regulation/physiology
MH  - Intestine, Small/cytology/*physiology
MH  - Matrix Metalloproteinase 3/physiology
MH  - Membrane Proteins/physiology
MH  - Microfilament Proteins/*biosynthesis/*physiology
MH  - Neuropeptide Y/pharmacology/*physiology
MH  - Peptide YY/pharmacology/*physiology
MH  - Platelet Membrane Glycoproteins
MH  - Rats
MH  - Signal Transduction
MH  - Tetraspanin 30
MH  - cdc42 GTP-Binding Protein/physiology
EDAT- 2004/10/27 09:00
MHDA- 2005/07/22 09:00
CRDT- 2004/10/27 09:00
PHST- 2004/10/27 09:00 [pubmed]
PHST- 2005/07/22 09:00 [medline]
PHST- 2004/10/27 09:00 [entrez]
AID - S0021-9258(20)76572-5 [pii]
AID - 10.1074/jbc.M408858200 [doi]
PST - ppublish
SO  - J Biol Chem. 2005 Jan 7;280(1):125-36. doi: 10.1074/jbc.M408858200. Epub 2004 Oct 
      25.