PMID- 2821619
OWN - NLM
STAT- MEDLINE
DCOM- 19871120
LR  - 20220318
IS  - 0036-8075 (Print)
IS  - 0036-8075 (Linking)
VI  - 238
IP  - 4826
DP  - 1987 Oct 23
TI  - New perspectives in cell adhesion: RGD and integrins.
PG  - 491-7
AB  - Rapid progress has been made in the understanding of the molecular interactions 
      that result in cell adhesion. Many adhesive proteins present in extracellular 
      matrices and in the blood contain the tripeptide arginine-glycine-aspartic acid 
      (RGD) as their cell recognition site. These proteins include fibronectin, 
      vitronectin, osteopontin, collagens, thrombospondin, fibrinogen, and von 
      Willebrand factor. The RGD sequences of each of the adhesive proteins are 
      recognized by at least one member of a family of structurally related receptors, 
      integrins, which are heterodimeric proteins with two membrane-spanning subunits. 
      Some of these receptors bind to the RGD sequence of a single adhesion protein 
      only, whereas others recognize groups of them. The conformation of the RGD 
      sequence in the individual proteins may be critical to this recognition 
      specificity. On the cytoplasmic side of the plasma membrane, the receptors 
      connect the extracellular matrix to the cytoskeleton. More than ten proved or 
      suspected RGD-containing adhesion-promoting proteins have already been 
      identified, and the integrin family includes at least as many receptors 
      recognizing these proteins. Together, the adhesion proteins and their receptors 
      constitute a versatile recognition system providing cells with anchorage, 
      traction for migration, and signals for polarity, position, differentiation, and 
      possibly growth.
FAU - Ruoslahti, E
AU  - Ruoslahti E
AD  - La Jolla Cancer Research Foundation, CA 92037.
FAU - Pierschbacher, M D
AU  - Pierschbacher MD
LA  - eng
GR  - CA 28896/CA/NCI NIH HHS/United States
GR  - CA 30199/CA/NCI NIH HHS/United States
GR  - CA 42507/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PT  - Review
PL  - United States
TA  - Science
JT  - Science (New York, N.Y.)
JID - 0404511
RN  - 0 (Glycoproteins)
RN  - 0 (Integrins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Oligopeptides)
RN  - 0 (Receptors, Cell Surface)
RN  - 78VO7F77PN (arginyl-glycyl-aspartic acid)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - *Cell Adhesion
MH  - Extracellular Matrix/physiology
MH  - Glycoproteins
MH  - Integrins
MH  - Membrane Glycoproteins/*physiology
MH  - Membrane Proteins/physiology
MH  - Oligopeptides/*physiology
MH  - Receptors, Cell Surface
RF  - 65
EDAT- 1987/10/23 00:00
MHDA- 1987/10/23 00:01
CRDT- 1987/10/23 00:00
PHST- 1987/10/23 00:00 [pubmed]
PHST- 1987/10/23 00:01 [medline]
PHST- 1987/10/23 00:00 [entrez]
AID - 10.1126/science.2821619 [doi]
PST - ppublish
SO  - Science. 1987 Oct 23;238(4826):491-7. doi: 10.1126/science.2821619.