Tiggrin, a novel Drosophila extracellular matrix protein that functions as a ligand for Drosophila alpha PS2 beta PS integrins.
Genetic and other studies of Drosophila integrins have implicated these extracellular matrix receptors in various morphogenetic events, but identification of their endogenous ligands has been elusive. We report the biochemical purification and cloning of tiggrin, a novel extracellular matrix protein from Drosophila. This 255 x 10(3) M(r) polypeptide contains the potential integrin recognition sequence Arg-Gly-Asp (RGD) and 16 repeats of a novel 73-77 amino acid motif. The tiggrin gene is at chromosome locus 26D1-2 and is expressed by embryonic hemocytes and fat body cells. Tiggrin protein is detected in matrices, especially at muscle attachment sites that also strongly express integrins. Tiggrin-coated surfaces support primary embryo cell culture and provide excellent substrates for alpha PS2 beta PS integrin-mediated cell spreading. Soluble RGD-peptides inhibit this cell spreading.
Fogerty
F J
FJ
Department of Biology, University of California, Los Angeles 90024-1606.
Fessler
L I
LI
Bunch
T A
TA
Yaron
Y
Y
Parker
C G
CG
Nelson
R E
RE
Brower
D L
DL
Gullberg
D
D
Fessler
J H
JH
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015153:Blotting, Western; D003001:Cloning, Molecular; D004330:Drosophila / Q000196:embryology*; D029721:Drosophila Proteins; D004591:Electrophoresis, Polyacrylamide Gel; D016326:Extracellular Matrix Proteins / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D017403:In Situ Hybridization; D039001:Integrin alpha Chains; D016023:Integrins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009024:Morphogenesis / Q000502:physiology; D009132:Muscles / Q000196:embryology; D016415:Sequence Alignment
D029721:Drosophila Proteins; D016326:Extracellular Matrix Proteins; D039001:Integrin alpha Chains; D016023:Integrins; C089678:Tig protein, Drosophila; C082188:if protein, Drosophila