Latent transforming growth factor β-binding protein-3 and fibulin-1C interact with the extracellular domain of the heparin-binding EGF-like growth factor precursor -: art. no. 2

被引:18
作者
Brooke, JS [1 ]
Cha, JH [1 ]
Eidels, L [1 ]
机构
[1] Univ Texas, SW Med Ctr, Dept Microbiol, Dallas, TX 75390 USA
关键词
D O I
10.1186/1471-2121-3-2
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Background: The membrane-bond cell-surface precursor and soluble forms of heparin-binding epidermal growth factor-like growth factor (HB-EGF) contribute to many cellular developmental processes. The widespread occurrence of HB-EGF in cell and tissue types has led to observations of its role in such cellular and tissue events as tumor formation, cell migration, extracellular matrix formation, wound healing, and cell adherence. Several studies have reported the involvement of such extracellular matrix proteins as latent transforming growth factor beta-binding protein, TGF-beta, and fibulin-1 in some of these processes. To determine whether HB-EGF interacts with extracellular matrix proteins we used the extracellular domain of proHB-EGF in a yeast two-hybrid system to screen a monkey kidney cDNA library. cDNA clones containing nucleotide sequences encoding domains of two proteins were obtained and their derived amino acid sequences were evaluated. Results: From approximate to 3 x 10(6) screened monkey cDNA clones, cDNA clones were recovered that contained nucleotide sequences encoding domains of the monkey latent transforming growth factor-beta binding protein-3 (MkLTBP-3) and fibulin-1C protein. The amino acid sequence derived from the MkLTBP-3 gene shared 98.6% identity with h man LTBP-3 and 86.7% identity with mouse LTBP-3 amino acid sequences. The amino acid sequence derived from the monkey fibulin-1C gene shared 97.2% identity with human fibulin-1C. Yeast two-hybrid screens indicate that LTBP-3 and fibulin-1C interact with proHB-EGF through their calcium-binding EGF-like modules. Conclusions: The interactions of the extracellular domain of proHB-EGF with LTBP-3 and fibulin-1C suggest novel functions for HB-EGF between cell and tissue surfaces.
引用
收藏
页数:36
相关论文
共 52 条
[1]   Binding of fibulin-1 to nidogen depends on its C-terminal globular domain and a specific array of calcium-binding epidermal growth factor-like (EG) modules [J].
Adam, S ;
Gohring, W ;
Wiedemann, H ;
Chu, ML ;
Timpl, R ;
Kostka, G .
JOURNAL OF MOLECULAR BIOLOGY, 1997, 272 (02) :226-236
[2]   FIBULIN IS AN EXTRACELLULAR-MATRIX AND PLASMA GLYCOPROTEIN WITH REPEATED DOMAIN-STRUCTURE [J].
ARGRAVES, WS ;
TRAN, H ;
BURGESS, WH ;
DICKERSON, K .
JOURNAL OF CELL BIOLOGY, 1990, 111 (06) :3155-3164
[3]   Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican [J].
Aspberg, A ;
Adam, S ;
Kostka, G ;
Timpl, R ;
Heinegård, D .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (29) :20444-20449
[4]  
BALBONA K, 1992, J BIOL CHEM, V267, P20120
[5]  
BIGNON C, 1994, J BIOL CHEM, V269, P3318
[6]  
BROWN JC, 1994, J CELL SCI, V107, P329
[7]   Heparin binding epidermal growth factor-like growth factor is a transforming growth factor β-regulated gene in intestinal epithelial cells [J].
Bulus, N ;
Barnard, JA .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1999, 264 (03) :808-812
[8]  
Carpenter G., 1990, HDB EXPT PHARM, P69
[9]   Cell surface monkey CD9 antigen is a coreceptor that increases diphtheria toxin sensitivity and diphtheria toxin receptor affinity [J].
Cha, JH ;
Brooke, JS ;
Ivey, KN ;
Eidels, L .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (10) :6901-6907
[10]  
DAVISFLEISCHER KM, 1998, FRONT BIOSCI, V3, P288