Proton NMR assignment and secondary structure of the calcium-free form of the amino-terminal epidermal growth factor like domain in coagulation factor X

Biochemistry ◽  
1990 ◽  
Vol 29 (35) ◽  
pp. 8111-8118 ◽  
Author(s):  
Maria Selander ◽  
Egon Persson ◽  
Johan Stenflo ◽  
Torbjoern Drakenberg
Keyword(s):  
Growth Factor ◽  
Secondary Structure ◽  
Epidermal Growth Factor ◽  
Nmr Assignment ◽  
Proton Nmr ◽  
Coagulation Factor ◽  
Free Form ◽  
Factor X ◽  
Amino Terminal ◽  
Epidermal Growth

scholarly journals The juxtamembrane regions of the epidermal growth factor receptor and gp185erbB-2 determine the specificity of signal transduction.

1991 ◽  
Vol 11 (6) ◽  
pp. 3191-3202 ◽  
Author(s):  
O Segatto ◽  
F Lonardo ◽  
D Wexler ◽  
F Fazioli ◽  
J H Pierce ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Tyrosine Kinase ◽  
Mutational Analysis ◽  
Growth Factor Receptor ◽  
Tyrosine Kinase Domain ◽  
Amino Terminal ◽  
Epidermal Growth

The epidermal growth factor receptor (EGFR) and gp185erbB-2 are closely related tyrosine kinases. Despite extensive sequence and structural homology, these two receptors display quantitative and qualitative differences in their ability to couple with mitogenic signalling pathways. By using chimeric molecules between EGFR and erbB-2, we found that the determinants responsible for the specificity of mitogenic signal transduction are located in the amino-terminal half of the tyrosine kinase domain of either receptor. In the EGFR, mutational analysis within this subdomain revealed that deletion of residues 660 to 667 impaired receptor mitogenic activity without affecting its tyrosine kinase properties. This sequence is therefore likely to contribute to the specificity of substrate recognition by the EGFR kinase.

Epidermal growth factor prohormone is secreted in human urine

1992 ◽  
Vol 263 (1) ◽  
pp. E142-E150 ◽  
Author(s):  
J. Lakshmanan ◽  
E. C. Salido ◽  
R. Lam ◽  
D. A. Fisher
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Molecular Mass ◽  
Human Urine ◽  
Age Groups ◽  
Adult Males ◽  
Rat Urine ◽  
Immunoreactive Protein ◽  
Amino Terminal ◽  
Epidermal Growth

Examination of adult human urine by immunoblot analysis with antiserum specific to human recombinant 6-kDa epidermal growth factor (EGF) reveals the presence of an immunoreactive protein with a molecular mass of 165 kDa. This protein is consistently found in the morning (first) but not in day urine of adult males and females. Day urine contains variable proportions of four other high-molecular-weight EGFs with approximate molecular masses of 97, 66, 50, and 42 kDa. The 165-kDa EGF immunoreactive protein reacts with mouse amino-terminal EGF prohormone (proEGF) antiserum and comigrates with mouse urinary proEGF, suggesting that the protein is the human EGF prohormone. The 165-kDa human proEGF exhibits strong binding affinity to concanavalin A, indicating that it is glycosylated. Immunoblotting of urine in infants and children of various age groups demonstrates the presence of proEGF in all age groups, but its concentration is highest in children 2-4 yr of age. These findings, taken together with secretion of proEGF of similar molecular mass in mouse and rat urine, suggest that renal proEGF secretion is an evolutionarily conserved phenomenon and may have an important function or functions distal to the site of its synthesis.

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