New concepts in regulation and function of the insulin-like growth factors: implications for understanding normal growth and neoplasia

2000 ◽  
Vol 57 (6) ◽  
pp. 932-942 ◽  
Author(s):  
H. Werner ◽  
D. Le Roith*

1990 ◽  
Vol 2 (2) ◽  
pp. 99-109 ◽  
Author(s):  
Margaret C. Eggo ◽  
Laura K. Bachrach ◽  
Gerard N. Burrow


1988 ◽  
Vol 20 (S 7) ◽  
pp. 436-442 ◽  
Author(s):  
S. Gammeltoft ◽  
R. Ballotti ◽  
F. Nielsen ◽  
Aline Kowalski ◽  
E. Van Obberghen


1995 ◽  
Vol 7 (3) ◽  
pp. 333 ◽  
Author(s):  
J Robinson ◽  
S Chidzanja ◽  
K Kind ◽  
F Lok ◽  
P Owens ◽  
...  

The placenta exerts its effects on the growth of the fetus from the beginning of pregnancy via metabolic and endocrine mechanisms. To achieve this, the placenta exchanges a wide array of nutrients, endocrine signals, cytokines and growth factors with the mother and the fetus. These exchanges modulate or programme fetal growth and development. This review concentrates on the function and structure of the placenta in humans and in animals, and the effects of experimental perturbation of placental size and function on fetal growth. The consequences for fetal growth of varying the abundance of peptides or, by deleting genes, insulin-like growth factors or cytokines, are also described. Maternal nutritional and hormonal state from as early as the first few days after fertilization, can influence the growth rate of the placenta and the fetus and also the length of gestation. Influences on placental development and their consequences will clearly have an impact on the placental control of fetal growth. Variations in the maternal environment and consequent perturbation of the metabolic and endocrine environment of the placenta and fetus are implicated as being responsible for the associations between prenatal growth of the placenta and its fetus and the subsequent risk of adult disease. The next challenge will be to determine the dominant influences at each stage of fetal and placental growth.



1985 ◽  
Vol 6 (3) ◽  
pp. 400-420 ◽  
Author(s):  
ELI Y. ADASHI ◽  
CAROL E. RESNICK ◽  
A. JOSEPH D'ERCOLE ◽  
MARJORIE E. SVOBODA ◽  
JUDSON J. VAN WYK


1988 ◽  
Vol 251 (1) ◽  
pp. 95-103 ◽  
Author(s):  
G L Francis ◽  
F M Upton ◽  
F J Ballard ◽  
K A McNeil ◽  
J C Wallace

1. Insulin-like growth factors 1 and 2 (IGF-1 and IGF-2) together with a truncated form of IGF-1 were purified to homogeneity from bovine colostrum. 2. Two forms of IGF-1 were totally resolved from IGF-2 in the purification by h.p.l.c. involving cation-exchange and reverse-phase columns. 3. The complete amino acid sequences for all three forms of IGF were determined. The sequence of bovine IGF-1 was found to be identical with that of human IGF-1, and that of the variant lacked the N-terminal tripeptide Gly-Pro-Glu (-3N:IGF-1). Bovine IGF-2 was found to differ in three residues of the C-domain compared with human IGF-2, with serine, isoleucine and asparagine substituted for alanine, valine and serine respectively at positions 32, 35 and 36. 4. Protein synthesis in L6 rat myoblasts was stimulated and protein degradation inhibited in a co-ordinate response with all three IGFs. The relative potency in both processes was −3N:IGF-1 greater than IGF-1 greater than IGF-2. A similar order of potency was obtained for the stimulation of DNA synthesis by −3N:IGF-1 and IGF-1. The approximately 10-fold effect on biological activity of removing the N-terminal tripeptide is unexpected in view of current information on IGF-1 structure and function.



2014 ◽  
Vol 24 (1) ◽  
pp. 12 ◽  
Author(s):  
Richard J Griffeth ◽  
Vanessa Bianda ◽  
Serge Nef






Diabetes ◽  
1986 ◽  
Vol 35 (4) ◽  
pp. 416-420 ◽  
Author(s):  
M. Grant ◽  
B. Russell ◽  
C. Fitzgerald ◽  
T. J. Merimee


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