Sequence of cDNA encoding human insulin-like growth factor I precursor

  title={Sequence of cDNA encoding human insulin-like growth factor I precursor},
  author={M. Jansen and Frederik M. A. van Schaik and Alyne T. Ricker and B Bullock and Donald E. Woods and Kenneth H. Gabbay and Alexander L. Nussbaum and John S. Sussenbach and J. L. Brande},
Somatomedins (SM) or insulin-like growth factors (IGF) constitute a heterogeneous group of peptides1 with important growth-promoting effects in vitro2,3 as well as in vivo4,5. Amino acid sequences have been determined for only two of them, IGF-I and IGF-II, which are highly homologous6,7. IGF-I, which is identical with SM-C8, is composed of 70 amino acid residues and IGF-II contains 73 amino acids and may be identical with SM-A9. Other peptides with different charge properties but with similar… 
Isolation of a cDNA clone encoding rat insulin-like growth factor-II precursor
The results indicate that pro-rIGF-II is synthesized as a 156 amino acid peptide precursor containing mature rIGf-II 1–67 at its amino-terminus and an 89-residue carboxy-terminal peptide extension.
Insulin-Like Growth Factors and Their Receptors in the Pituitary and Hypothalamus
The somatomedins, or insulin-like growth factors (IGFs), constitute a family of peptide hormones which are growth hormone dependent, possess insulin-like activity and have mitogenic activity in a
Sequence of a cDNA clone encoding human preproinsulin-like growth factor II
As a first step in studying the biosynthesis of these proteins and elucidating their role(s) in normal development and in tumorigenesis, isolated and sequenced cDNAs prepared from adult human liver mRNA which encode the precursors to IGF-I and -II are reported.
Structure and expression of a chicken insulin-like growth factor I precursor.
There is strong amino acid conservation between chicken and mammalian IGF-I throughout the entire protein, suggesting that it functions as the authentic translation initiation site, an observation supported by cell-free studies of biosynthesis and cotranslational proteolytic processing.
Transcriptional Diversity in Rat Insulin-Like Growth Factor I Gene Expression
Insulin-like growth factor I (IGF-I), or Somatomedin C, is a member of a family of insulin-like peptides which also includes insulin itself, insulin-like growth factor II (IGF-II) or
The human somatomedin/insulin‐like growth factor genes: organization and development‐specific expression
The organization of the genes for IGF-i and IGF-I1 has been established and shows several surprising features, indicating that both IGFs are synthesized as precursor molecules.
Cloning of ovine insulin-like growth factor-I cDNAs: heterogeneity in the mRNA population.
We have isolated and characterized lamb liver cDNAs encoding ovine insulin-like growth factor-I (oIGF-I) precursor polypeptide to study IGF-I gene expression in ruminants. Four cDNA clones were
Insulinlike growth factor-binding proteins.
Isolation of rat testis cDNAs encoding an insulin-like growth factor I precursor.
Rat testis cDNAs encoding insulin-like growth factor I (IGF-I) precursor are characterized and it is concluded that IGF-I is synthesized as a precursor in the rat testis and that the structure of IGF- I genes, mRNAs, and precursors are highly conserved across species.
Insulin-like growth factor II precursor gene organization in relation to insulin gene family
The data, presented here, indicate that both MSA12 and human IGF-II are synthesized initially as larger precursor molecules, and both have molecular weights of 20,100 and contain C-terminal propeptides of 89 amino acid residues, which are named E-peptides.


Sequence analysis of somatomedin-C: confirmation of identity with insulin-like growth factor I.
The results of these studies document that Sm-C and IGF-I are identical peptides, thus supporting previous observations that Sm/IGF/C are qualitatively and quantitatively indistinguishable in radioligand and biological assay systems.
Nucleotide sequence of a cDNA clone encoding human preproinsulin
The cloning of a cDNA prepared from human insulin mRNA and an analysis of the nucleotide sequence of the cloned molecule including the region coding for the prepeptide and portions of the 5′- and the 3′-untranslated regions of the molecule are reported.
Partial nucleotide sequence of human calcitonin precursor mRNA identifies flanking cryptic peptides
It is demonstrated by nucleotide sequence analysis of these cloned cDNA sequences that human calcitonin resides towards the carboxy terminal of a precursor polyprotein, and is flanked at the amino and car boxy termini by cryptic peptide sequences of unknown biological significance.
Structure of a genomic clone encoding biologically active human relaxin
Synthesis of biologically active relaxin has shown that the novel gene structure described herein codes for an authentic human relaxin, believed to be the first successful synthesis of a biologically active hormone whose structure was predicted solely from the structure of a genomic clone.
A second plasma calcium-lowering peptide from the human calcitonin precursor
It is reported that the synthetic C-terminal flanking peptide (PDN-21) predicted from the nucleotide sequence is highly active biologically—it approaches the potency of calcitonin in reducing the level of plasma calcium.
Insulin-like growth factor I stimulates growth in hypophysectomized rats
It is reported that pure IGF I stimulates the growth of hypophysectomized rats in a dose-dependent manner, which strongly supports the notion that the action of growth hormone is mediated by peptides of the somatomedin family.
Isolation and characterization of cDNA clones for human apolipoprotein A-I.
Isolation of these cDNA clones will facilitate molecular analyses of apolipoproteins in normal and disease states and help clarify the role of RNA in the structure and function of apo A-I.
Cell-Free Synthesis of Rat Insulin-like Growth Factor II
Total RNA extracted from a rat liver cell line that synthesizes rat insulin-like growth factor II was translated in a reticulocyte lysate cell-free system and selectively immunoprecipitated a Mr 21,600 protein that is proposed to represent pre-pro-IGF-II.