Amino-Terminal Sequences of Two Polypeptides from Human Serum with Nonsuppressible Insulin-Like and Cell-Growth-Promoting Activities: Evidence for Structural Homology with Insulin B Chain
The amino-terminal sequences of two polypeptides with nonsuppressible insulin-like and cell-growth-promoting activities (NSILA I and II), isolated from human serum, were determined. Of the first 31 residues, 22 are identical in NSILA I and II. Moreover, a striking structural similarity was found bet...
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| Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 73; no. 12; pp. 4379 - 4381 |
|---|---|
| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
United States
National Academy of Sciences of the United States of America
01.12.1976
National Acad Sciences |
| Subjects | |
| Online Access | Get full text |
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| Abstract | The amino-terminal sequences of two polypeptides with nonsuppressible insulin-like and cell-growth-promoting activities (NSILA I and II), isolated from human serum, were determined. Of the first 31 residues, 22 are identical in NSILA I and II. Moreover, a striking structural similarity was found between NSILA and insulin B chain: 47 and 57% of residues 1-30 in NSILA I are identical to those in insulin B chain from man and tuna fish, respectively. This high degree of sequence identity is presented as evidence for homology and thus for a common evolutionary origin of insulin and NSILA. Based on these results and on biological properties of NSILA described earlier, a new designation for NSILA is proposed: insulin-like growth factor (IGF). |
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| AbstractList | The amino-terminal sequences of two polypeptides with nonsuppressible insulin-like and cell-growth-promoting activities (NSILA I and II), isolated from human serum, were determined. Of the first 31 residues, 22 are identical in NSILA I and II. Moreover, a striking structural similarity was found between NSILA and insulin B chain: 47 and 57% of residues 1-30 in NSILA I are identical to those in insulin B chain from man and tuna fish, respectively. This high degree of sequence identity is presented as evidence for homology and thus for a common evolutionary origin of insulin and NSILA. Based on these results and on these results and on biological properties of NSILA described earlier, a new designation for NSILA is proposed: insulin-like growth factor (IGF). The amino-terminal sequences of two polypeptides with nonsuppressible insulin-like and cell-growth-promoting activities (NSILA I and II), isolated from human serum, were determined. Of the first 31 residues, 22 are identical in NSILA I and II. Moreover, a striking structural similarity was found between NSILA and insulin B chain: 47 and 57% of residues 1-30 in NSILA I are identical to those in insulin B chain from man and tuna fish, respectively. This high degree of sequence identity is presented as evidence for homology and thus for a common evolutionary origin of insulin and NSILA. Based on these results and on biological properties of NSILA described earlier, a new designation for NSILA is proposed: insulin-like growth factor (IGF). |
| Author | Humbel, René E. Rinderknecht, Ernst |
| Author_xml | – sequence: 1 givenname: Ernst surname: Rinderknecht fullname: Rinderknecht, Ernst – sequence: 2 givenname: René E. surname: Humbel fullname: Humbel, René E. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/1069990$$D View this record in MEDLINE/PubMed |
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| SubjectTerms | Amino Acid Sequence Amino acids Autoanalysis Biochemistry Cell growth Growth Substances - analysis Human growth Humans Insulin Insulin - analysis Insulin like effects Molecules Nonsuppressible Insulin-Like Activity - analysis Sequencing Somatomedins Tuna |
| Title | Amino-Terminal Sequences of Two Polypeptides from Human Serum with Nonsuppressible Insulin-Like and Cell-Growth-Promoting Activities: Evidence for Structural Homology with Insulin B Chain |
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