A NEW FAMILY OF GROWTH FACTOR-LIKE PEPTIDES - TREFOIL DISULFIDE LOOP STRUCTURES AS A COMMON FEATURE IN BREAST-CANCER ASSOCIATED PEPTIDE (PS2), PANCREATIC SPASMOLYTIC POLYPEPTIDE (PSP), AND FROG-SKIN PEPTIDES (SPASMOLYSINS)
A NEW FAMILY OF GROWTH FACTOR-LIKE PEPTIDES - TREFOIL DISULFIDE LOOP STRUCTURES AS A COMMON FEATURE IN BREAST-CANCER ASSOCIATED PEPTIDE (PS2), PANCREATIC SPASMOLYTIC POLYPEPTIDE (PSP), AND FROG-SKIN PEPTIDES (SPASMOLYSINS)
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DOI:
10.1016/0014-5793(89)80690-8
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发表时间:
1989-06-19
期刊:
影响因子:
3.5
通讯作者:
THIM, L
中科院分区:
文献类型:
--
作者:
THIM, L
Four peptides present in completely different biological sources have been shown to exhibit a large degree of structural similarity. The peptides include: (i) a 60 amino acid residue breast cancer associated pS2 peptide isolated from human gastric juice and the culture media of the human breast cancer cell line MCF-7; (ii) a 106 amino acid residue pancreatic spasmolytic polypeptide (PSP) isolated from porcine pancreas and pancreatic juice; and (iii) a 49 and 50 amino acid residue peptide predicted from a cDNA isolated from the skin of the frog,Xenopus laevis. These peptides are characterized by having one (pS2 and the frog peptides) or two (PSP) domains of a highly conserved 38–39 amino acid residue consensus sequence not found in any other known peptides or proteins. The domain sequences contain 6 cysteine residues in nearly the same positions and it is suggested that these 6 residues are linked by 3 disulphide bonds to form a characteristic ‘trefoil’ disulphide loop structure common in all four peptides. From the sources of which the peptides have been isolated and from experiments showing that PSP has a growth factor stimulatory effect on MCF-7 cells, it is further suggested that these peptides may represent members of a new family of growth factors.