Purification from human plasma of a tetrapeptide that potentiates insulin-like growth factor-I activity in chick embryo cartilage.
Human plasma has been shown to contain a low molecular weight factor that potentiates human IGF-I stimulation of glycosaminoglycan synthesis in chick embryo cartilage. The peptide was purified and characterized by Edman degradation and electrospray mass spectrometry. The primary structure determined was: Trp-Gly-His-Glu. A homologous synthetic peptide similarly promoted matrix biosynthesis in cartilage exposed to IGF-I.
Straczek
J
J
Biochemistry Laboratory, Faculty of Medicine, University of Nancy I, Vandoeuvre, France.
Maachi
F
F
Le Nguyen
D
D
Becchi
M
M
Heulin
M H
MH
Nabet
P
P
Belleville
F
F
D000595:Amino Acid Sequence; D000818:Animals; D002356:Cartilage / Q000378:metabolism*; D002642:Chick Embryo; D002851:Chromatography, High Pressure Liquid; D019075:Electrophoresis, Capillary; D005109:Extracellular Matrix / Q000378:metabolism; D006025:Glycosaminoglycans / Q000096:biosynthesis*; D006801:Humans; D007334:Insulin-Like Growth Factor I / Q000494:pharmacology*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000096:biosynthesis* / Q000097:blood* / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000494:pharmacology
D006025:Glycosaminoglycans; D009842:Oligopeptides; D011994:Recombinant Proteins; C096352:tryptophyl-glycyl-histidyl-glutamic acid; D007334:Insulin-Like Growth Factor I