Involvement of thymosin beta 4 and endoproteinase Asp-N in the biosynthesis of the tetrapeptide AcSerAspLysPro a regulator of the hematopoietic system.
It is shown that AcSDKP a new regulator of the hematopoietic system can be generated from thymosin beta 4 by a one-step enzymatic cleavage in vitro and in vivo. AcSDKP and T beta 4 were both detected in bone marrow cells (BMC). Incubation of [3H]T beta 4 with either intact or lysed BMC led to the formation of [3H]AcSDKP whereas the labelled tetrapeptide was not degraded under these conditions. Model enzymatic degradation of T beta 4 carried out with bacterial enzymes suggests that a mammalian endoproteinase Asp-N might be involved in the formation of AcSDKP through the specific cleavage of the 4Pro-5 Asp peptide bond of T beta 4.
Grillon
C
C
Institut de Chimie des Substances Naturelles, CNRS, Gif-sur-Yvette, France.
Rieger
K
K
Bakala
J
J
Schott
D
D
Morgat
J L
JL
Hannappel
E
E
Voelter
W
W
Lenfant
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001853:Bone Marrow / Q000502:physiology*; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases / Q000378:metabolism*; D006412:Hematopoietic Stem Cells / Q000187:drug effects*; D008666:Metalloendopeptidases; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism; D011817:Rabbits; D013947:Thymosin / Q000031:analogs & derivatives* / Q000302:isolation & purification / Q000378:metabolism; D000099201:Thymosin beta(4)
D010450:Endopeptidases; D008666:Metalloendopeptidases; D009842:Oligopeptides; D013947:Thymosin; D000099201:Thymosin beta(4); C058921:endoproteinase Asp-N; C058504:goralatide