Formation of acetyl-Ser-Asp-Lys-Pro, a new regulator of the hematopoietic system, through enzymatic processing of thymosin beta 4.
The demonstration that AcSDKP, a new regulator of the hematopoietic system, is formed in the bone marrow by a one-step enzymatic maturation processing of thymosin beta 4 (T beta 4) is presented. 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 labeled 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 Pro4-Asp5 peptidic bond of T beta 4. In contrast, alpha-prolyl-endopeptidase was ineffective in carrying out a similar processing.
Lenfant
M
M
Institut de Chimie des Substances Naturelles, C.N.R.S., Gif-sur-Yvette,France.
Grillon
C
C
Rieger
K J
KJ
Sotty
D
D
Wdzieczak-Bakala
J
J
D000595:Amino Acid Sequence; D000818:Animals; D001853:Bone Marrow / Q000201:enzymology*; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases / Q000378:metabolism*; D005417:Flavobacterium / Q000201:enzymology; D006410:Hematopoiesis; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000302:isolation & purification / Q000378:metabolism*; D000085822:Prolyl Oligopeptidases; D011817:Rabbits; D012697:Serine Endopeptidases; D013947:Thymosin / Q000031:analogs & derivatives* / Q000378:metabolism; D000099201:Thymosin beta(4)
D010450:Endopeptidases; D009842:Oligopeptides; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases; D013947:Thymosin; D000099201:Thymosin beta(4); C058504:goralatide