Abstract:
BACKGROUND & AIMS:Amidated gastrins are acid secretagogues and growth factors. Their precursor, progastrin, is a growth factor but not a secretagogue. Cleavage of progastrin at Arg94/95 determines the expression of these two alternative patterns of biological activity. We examined the hypothesis that cleavage at Arg94/95 is regulated by phosphorylation of the adjacent Ser96 residue. METHODS:Hamster insulinoma cells were stably transfected with wild-type rat preprogastrin and phosphorylation site mutants; biosynthesis was studied by a pulse-chase protocol. RESULTS:Rates of cleavage at Arg94/95 were increased in Ser96-->Ala compared with wild-type progastrin. Mutation of Glu98 to Ala inhibited incorporation of [32P]phosphate into progastrin and increased the rate of cleavage at Arg94/95. Conversely, mutation of Ser96 to Asp reduced rates of cleavage at Arg94/95. Depletion of calcium stores decreased phosphorylation of Ser96 and increased cleavage at Arg94/95. Modulation of Ser96 phosphorylation also directly influenced the ratio of progastrin-cleavage products (progastrin/CFP; G17Gly/G34Gly) secreted into the medium. CONCLUSIONS:Phosphorylation of progastrin is dependent on calcium stores, determines prohormone cleavage rates, and thereby controls the production of the alternative active products of preprogastrin translation.
journal_name
Gastroenterologyjournal_title
Gastroenterologyauthors
Bishop L,Dimaline R,Blackmore C,Deavall D,Dockray GJ,Varro Adoi
10.1016/s0016-5085(98)70086-1subject
Has Abstractpub_date
1998-11-01 00:00:00pages
1154-62issue
5eissn
0016-5085issn
1528-0012pii
S0016508598004909journal_volume
115pub_type
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