Faculty Research 1990 - 1999

Hyperproinsulinaemia in obese fat/fat mice associated with a carboxypeptidase E mutation which reduces enzyme activity.

Document Type

Article

Publication Date

1995

Keywords

Animal, Base-Sequence, Carboxypeptidases: ge, me, Cattle, Chromosome-Mapping, Comparative-Study, Conserved-Sequence, Enzyme-Activation, Female, Islets-of-Langerhans: en, ul, Male, Mice, Mice-Inbred-C57BL, Mice-Inbred-NOD, Mice-Obese, Mice-SCID, Molecular-Sequence-Data, Mutagenesis-Site-Directed, Mutation, Pituitary-Gland: en, Proinsulin: bl, me, Rats, Sequence-Alignment, SUPPORT-NON-U-S-GOVT, SUPPORT-U-S-GOVT-P-H-S, Transfection

First Page

135

Last Page

142

JAX Source

Nat Genet 1995 Jun;10(2):135-42

Grant

RO1DK46977/DK/NIDDK, RO1DA04494/DA/NIDA, K02DA00194/DA/NIDA

Abstract

Mice homozygous for the fat mutation develop obesity and hyperglycaemia that can be suppressed by treatment with exogenous insulin. The fat mutation maps to mouse chromosome 8, very close to the gene for carboxypeptidase E (Cpe), which encodes an enzyme (CPE) that processes prohormone intermediates such as proinsulin. We now demonstrate a defect in proinsulin processing associated with the virtual absence of CPE activity in extracts of fat/fat pancreatic islets and pituitaries. A single Ser202Pro mutation distinguishes the mutant Cpe allele, and abolishes enzymatic activity in vitro. Thus, the fat mutation represents the first demonstration of an obesity-diabetes syndrome elicited by a genetic defect in a prohormone processing pathway.

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