Characterisation of a novel murine intestinal serine protease, DISP

C J Shaw-Smith; A J Coffey; M Leversha; T C Freeman; D R Bentley; J R Walters

doi:10.1016/s0167-4781(99)00226-2

Characterisation of a novel murine intestinal serine protease, DISP

Biochim Biophys Acta. 2000 Jan 31;1490(1-2):131-6. doi: 10.1016/s0167-4781(99)00226-2.

Authors

C J Shaw-Smith¹, A J Coffey, M Leversha, T C Freeman, D R Bentley, J R Walters

Affiliation

¹ Division of Medicine, Imperial College School of Medicine, Hammersmith Hospital, London, UK.

PMID: 10786627
DOI: 10.1016/s0167-4781(99)00226-2

Abstract

A putative novel murine serine protease, DISP, was identified by cDNA indexing and shown to be expressed primarily in distal gut. FISH analysis showed it to be localised to mouse chromosome 17A3. A possible human homologue for DISP has been identified. DISP is a novel member of clan SA/family S1 of the serine proteases, at present of unknown function.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Animals
Base Sequence
DNA, Complementary / analysis
Electrophoresis, Agar Gel
Epithelial Cells / metabolism
Gene Expression
Ileum / metabolism
Intestine, Small / enzymology*
Mice
Mice, Inbred C57BL
Molecular Sequence Data
RNA, Messenger / analysis
Reverse Transcriptase Polymerase Chain Reaction
Serine Endopeptidases / analysis
Serine Endopeptidases / chemistry
Serine Endopeptidases / genetics*

Substances

DNA, Complementary
RNA, Messenger
Serine Endopeptidases
distal intestinal serine protease

Associated data

GENBANK/AJ243866