Bl. Shneider et al., CLONING AND CHARACTERIZATION OF A NOVEL PEPTIDASE FROM RAT AND HUMAN ILEUM, The Journal of biological chemistry, 272(49), 1997, pp. 31006-31015
A novel 100-kDa ileal brush border membrane protein (I100) has been pu
rified by anionic glycocholate affinity chromatography, Polyclonal ant
ibodies raised against this protein were utilized to clone and charact
erize I100 in rats, A partial length human I100 cDNA was identified by
hybridization screening, In the rat, the I100 protein is a 746-amino
acid glycosylated (calculated core molecular mass of 80 kDa) type II i
ntegral membrane protein found on the apical surface of ileal villus e
nterocytes, Its a,6-kilobase mRNA is expressed in distal small intesti
ne in rats and in humans, The I100 cDNA is homologous to but distinct
from human prostate-specific membrane antigen and rat brain N-acetylas
partylglutamate peptidase, It is expressed on both the basolateral and
apical surfaces of stably transfected Madin Darby canine kidney cells
, Analysis of these stably transfected Madin Darby canine kidney cells
and I100 immunoprecipitates of rat ileal brush border membrane vesicl
es reveals that it has dipeptidyl peptidase TV activity. Future invesi
tgations will need to determine the exact substrate specificity of thi
s novel peptidase.