Tyrosine sulphation is not required for microvillar expression of intestinal aminopeptidase N
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Tyrosine sulphation is not required for microvillar expression of intestinal aminopeptidase N. / Danielsen, E M.
In: Biochemical Journal, Vol. 254, No. 1, 1988, p. 219-22.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Tyrosine sulphation is not required for microvillar expression of intestinal aminopeptidase N
AU - Danielsen, E M
N1 - Keywords: Aminopeptidases; Animals; Antigens, CD13; Electrophoresis, Polyacrylamide Gel; Enzyme Induction; Intestinal Mucosa; Microvilli; Nitrophenols; Organ Culture Techniques; Protein Biosynthesis; Sulfur Radioisotopes; Swine; Tyrosine
PY - 1988
Y1 - 1988
N2 - The effect of 2,6-dichloro-4-nitrophenol (DCNP), an inhibitor of phenol sulphotransferases (EC 2.8.2.-), on the biosynthesis of aminopeptidase N (EC 3.4.11.2) was studied in organ-cultured pig intestinal mucosal explants. At 50 microM DCNP did not affect protein synthesis but it decreased incorporation of [35S]sulphate into aminopeptidase N and other major microvillar hydrolases by 70-85% compared with controls, indicating an inhibition of their post-translational tyrosine sulphation. In labelling experiments with [35S]methionine from 0.5 to 5 h, DCNP was tested for its possible influence on synthesis, processing and microvillar expression of aminopeptidase N, but no effect on any of these parameters could be detected. It can therefore be concluded that tyrosine sulphation is not required (for instance as a sorting signal) for the targeting of newly synthesized enzymes to the microvillar membrane.
AB - The effect of 2,6-dichloro-4-nitrophenol (DCNP), an inhibitor of phenol sulphotransferases (EC 2.8.2.-), on the biosynthesis of aminopeptidase N (EC 3.4.11.2) was studied in organ-cultured pig intestinal mucosal explants. At 50 microM DCNP did not affect protein synthesis but it decreased incorporation of [35S]sulphate into aminopeptidase N and other major microvillar hydrolases by 70-85% compared with controls, indicating an inhibition of their post-translational tyrosine sulphation. In labelling experiments with [35S]methionine from 0.5 to 5 h, DCNP was tested for its possible influence on synthesis, processing and microvillar expression of aminopeptidase N, but no effect on any of these parameters could be detected. It can therefore be concluded that tyrosine sulphation is not required (for instance as a sorting signal) for the targeting of newly synthesized enzymes to the microvillar membrane.
M3 - Journal article
C2 - 2902847
VL - 254
SP - 219
EP - 222
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - 1
ER -
ID: 9881094