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J Biol Chem, Vol. 273, Issue 14, 8177-8182, April 3, 1998
From the Department of Physiological Chemistry, Faculty of
Pharmaceutical Sciences, Kyoto University, Sakyo-ku,
Kyoto 606, Japan
To clarify the process of post-translational
modification of L-histidine decarboxylase (HDC), we
investigated the conversion of the 74-kDa form of HDC into the 53-kDa
form in specialized organella of a rat basophilic/mast cell line
(RBL-2H3). With treatment of streptolysin-O, RBL-2H3 cells released
approximately 40% of HDC activity accompanied by over 90% of lactate
dehydrogenase activity. Only the 74-kDa form of HDC was detected in the
leaked fraction by SDS-polyacrylamide gel electrophoresis. The 74-kDa form in the homogenate of pulse-labeled cells was recovered in both the
supernatant and particulate fractions, while the 53-kDa form was
detected only in the particulate fraction containing marker proteins of
microsomes, Golgi, and lysosomal granules. Confocal microscopic
observation using double staining immunofluorescence with anti-GST
fusion HDC antiserum showed that most of the HDC coexists with
protein-disulfide isomerase, a typical marker of the luminal space of
the ER. With treatment of digitonin, RBL-2H3 cells released only 74-kDa
HDC. Trypsin digestion of digitonin-permeabilized cells resulted in the
disappearance of the 74-kDa form but not the 53-kDa form. From
these results, it is assumed that the 74-kDa form of HDC, synthesized
in the cytosol, is translocated into the lumen of the ER, where it is
converted to the 53-kDa form.
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