Identification of the proteins exposed on the cytoplasmic surface of the pancreatic zymogen granule.
Lactoperoxidase-catalyzed 125I-iodination was used to label pancreatic zymogen granules. Membrane proteins facing the cytoplasmic surface were specifically labeled. Two low molecular weight proteins of 17 000 and 15 000 were intensely labeled at 0 degree C. Another small 13 kDa protein was strongly iodinated at 25 degrees C along with some others, including the 29 kDa subunit of the ATP diphosphohydrolase. The major glycoprotein of the granule membrane was not iodinated but the presence of an iodinated 80 kDa protein suggests that proteolytic fragments of the 92 kDa glycoprotein were accessible to iodination on the intact granule. These proteins localized on the cytoplasmic surface of the granule are believed to play a major role in the exocytotic phenomenon of the exocrine pancreas.
D000818:Animals; D003594:Cytoplasmic Granules / Q000032:analysis*; D004792:Enzyme Precursors / Q000032:analysis*; D005089:Exocytosis; D006023:Glycoproteins / Q000032:analysis; D008565:Membrane Proteins / Q000032:analysis*; D008970:Molecular Weight; D010179:Pancreas / Q000648:ultrastructure*; D013552:Swine
D004792:Enzyme Precursors; D006023:Glycoproteins; D008565:Membrane Proteins