A novel pancreas-specific serpin (ZG-46p) localizes to the soluble and membrane fraction of the Golgi complex and the zymogen granules of acinar cells.

@article{Chen1997ANP,
  title={A novel pancreas-specific serpin (ZG-46p) localizes to the soluble and membrane fraction of the Golgi complex and the zymogen granules of acinar cells.},
  author={Cindy Y Chen and U Cronshagen and Horst F. Kern},
  journal={European journal of cell biology},
  year={1997},
  volume={73 3},
  pages={205-14}
}
By immunoscreening a cDNA expression library of rat pancreas using a polyspecific antiserum raised against purified pancreatic zymogen granule membranes, we have identified a cDNA clone coding for a novel protein, named ZG-46p. The cDNA contains an ORF of 1215 bp coding for a protein of 405 amino acids with a calculated molecular mass of 46 kDa. Sequence analysis revealed high homologies to known serine protease inhibitors (serpins), e.g. human anti-thrombin III (47.2%) or human and rat anti… CONTINUE READING

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The cellular localization , the distribution in the soluble and membrane fraction of Golgi complex and zymogen granules , and the finding that pancreatic serpin is associated with aggregated secretory proteins suggest a role in the sorting of pancreatic enzymes during granule formation .
The cellular localization , the distribution in the soluble and membrane fraction of Golgi complex and zymogen granules , and the finding that pancreatic serpin is associated with aggregated secretory proteins suggest a role in the sorting of pancreatic enzymes during granule formation .
Sequence analysis revealed high homologies to known serine protease inhibitors ( serpins ) , e.g. human anti - thrombin III ( 47.2% ) or human and rat anti - trypsin ( 44% ) .
Serine Proteinase InhibitorsIs biochemical function of gene productSerpins
Sequence analysis revealed high homologies to known serine protease inhibitors ( serpins ) , e.g. human anti - thrombin III ( 47.2% ) or human and rat anti - trypsin ( 44% ) .
Sequence analysis revealed high homologies to known serine protease inhibitors ( serpins ) , e.g. human anti - thrombin III ( 47.2% ) or human and rat anti - trypsin ( 44% ) .
Sequence analysis revealed high homologies to known serine protease inhibitors ( serpins ) , e.g. human anti - thrombin III ( 47.2% ) or human and rat anti - trypsin ( 44% ) .
Sequence analysis revealed high homologies to known serine protease inhibitors ( serpins ) , e.g. human anti - thrombin III ( 47.2% ) or human and rat anti - trypsin ( 44% ) .
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