PMID- 10099930
OWN - NLM
STAT- MEDLINE
DCOM- 19990707
LR  - 20061115
IS  - 0171-9335 (Print)
IS  - 0171-9335 (Linking)
VI  - 78
IP  - 2
DP  - 1999 Feb
TI  - The secretory lectin ZG16p mediates sorting of enzyme proteins to the zymogen
      granule membrane in pancreatic acinar cells.
PG  - 79-90
AB  - The recently established in vitro assay of condensation-sorting of pancreatic
      enzymes to the zymogen granule membrane (ZGM) (Dartsch, H., R. Kleene, H. F.
      Kern: In vitro condensation-sorting of enzyme proteins isolated from rat
      pancreatic acinar cells. Eur. J. Cell Biol. 75, 211-222 (1998)) was used to study
      the involvement of a novel secretory lectin, ZG16p, in the binding of aggregated 
      proteins to ZGM. In isolated zymogen granules the lectin is predominantly
      associated with the membrane and can be removed to a large extent by bicarbonate 
      treatment at pH 11.5. In the in vitro assay in which secretory proteins aggregate
      at pH 5.9 but only those bound to ZGM are sedimented into the pellet, ZG16p is
      significantly enriched in this pellet fraction, shown both by biochemical and
      fine structural analysis. Pretreatment of ZGM with anti-ZG16p antibody before
      their addition to the assay inhibits binding to the membrane by about 50%.
      Similarly, removal of ZG16p or prevention of its interaction with
      glycosaminoglycans (GAGs) in the submembranous matrix of ZGM by sodium
      bicarbonate treatment or chondroitinase digestion of ZGM also inhibits the
      binding efficiency of secretory proteins to ZGM to about the same extent. We
      conclude that ZG16p may act as a linker molecule between the submembranous matrix
      on the luminal side of ZGM and aggregated secretory proteins during granule
      formation in the TGN.
FAU - Kleene, R
AU  - Kleene R
AD  - Department of Cell Biology and Cell Pathology, Philipps University Marburg,
      Germany. kleene@mailer.uni-marburg.de
FAU - Dartsch, H
AU  - Dartsch H
FAU - Kern, H F
AU  - Kern HF
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Eur J Cell Biol
JT  - European journal of cell biology
JID - 7906240
RN  - 0 (Disaccharides)
RN  - 0 (Enzyme Precursors)
RN  - 0 (Lectins)
RN  - 0 (Monosaccharides)
RN  - 0 (ZG16 protein, rat)
SB  - IM
MH  - Animals
MH  - Binding, Competitive/physiology
MH  - Cells, Cultured
MH  - Cytoplasmic Granules/*metabolism
MH  - Disaccharides/pharmacology
MH  - Electrophoresis, Gel, Two-Dimensional
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Enzyme Precursors/*metabolism
MH  - Intracellular Membranes/metabolism
MH  - Lectins/*metabolism/physiology
MH  - Male
MH  - Molecular Weight
MH  - Monosaccharides/pharmacology
MH  - Pancreas/drug effects/metabolism
MH  - Rats
MH  - Rats, Wistar
MH  - Subcellular Fractions/metabolism
EDAT- 1999/04/01 00:00
MHDA- 1999/04/01 00:01
CRDT- 1999/04/01 00:00
PHST- 1999/04/01 00:00 [pubmed]
PHST- 1999/04/01 00:01 [medline]
PHST- 1999/04/01 00:00 [entrez]
AID - S0171-9335(99)80009-0 [pii]
AID - 10.1016/S0171-9335(99)80009-0 [doi]
PST - ppublish
SO  - Eur J Cell Biol. 1999 Feb;78(2):79-90. doi: 10.1016/S0171-9335(99)80009-0.