ArticleProceedings of the National Academy of Sciences of the United States of America1991
A single gene encodes membrane-bound and free forms of GP-2, the major glycoprotein in pancreatic secretory (zymogen) granule membranes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 93 citations in OpenAlex.
- CDKAL1-related single nucleotide polymorphisms are associated with insulin resistance in a cross-sectional cohort of Greek children.PloS one · 2014Trial
- Glycoprotein 2 as a gut gate keeper for mucosal equilibrium between inflammation and immunity.Seminars in immunopathology · 2024Review
- Rab7 localized on zymogen granules is involved in maturation but not in autophagy or regulated exocytosis in pancreatic acinar cells.Scientific reports · 2023Article
- Epithelial glycosylation in gut homeostasis and inflammation.Nature immunology · 2016Review
- Intestinal M cells.Journal of biochemistry · 2016Review
- Genetic and phenotypic heterogeneity in tropical calcific pancreatitis.World journal of gastroenterology · 2014Review
- Ileal inflammation may trigger the development of GP2-specific pancreatic autoantibodies in patients with Crohn's disease.Clinical & developmental immunology · 2012Article
- The pancreatic zymogen granule membrane protein, GP2, binds Escherichia coli Type 1 fimbriae.BMC gastroenterology · 2009Article
- Article
- Protection from pancreatitis by the zymogen granule membrane protein integral membrane-associated protein-1.The Journal of biological chemistry · 2002Article
- Interaction of syncollin with GP-2, the major membrane protein of pancreatic zymogen granules, and association with lipid microdomains.The Biochemical journal · 2002Article
- Cholesterol-dependent interaction of syncollin with the membrane of the pancreatic zymogen granule.The Biochemical journal · 2001Article
- Chromogranin B (secretogranin I), a neuroendocrine-regulated secretory protein, is sorted to exocrine secretory granules in transgenic mice.The EMBO journal · 1998Article
- Identification of membrane dipeptidase as a major glycosyl-phosphatidylinositol-anchored protein of the pancreatic zymogen granule membrane, and evidence for its release by phospholipase A.The Biochemical journal · 1997Article
- Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells.The Journal of cell biology · 1995Article
- Molecular cloning of chick beta-tectorin, an extracellular matrix molecule of the inner ear.The Journal of cell biology · 1995Article
- Exocrine granule specific packaging signals are present in the polypeptide moiety of the pancreatic granule membrane protein GP2 and in amylase: implications for protein targeting to secretory granules.The EMBO journal · 1994Article
- GP2, the homologue to the renal cast protein uromodulin, is a major component of intraductal plugs in chronic pancreatitis.The Journal of clinical investigation · 1993Article
- Immunolocalization of a glycosylphosphatidylinositol-specific phospholipase D in mast cells found in normal tissue and neurofibromatosis lesions.The American journal of pathology · 1992Article
- GP-2/THP gene family encodes self-binding glycosylphosphatidylinositol-anchored proteins in apical secretory compartments of pancreas and kidney.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
GP-2, a 75-kDa glycoprotein, was isolated from dog pancreatic zymogen granule membranes (ZGMs). In a carbohydrate-shift strategy, N-terminal and internal peptide sequences were obtained on glycosylated and deglycosylated forms of GP-2, respectively, by gas-phase sequencing. Sets of mixed oligonucleotides and the polymerase chain reaction were used to obtain a double-stranded cDNA probe, which was used to isolate overlapping cDNA clones from a dog pancreatic cDNA library. The sequence of these clones revealed an open reading frame that encodes a protein of 509 amino acids, eight N-linked oligosaccharide attachment sites, and an N-terminal signal sequence absent from the mature form of GP-2 associated with ZGMs. The C terminus shows a 20-residue hydrophobic transmembrane domain preceded by a decapeptide containing potential phosphatidylinositol-glycan attachment sites. GP-2 completely released from ZGMs by exogenous phospholipase C showed similar immunochemical properties and electrophoretic mobilities compared to the form associated with ZGMs. A similar form of GP-2 was released from zymogen granules permeabilized with saponin and incubated in the absence of added phospholipase C. Kinetic analysis of GP-2 release at 0 degrees C and 37 degrees C suggested the presence of a granule enzyme responsible for endogenous release of GP-2 to granule contents and into the apical medium. The data indicate that GP-2 is a phosphatidylinositol-glycan-linked membrane protein released from the membrane of mature zymogen granules by an enzymatic mechanism. The cDNA structure presented here thus encodes both membrane-bound and free forms of GP-2.
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