ArticleThe Biochemical journal2000
Control of pancreatic bile-salt-dependent-lipase secretion by the glucose-regulated protein of 94 kDa (Grp94).
Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- The HSP GRP94 interacts with macrophage intracellular complement C3 and impacts M2 profile during ER stress.Cell death & disease · 2021Article
- Pharmacological Targeting of the ER-Resident Chaperones GRP94 or Cyclophilin B Induces Secretion of IL-22 Binding Protein Isoform-1 (IL-22BPi1).International journal of molecular sciences · 2019Article
- The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease.International journal of molecular sciences · 2018Review
- Review
- Mapping the Interactome of a Major Mammalian Endoplasmic Reticulum Heat Shock Protein 90.PloS one · 2017Article
- Comparative venomics of Psyttalia lounsburyi and P. concolor, two olive fruit fly parasitoids: a hypothetical role for a GH1 β-glucosidase.Scientific reports · 2016Article
- GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum.Biochimica et biophysica acta · 2012Review
- The endoplasmic reticulum protein folding factory and its chaperones: new targets for drug discovery?British journal of pharmacology · 2011Review
- Hormone-sensitive lipase expression and IHC localization in the rat ovary, oviduct, and uterus.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2009Article
- Heat shock protein 90 modulates the unfolded protein response by stabilizing IRE1alpha.Molecular and cellular biology · 2002Article
- Monoclonal antibody 16D10 to the C-terminal domain of the feto-acinar pancreatic protein binds to membrane of human pancreatic tumoral SOJ-6 cells and inhibits the growth of tumor xenografts.Neoplasia (New York, N.Y.)Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bile-salt-dependent lipase (BSDL; EC 3.1.1.13) is an enzyme expressed by the pancreatic acinar cell and secreted as a component of the pancreatic juice. During its route towards secretion, BSDL is associated with intracellular membranes by means of a multiprotein folding complex, which includes the glucose-regulated protein of 94 kDa (Grp94). We have postulated that the association of BSDL with membranes is required for the complete O-glycosylation of the protein, which diverts BSDL from a degradation route and consequently allows its secretion. To further characterize the role of Grp94 in BSDL secretion, we have studied the effect of a ribozyme specifically targeted to Grp94 mRNA. This ribozyme has been transfected into AR4-2J cells, and we have shown that a decrease in Grp94 expression leads to a concomitant decrease in BSDL secretion and expression. Geldanamycin (GA), which alters Grp94 functions, also affects the release of BSDL into the culture medium of AR4-2J cells. BSDL expressed in GA-treated AR4-2J cells is unstable. Furthermore, under conditions that decrease the level of BSDL secretion, no intracellular accumulation of the enzyme was observed, suggesting that BSDL that cannot associate with (or be structured by) Grp94 could be rapidly degraded. We have further shown that this degradation probably occurs via the ubiquitin-dependent pathway. Altogether, these results indicate that Grp94 has a pivotal role in BSDL folding and in the sorting of this pancreatic enzyme.
Indexed as
Identifiers
11104697PMC1221528W2123702209What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.