| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| S Harada, R M Smith, J A Smith, L Jaret. Inhibition of insulin-degrading enzyme increases translocation of insulin to the nucleus in H35 rat hepatoma cells: evidence of a cytosolic pathway. Endocrinology. vol 132. issue 6. 1993-07-02. PMID:8504733. |
furthermore, when ide activity was inhibited by high cytosolic insulin concentrations, the amount of 125i-insulin in the nucleus was significantly increased. |
1993-07-02 |
2023-08-12 |
rat |
| S Harada, R M Smith, J A Smith, L Jaret. Inhibition of insulin-degrading enzyme increases translocation of insulin to the nucleus in H35 rat hepatoma cells: evidence of a cytosolic pathway. Endocrinology. vol 132. issue 6. 1993-07-02. PMID:8504733. |
our study suggests internalized insulin is probably released from endosomes into the cytosol where modulation of ide activity could have significant effects on the accumulation of insulin, or insulin-cytoplasmic protein complexes, in nuclei. |
1993-07-02 |
2023-08-12 |
rat |
| S Harada, R M Smith, J A Smith, L Jaret. Inhibition of insulin-degrading enzyme increases translocation of insulin to the nucleus in H35 rat hepatoma cells: evidence of a cytosolic pathway. Endocrinology. vol 132. issue 6. 1993-07-02. PMID:8504733. |
the ide regulatory mechanism, by controlling the translocation of insulin to the cell nucleus, could play a crucial role in insulin's regulation of gene expression and cell proliferation. |
1993-07-02 |
2023-08-12 |
rat |
| W L Kuo, A G Montag, M R Rosne. Insulin-degrading enzyme is differentially expressed and developmentally regulated in various rat tissues. Endocrinology. vol 132. issue 2. 1993-03-02. PMID:7678795. |
insulin-degrading enzyme (ide), a cytosolic metalloendoprotease, can degrade insulin, insulin-like growth factor-ii, insulin-like growth factor-i, and transforming growth factor-alpha. |
1993-03-02 |
2023-08-12 |
human |
| W L Kuo, A G Montag, M R Rosne. Insulin-degrading enzyme is differentially expressed and developmentally regulated in various rat tissues. Endocrinology. vol 132. issue 2. 1993-03-02. PMID:7678795. |
while ide has been implicated in the cellular degradation of insulin, other physiological functions of this enzyme are not known. |
1993-03-02 |
2023-08-12 |
human |
| J W Semple, Y Lang, E R Speck, T L Delovitc. Processing and presentation of insulin. III. Insulin degrading enzyme: a neutral metalloendoproteinase that is non-homologous to classical endoproteinases mediates the processing of insulin epitopes for helper T cells. International immunology. vol 4. issue 10. 1993-02-26. PMID:1283335. |
we show here that insulin degrading enzyme (ide), a neutral thiol metalloendoproteinase that is structurally non-homologous to the classical metallo, thiol, acid, or serine proteinases, is relatively specific in its proteolytic activity for insulin and digests human insulin (h(i)) into peptides that are presented by murine ta3 b cell antigen presenting cells (apcs) to hi/i-ad-reactive t cells. |
1993-02-26 |
2023-08-11 |
human |
| J W Semple, Y Lang, E R Speck, T L Delovitc. Processing and presentation of insulin. III. Insulin degrading enzyme: a neutral metalloendoproteinase that is non-homologous to classical endoproteinases mediates the processing of insulin epitopes for helper T cells. International immunology. vol 4. issue 10. 1993-02-26. PMID:1283335. |
these data show that ide is an endoproteinase that is involved in the processing of insulin and that this ide-mediated proteolysis is necessary but not sufficient for the recognition of insulin by t cells. |
1993-02-26 |
2023-08-11 |
human |
| W L Kuo, B D Gehm, M R Rosne. Regulation of insulin degradation: expression of an evolutionarily conserved insulin-degrading enzyme increases degradation via an intracellular pathway. Molecular endocrinology (Baltimore, Md.). vol 5. issue 10. 1992-03-05. PMID:1775131. |
the insulin-degrading enzyme (ide) is an evolutionarily conserved enzyme that has been implicated in cellular insulin degradation, but its site of action and importance in regulating insulin degradation have not been clearly established. |
1992-03-05 |
2023-08-11 |
human |
| W L Kuo, B D Gehm, M R Rosne. Regulation of insulin degradation: expression of an evolutionarily conserved insulin-degrading enzyme increases degradation via an intracellular pathway. Molecular endocrinology (Baltimore, Md.). vol 5. issue 10. 1992-03-05. PMID:1775131. |
we addressed this question by examining the effects of overexpressing ide on insulin degradation in cos cells, using both human ide (hide) and its drosophila homolog (dide). |
1992-03-05 |
2023-08-11 |
human |
| W L Kuo, B D Gehm, M R Rosne. Regulation of insulin degradation: expression of an evolutionarily conserved insulin-degrading enzyme increases degradation via an intracellular pathway. Molecular endocrinology (Baltimore, Md.). vol 5. issue 10. 1992-03-05. PMID:1775131. |
transient expression of dide or hide in cos monkey kidney cells led to a 5- to 7-fold increase in the rate of degradation of extracellular insulin, indicating that ide can regulate cellular insulin degradation. |
1992-03-05 |
2023-08-11 |
human |
| W L Kuo, B D Gehm, M R Rosne. Regulation of insulin degradation: expression of an evolutionarily conserved insulin-degrading enzyme increases degradation via an intracellular pathway. Molecular endocrinology (Baltimore, Md.). vol 5. issue 10. 1992-03-05. PMID:1775131. |
to further localize the site of ide action, the fate of insulin after receptor binding was examined. |
1992-03-05 |
2023-08-11 |
human |
| W L Kuo, B D Gehm, M R Rosne. Regulation of insulin degradation: expression of an evolutionarily conserved insulin-degrading enzyme increases degradation via an intracellular pathway. Molecular endocrinology (Baltimore, Md.). vol 5. issue 10. 1992-03-05. PMID:1775131. |
the results demonstrate that ide can regulate the degradation of insulin by intact cells via an intracellular pathway. |
1992-03-05 |
2023-08-11 |
human |
| W Ogawa, K Shii, K Yonezawa, S Baba, K Yokon. Affinity purification of insulin-degrading enzyme and its endogenous inhibitor from rat liver. The Journal of biological chemistry. vol 267. issue 2. 1992-02-14. PMID:1730651. |
a metallothiol protease called insulin-degrading enzyme (ide) seems to be implicated in insulin metabolism to terminate the response of cells to hormone, as well as in other biological functions, including muscle differentiation, regulation of growth factor levels, and antigen processing. |
1992-02-14 |
2023-08-11 |
rat |
| W Ogawa, K Shii, K Yonezawa, S Baba, K Yokon. Affinity purification of insulin-degrading enzyme and its endogenous inhibitor from rat liver. The Journal of biological chemistry. vol 267. issue 2. 1992-02-14. PMID:1730651. |
it inhibited both the insulin degradation by ide in a competitive manner and the cross-linking of 125i-insulin to ide. |
1992-02-14 |
2023-08-11 |
rat |
| D Müller, H Baumeister, F Buck, D Richte. Atrial natriuretic peptide (ANP) is a high-affinity substrate for rat insulin-degrading enzyme. European journal of biochemistry. vol 202. issue 2. 1992-02-11. PMID:1836994. |
in addition to the known substrates, insulin and transforming-growth-factor alpha ide binds also with high affinity (apparent kd 60 nm) to anp. |
1992-02-11 |
2023-08-11 |
rat |
| A Ebrahim, F G Hamel, R G Bennett, W C Duckwort. Identification of the metal associated with the insulin degrading enzyme. Biochemical and biophysical research communications. vol 181. issue 3. 1992-02-07. PMID:1764090. |
insulin degrading enzyme (ide) is a thiol-dependent metalloendoprotease that is responsible for initiation of cellular insulin degradation. |
1992-02-07 |
2023-08-11 |
human |
| R Espinosa, R S Lemons, R K Perlman, W L Kuo, M R Rosner, M M Le Bea. Localization of the gene encoding insulin-degrading enzyme to human chromosome 10, bands q23----q25. Cytogenetics and cell genetics. vol 57. issue 4. 1992-01-16. PMID:1743072. |
insulin-degrading enzyme (ide) is a cytosolic proteinase involved in the cellular processing of insulin. |
1992-01-16 |
2023-08-11 |
mouse |
| B D Gehm, M R Rosne. Regulation of insulin, epidermal growth factor, and transforming growth factor-alpha levels by growth factor-degrading enzymes. Endocrinology. vol 128. issue 3. 1991-04-10. PMID:1847863. |
insulin degradation is believed to be mediated by a specific metalloprotease, insulin-degrading enzyme (ide). |
1991-04-10 |
2023-08-11 |
human |
| B D Gehm, M R Rosne. Regulation of insulin, epidermal growth factor, and transforming growth factor-alpha levels by growth factor-degrading enzymes. Endocrinology. vol 128. issue 3. 1991-04-10. PMID:1847863. |
the results suggest that bacitracin-sensitive metalloproteases are involved in the degradation of tgf alpha and egf as well as insulin, and that the degradation of tgf alpha, but not egf, is mediated in part by ide. |
1991-04-10 |
2023-08-11 |
human |
| B D Gehm, M R Rosne. Regulation of insulin, epidermal growth factor, and transforming growth factor-alpha levels by growth factor-degrading enzymes. Endocrinology. vol 128. issue 3. 1991-04-10. PMID:1847863. |
the existence of separate degradative pathways for egf and tgf alpha may explain how the two factors exert differential effects in some systems, and degradation of tgf alpha by ide would provide a possible mechanism for interaction between the insulin and tgf alpha/egf signalling systems. |
1991-04-10 |
2023-08-11 |
human |