<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Liu G</submitter><funding>NCI NIH HHS</funding><pagination>5786-91</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC33291</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>98(10)</volume><pubmed_abstract>Proteinase inhibitor I (Inh I) and proteinase inhibitor II (Inh II) from potato tubers are effective proteinase inhibitors of chymotrypsin and trypsin. Inh I and Inh II were shown to suppress irradiation-induced transformation in mouse embryo fibroblasts suggesting that they possess anticarcinogenic characteristics. We have previously demonstrated that Inh I and Inh II could effectively block UV irradiation-induced activation of transcription activator protein 1 (AP-1) in mouse JB6 epidermal cells, which mechanistically may explain their anticarcinogenic actions. In the present study, we investigated the effects of Inh I and Inh II on the expression and composition pattern of the AP-1 complex following stimulation by UV B (UVB) irradiation in the JB6 model. We found that Inh I and Inh II specifically inhibited UVB-induced AP-1, but not NFkappaB, activity in JB6 cells. Both Inh I and Inh II up-regulated AP-1 constituent proteins, JunD and Fra-2, and suppressed c-Jun and c-Fos expression and composition in bound AP-1 in response to UVB stimulation. This regulation of the AP-1 protein compositional pattern in response to Inh I or Inh II may be critical for the inhibition of UVB-induced AP-1 activity by these agents found in potatoes.</pubmed_abstract><journal>Proceedings of the National Academy of Sciences of the United States of America</journal><pubmed_title>Proteinase inhibitors I and II from potatoes block UVB-induced AP-1 activity by regulating the AP-1 protein compositional patterns in JB6 cells.</pubmed_title><pmcid>PMC33291</pmcid><funding_grant_id>R01 CA077646</funding_grant_id><funding_grant_id>CA77646</funding_grant_id><funding_grant_id>R37 CA081064</funding_grant_id><funding_grant_id>R01 CA081064</funding_grant_id><funding_grant_id>CA74916</funding_grant_id><funding_grant_id>CA81064</funding_grant_id><pubmed_authors>Chen N</pubmed_authors><pubmed_authors>Kaji A</pubmed_authors><pubmed_authors>Dong Z</pubmed_authors><pubmed_authors>Ryan CA</pubmed_authors><pubmed_authors>Bode AM</pubmed_authors><pubmed_authors>Liu G</pubmed_authors></additional><is_claimable>false</is_claimable><name>Proteinase inhibitors I and II from potatoes block UVB-induced AP-1 activity by regulating the AP-1 protein compositional patterns in JB6 cells.</name><description>Proteinase inhibitor I (Inh I) and proteinase inhibitor II (Inh II) from potato tubers are effective proteinase inhibitors of chymotrypsin and trypsin. Inh I and Inh II were shown to suppress irradiation-induced transformation in mouse embryo fibroblasts suggesting that they possess anticarcinogenic characteristics. We have previously demonstrated that Inh I and Inh II could effectively block UV irradiation-induced activation of transcription activator protein 1 (AP-1) in mouse JB6 epidermal cells, which mechanistically may explain their anticarcinogenic actions. In the present study, we investigated the effects of Inh I and Inh II on the expression and composition pattern of the AP-1 complex following stimulation by UV B (UVB) irradiation in the JB6 model. We found that Inh I and Inh II specifically inhibited UVB-induced AP-1, but not NFkappaB, activity in JB6 cells. Both Inh I and Inh II up-regulated AP-1 constituent proteins, JunD and Fra-2, and suppressed c-Jun and c-Fos expression and composition in bound AP-1 in response to UVB stimulation. This regulation of the AP-1 protein compositional pattern in response to Inh I or Inh II may be critical for the inhibition of UVB-induced AP-1 activity by these agents found in potatoes.</description><dates><release>2001-01-01T00:00:00Z</release><publication>2001 May</publication><modification>2025-05-29T19:21:54.38Z</modification><creation>2025-05-29T19:21:54.38Z</creation></dates><accession>S-EPMC33291</accession><cross_references><pubmed>11331771</pubmed><doi>10.1073/pnas.101116298</doi></cross_references></HashMap>