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SK-BR-3 cells with γ1-adaptin depletion were used for functional assays, while localization was assessed by immunohistochemistry and double immunohistofluorescence. Results show γ1-adaptin depletion suppresses growth, migration, and invasion, and high γ1-adaptin intensity correlates with worse relapse-free survival and acts as an independent prognostic factor.",{"@graph":14,"@context":72},[15,34,55],{"@type":16,"itemListElement":17},"BreadcrumbList",[18,23,27,31],{"item":19,"name":20,"@type":21,"position":22},"https://docshare.wps.com","Home","ListItem",1,{"item":24,"name":25,"@type":21,"position":26},"https://docshare.wps.com/document/","Document",2,{"item":28,"name":29,"@type":21,"position":30},"https://docshare.wps.com/document/research-report/","Research & 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\n[https://doi.org/10.1007/s12282-023-01539-1](https://doi.org/10.1007/s12282-023-01539-1)  \nEndosomal protein expression of γ1‑adaptin is associated with tumor growth activity and relapse‑free survival in breast cancer  \nNobuhiro Hoshi1 · Takefumi Uemura2 · Kazunoshin Tachibana1 · Sadahiko Abe1 · Yuko Murakami‑Nishimagi1 · Maiko Okano1 · Masaru Noda1 · Katsuharu Saito3 · Koji Kono3 · Tohru Ohtake1 · Satoshi Waguri2  \nReceived: 20 October 2022 / Accepted: 20 December 2023 / Published online: 24 January 2024 © The Author(s) 2024  \nAbstract  \nBackground γ1-Adaptin is a subunit of adaptor protein complex-1 (AP-1), which regulates intracellular transport between the trans-Golgi network (TGN) and endosomes. Since expression levels of AP-1 subunits have been reported to be associated with cell proliferation and cancer malignancy, we investigated the relationships between the immunohistochemical expression of γ1-adaptin and both clinicopathological factors and relapse-free survival (RFS) in breast cancer tissue.  \nMaterials and methods SK-BR-3 cell line depleted of γ1-adaptin was used for cell proliferation, migration, and invasion assay. Intracellular localization of γ1-adaptin was examined with immunohistochemistry (IHC) using an antibody against γ1-adaptin, and with double immunohistofluorescence (IHF) microscopy using markers for the TGN and endosome.γ1-Adaptin intensities in IHC samples from 199 primary breast cancer patients were quantified and assessed in relation to clinicopathological factors and RFS.  \nResults Cell growth, migration, and invasion of SK-BR-3 cells were significantly suppressed by the depletion of γ1-adaptin. Although the staining patterns in the cancer tissues varied among cases by IHC, double IHF demonstrated that γ1-adaptin was mainly localized in EEA1-positive endosomes, but not in the TGN. γ1-Adaptin intensity was significantly higher in the tumor regions than in non-tumor regions. It was also higher in patients with Ki-67 (high), ER (–), PgR (–), and HER2 (+) . Among subtypes of breast cancer, γ1-adaptin intensity was higher in HER2 than in luminal A or luminal B. The results of the survival analysis indicated that high γ1-adaptin intensity was significantly associated with worse RFS, and this association was also observed in group with ER (+), PgR (+), HER2 (–), Ki-67 (high), or luminal B. In addition, the Cox proportional hazards model showed that high γ1-adaptin intensity was an independent prognostic factor.  \nConclusion These results suggest that the endosomal expression of γ1-adaptin is positively correlated with breast cancer malignancy and could be a novel prognostic marker.  \nKeywords γ1-Adaptin · Clathrin adaptor · Adaptor protein complex-1 · AP-1 · Endosome  \nIntroduction  \nBreast cancer is the leading cause of cancer death among females worldwide, according to GLOBOCAN 2020 estimates [1] . It is a complex disease, and currently classified  \n* Satoshi Waguri [waguri@fmu.ac.jp](waguri@fmu.ac.jp)  \n1 Department of Breast Surgery, Fukushima Medical University School of Medicine, Fukushima, Japan  \n2 Department of Anatomy and Histology, Fukushima Medical University School of Medicine, Fukushima, Japan  \n3 Department of Gastrointestinal Tract Surgery, Fukushima Medical University School of Medicine, Fukushima, Japan  \ninto four subtypes: luminal A, luminal B, human epidermal growth factor receptor type 2 (HER2)-positive, and triple-negative breast cancer (TNBC). They reflect intrinsic biological subtypes [2] determined by the immunohistochemistry (IHC) of estrogen receptor (ER), progesterone receptor (PgR), HER2, and a cell proliferation marker Ki-67 [3, 4] . Importantly, these subtypes are strongly associated with treatment strategies and prognosis; e.g., TNBC shows poorer prognosis than the luminal types of breast cancer [5, 6]. However, late recurrence was higher in patients with ER-positive primary tumors [7] and pathological complete response following preopera","cbCaimzvlT9seBG3","https://ap.wps.com/l/cbCaimzvlT9seBG3","pdf",1844381,12,"English","# Abstract\n## Background\n## Materials and methods\n## Results\n## Conclusion\n# Keywords\n# Introduction","[{\"question\":\"What role does γ1-adaptin play in relation to AP-1 and endosomal transport?\",\"answer\":\"γ1-adaptin is a γ1 subunit of AP-1 (adaptor protein complex-1), which regulates intracellular transport between the trans-Golgi network and endosomes.\"},{\"question\":\"How were the effects of γ1-adaptin depletion tested in this study?\",\"answer\":\"SK-BR-3 cells depleted of γ1-adaptin were used for proliferation, migration, and invasion assays, assessing functional impact on cancer cell behavior.\"},{\"question\":\"What clinical outcome was associated with higher γ1-adaptin intensity?\",\"answer\":\"High γ1-adaptin intensity was significantly associated with worse relapse-free survival, and Cox proportional hazards modeling showed it as an independent prognostic factor.\"}]","Endosomal protein expression of γ1-adaptin is associated with tumor growth activity and relapse-free survival in breast cancer | PDF",1790047097]