A PHP Error was encountered

Severity: Warning

Message: file_get_contents(https://...@gmail.com&api_key=61f08fa0b96a73de8c900d749fcb997acc09): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests

Filename: helpers/my_audit_helper.php

Line Number: 143

Backtrace:

File: /var/www/html/application/helpers/my_audit_helper.php
Line: 143
Function: file_get_contents

File: /var/www/html/application/helpers/my_audit_helper.php
Line: 209
Function: simplexml_load_file_from_url

File: /var/www/html/application/helpers/my_audit_helper.php
Line: 994
Function: getPubMedXML

File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3134
Function: GetPubMedArticleOutput_2016

File: /var/www/html/application/controllers/Detail.php
Line: 574
Function: pubMedSearch_Global

File: /var/www/html/application/controllers/Detail.php
Line: 488
Function: pubMedGetRelatedKeyword

File: /var/www/html/index.php
Line: 316
Function: require_once

USP35 promotes breast cancer progression by regulating PFK-1 ubiquitination to mediate glycolysis. | LitMetric

USP35 promotes breast cancer progression by regulating PFK-1 ubiquitination to mediate glycolysis.

Am J Physiol Cell Physiol

Department of Breast Surgery, Fujian Medical University Union Hospital, Fuzhou, Fujian, 350000, P.R. China.

Published: December 2024

Ubiquitin‑specific protease 35 (USP35) was found to be involved in various tumor progression, but its role in breast cancer remains largely unknown. USP35 mRNA and protein expression in breast cancer tissues and cells were evaluated by qPCR and Western bolt (WB), respectively. Subsequently, flow cytometry and EDU labeling were used to evaluate breast cancer cell apoptosis and proliferation. Cellular glycolytic function was analyzed using the Seahorse assay and various kits. Furthermore, Co-immunoprecipitation (Co-IP) and immunoprecipitation (IP) assays were utilized to validate the deubiquitylation mechanism of USP35. Finally, a subcutaneous human xenograft tumor model was established in nude mice to verify the effect of USP35 in vivo. By examining the clinical samples and cell lines, we found that USP35 expression was significantly upregulated in breast cancer. Further functional studies showed that knockdown USP35 expression inhibited cell proliferation and promoted apoptosis. In addition, knockdown of USP35 decreased PFK-1 expression and was associated with lower extracellular acidification rate (ECAR) and oxygen consumption rate (OCR) compared with sh-Control. Co-IP assays identified phosphofructokinase1 (PFK-1) as a direct deubiquitiation target of USP35. Importantly, we demonstrated that PFK-1 is an essential mediator for USP35-induced cell proliferation and glycolysis in vitro and in vivo. This study identified that USP35 regulates proliferation and glycolysis of breast cancer cells by mediating the ubiquitination level of PFK-1. The USP35/PFK-1 axis offers novel insight for the treatment of breast cancer.

Download full-text PDF

Source
http://dx.doi.org/10.1152/ajpcell.00733.2024DOI Listing

Publication Analysis

Top Keywords

breast cancer
28
usp35
10
usp35 expression
8
knockdown usp35
8
cell proliferation
8
proliferation glycolysis
8
breast
7
cancer
7
pfk-1
5
usp35 promotes
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!