Breast cancer is a malignant disease that seriously threatens women's health.Studying the mechanism of cancer occurrence and development is an urgent problem to be solved.In this paper,the eigen-microstate method ...Breast cancer is a malignant disease that seriously threatens women's health.Studying the mechanism of cancer occurrence and development is an urgent problem to be solved.In this paper,the eigen-microstate method was used to study conversion of normal breast cells into breast cancer cells and the reason.The main conclusions are as follows:the microstates of normal breast cell and breast cancer cell are different.There is a state conversion when a normal breast cell transforms into a breast cancer cell.The main reason for this state conversion is the combined effect of tumor suppressor genes and oncogenes.By analyzing the function of key genes,it was found that these genes do play an important role in the development of breast cancer.The findings contribute to understanding the mechanism by which breast cancer occurs and progresses,and key genes can serve as potential biomarkers or target genes for breast cancer treatment.展开更多
Various peptide toxins in animal venom inhibit voltage-gated sodium ion channel Nav1.7, including Nav-targeting spider toxin(NaSpTx) Family I. Toxins in NaSpTx Family I share a similar structure, i.e., Nterminal, loop...Various peptide toxins in animal venom inhibit voltage-gated sodium ion channel Nav1.7, including Nav-targeting spider toxin(NaSpTx) Family I. Toxins in NaSpTx Family I share a similar structure, i.e., Nterminal, loops 1–4, and C-terminal. Here, we used Mu-theraphotoxin-Ca2a(Ca2a), a peptide isolated from Cyriopagopus albostriatus, as a template to investigate the general properties of toxins in NaSpTx Family I. The toxins interacted with the cell membrane prior to binding to Nav1.7 via similar hydrophobic residues. Residues in loop 1, loop 4,and the C-terminal primarily interacted with the S3–S4 linker of domain II, especially basic amino acids binding to E818. We also identified the critical role of loop 2 in Ca2a regarding its affinity to Nav1.7.Our results provide further evidence that NaSpTx Family I toxins share similar structures and mechanisms of binding to Nav1.7.展开更多
基金the National Natural Science Foundation of China(Grant No.11735006)。
文摘Breast cancer is a malignant disease that seriously threatens women's health.Studying the mechanism of cancer occurrence and development is an urgent problem to be solved.In this paper,the eigen-microstate method was used to study conversion of normal breast cells into breast cancer cells and the reason.The main conclusions are as follows:the microstates of normal breast cell and breast cancer cell are different.There is a state conversion when a normal breast cell transforms into a breast cancer cell.The main reason for this state conversion is the combined effect of tumor suppressor genes and oncogenes.By analyzing the function of key genes,it was found that these genes do play an important role in the development of breast cancer.The findings contribute to understanding the mechanism by which breast cancer occurs and progresses,and key genes can serve as potential biomarkers or target genes for breast cancer treatment.
基金supported by the National Natural Science Foundation of China (31971190)Science Fund for Distinguished Young Scholars of Hunan Province (2021JJ10035)Education Department of Hunan Province (19A321)。
文摘Various peptide toxins in animal venom inhibit voltage-gated sodium ion channel Nav1.7, including Nav-targeting spider toxin(NaSpTx) Family I. Toxins in NaSpTx Family I share a similar structure, i.e., Nterminal, loops 1–4, and C-terminal. Here, we used Mu-theraphotoxin-Ca2a(Ca2a), a peptide isolated from Cyriopagopus albostriatus, as a template to investigate the general properties of toxins in NaSpTx Family I. The toxins interacted with the cell membrane prior to binding to Nav1.7 via similar hydrophobic residues. Residues in loop 1, loop 4,and the C-terminal primarily interacted with the S3–S4 linker of domain II, especially basic amino acids binding to E818. We also identified the critical role of loop 2 in Ca2a regarding its affinity to Nav1.7.Our results provide further evidence that NaSpTx Family I toxins share similar structures and mechanisms of binding to Nav1.7.