Myosin heavy chain 9(MYH9),a non-muscle myosin heavy chain protein,has been identified as a significant factor in gastrointestinal(GI)oncology,with its overexpression in various GI malignancies such as esophageal,gast...Myosin heavy chain 9(MYH9),a non-muscle myosin heavy chain protein,has been identified as a significant factor in gastrointestinal(GI)oncology,with its overexpression in various GI malignancies such as esophageal,gastric,and co-lorectal cancers being associated with poor prognosis and playing a role in tumor invasion and metastasis.This comprehensive review synthesizes the current body of knowledge regarding MYH9’s role in GI tumors,focusing on its molecular mechanisms,including its interaction with key signaling pathways like the phosphatidylinositol 3-kinase/protein kinase B/mechanistic target of rapamycin axis,which suggests a role in cancer cell survival,proliferation,and epithelial-mesenchymal transition.The review also explores MYH9’s potential as a therapeutic target,with preclinical models demonstrating promising results in inhibiting tumor growth and enhancing chemosensitivity.The evidence suggests that MYH9 is a multifaceted protein with significant implications in GI tumor biology,warranting further research to elucidate its mechanisms of action and develop targeted therapies that could improve patient outcomes.展开更多
The molecular structure of a higher plant myosin with two 174 kD heavy chains purified from the tendrils of Luffa cylindrica (L.) Roem. was viewed by electron microscopy. The myosin exhibited actin_activated MgATP...The molecular structure of a higher plant myosin with two 174 kD heavy chains purified from the tendrils of Luffa cylindrica (L.) Roem. was viewed by electron microscopy. The myosin exhibited actin_activated MgATPase activity and could be recognized immunologically by a monoclonal antibody against the skeletal muscle myosin. Electron micrographs of rotary shadowed images of this protein revealed that it had two heads with size and shape similar to those of the skeletal muscle myosin and a relatively short tail in comparison with the conventional myosin. Luffa tendril actin filaments were also visualized and occasionally other Luffa myosin_like proteins with globular structure at the tail ends were also observed. The structural similarity and immunological cross reactivity with antibodies against muscle myosin demonstrate that the 174 kD Luffa tendril myosin is a double_headed myosin. The possible involvement of myosin_actin interactions in Luffa tendril contact coiling will be the subject of further research.展开更多
文摘Myosin heavy chain 9(MYH9),a non-muscle myosin heavy chain protein,has been identified as a significant factor in gastrointestinal(GI)oncology,with its overexpression in various GI malignancies such as esophageal,gastric,and co-lorectal cancers being associated with poor prognosis and playing a role in tumor invasion and metastasis.This comprehensive review synthesizes the current body of knowledge regarding MYH9’s role in GI tumors,focusing on its molecular mechanisms,including its interaction with key signaling pathways like the phosphatidylinositol 3-kinase/protein kinase B/mechanistic target of rapamycin axis,which suggests a role in cancer cell survival,proliferation,and epithelial-mesenchymal transition.The review also explores MYH9’s potential as a therapeutic target,with preclinical models demonstrating promising results in inhibiting tumor growth and enhancing chemosensitivity.The evidence suggests that MYH9 is a multifaceted protein with significant implications in GI tumor biology,warranting further research to elucidate its mechanisms of action and develop targeted therapies that could improve patient outcomes.
文摘The molecular structure of a higher plant myosin with two 174 kD heavy chains purified from the tendrils of Luffa cylindrica (L.) Roem. was viewed by electron microscopy. The myosin exhibited actin_activated MgATPase activity and could be recognized immunologically by a monoclonal antibody against the skeletal muscle myosin. Electron micrographs of rotary shadowed images of this protein revealed that it had two heads with size and shape similar to those of the skeletal muscle myosin and a relatively short tail in comparison with the conventional myosin. Luffa tendril actin filaments were also visualized and occasionally other Luffa myosin_like proteins with globular structure at the tail ends were also observed. The structural similarity and immunological cross reactivity with antibodies against muscle myosin demonstrate that the 174 kD Luffa tendril myosin is a double_headed myosin. The possible involvement of myosin_actin interactions in Luffa tendril contact coiling will be the subject of further research.
