Srpk1-flox Mouse

Srpk1, or Serine-Arginine Protein Kinase 1, is an enzyme that phosphorylates splicing factors rich in serine/arginine domains. It is involved in various cellular activities such as cell cycle progression, innate immune response, chromatin reorganization, and regulation of mRNA-processing pathways [3]. It is associated with multiple signaling pathways including PI3K/AKT, NF-κB, and TGF-β, which are related to oncogenesis [2,3].

In the context of fertilized oocytes, Srpk1 initiates parental genome reprogramming by catalyzing site-specific phosphorylation of protamine, triggering protamine-to-histone exchange [1]. In cancer, elevated Srpk1 expression is linked to advanced disease stage and poor survival in many epithelial-derived cancers. Pre-clinical studies have shown that increased Srpk1 expression is associated with cancer cell proliferation, invasion, migration, and apoptosis in vitro, as well as tumor growth, tumorigenicity, and metastasis in vivo [2]. In sepsis-induced acute lung injury, overexpression of Srpk1 suppressed pyroptosis of human pulmonary microvascular endothelial cells, promoted cell proliferation, and alleviated the injury by regulating the PI3K/AKT/FOXO3/NLRP3 signaling pathway [4].

In conclusion, Srpk1 has diverse and crucial biological functions. Its role in parental genome reprogramming at the beginning of life is significant. In diseases, especially cancer, its abnormal expression is closely related to cancer development and progression. Studies on Srpk1 using various models help to understand its functions in different biological processes and disease conditions, potentially providing new targets for disease treatment.