Contributes to the aerobic glycolysis (Warburg effect), which is associated with aggressive, poor differentiated, metastatic tumors, resistance against chemotherapy, and shortened patients survival
Is the critical enzyme for glycolysis. PKM2 diverts glucose-derived carbons from catabolic to anabolic (biosynthetic) pathways, which is a hallmark of cancer
We found that SEMG1 interacted with both LDHA and PKM2, whereas SEMG2 interacted with PKM2 only
Piruvato quinasa M2 (PKM2) y lactato deshidrogenasa A (LDHA)
SEMG1 and SEMG2 genes belong to the family of cancer-testis antigens (CTAs), whose expression normally is restricted to male germ cells but is often restored in various malignancies. High levels of SEMG1 and SEMG2 expression are detected in prostate, renal, and lung cancer as well as hemoblastosis.
However, the functional importance of both SEMGs proteins in human neoplasms is still largely unknown.
We have demonstrated that SEMG1 and SEMG2 are frequently expressed in lung cancer clinical samples and cancer cell lines of different origins and are negatively associated with the survival rate of cancer patients.
Using the pull-down assay followed by LC-MS/MS mass-spectrometry, we have identified 119 proteins associated with SEMG1 and SEMG2. Among the SEMGs interacting proteins we noticed two critical glycolytic enzymes-pyruvate kinase M2 (PKM2) and lactate dehydrogenase A (LDHA).
Importantly, we showed that SEMGs increased the protein level and activity of both PKM2 and LDHA. Further, both SEMGs increased the membrane mitochondrial potential (MMP), glycolysis, respiration, and ROS production in several cancer cell lines. Taken together, these data provide first evidence that SEMGs can up-regulate the energy metabolism of cancer cells, exemplifying their oncogenic features.
Spermatozoa (spermatozoon cells)
Semenogelin (SEMG1/SEMG2) (ROS) generation FROM Seminal vesicles
Prostate-specific antigen (PSA) FROM Prostated gland (epithelial cells)
Component | Source | Function |
---|---|---|
Semenogelins (SEMG1/2) | Seminal vesicles | Gel semen, regulate viscosity; oncogenic in cancers via metabolic enzyme interaction |
PKM2 and LDHA | Cancer cells | Glycolytic enzymes promoting Warburg effect and tumor progression |
Prostate-specific antigen | Prostate gland | Liquefies semen by breaking down semenogelins |
Hydroxyapatite (HAP) | Teeth enamel | Supports tissue regeneration and repair |
Mucin | Goblet cells in epithelia | Provides mucus viscosity and protection |
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