serglycin Proteine (SRGN)

Human serglycin (SRGN) Interaktionspartner

1. SRGN overexpression promoted colorectal cancer cell migration and invasion and SRGN was physically binding to a hypoxia response element in its promoter region.

2. SRGN secreted by tumor cells and stromal components in the TME promotes malignant phenotypes through interacting with tumor cell receptor CD44 (zeige CD44 Proteine)

3. Extracellular spce serglycin upregulated CD44 (zeige CD44 Proteine) receptor expression to maintain nasopharyngeal carcinoma stemness by interacting with CD44 (zeige CD44 Proteine) and activating the MAPK (zeige MAPK1 Proteine)/beta-catenin (zeige CTNNB1 Proteine) pathway.

4. SRGN expression is significantly upregulated in human masticatory mucosa during wound healing

5. Patients with NPC (zeige NPC1 Proteine) with tumors showing strong tumor intensity and low infiltrated percentage of tumor-infiltrated lymphocytes with serglycin may be at high risk for distant metastases.

6. The elevated levels of serglycin in aggressive cancer and stromal cells may suggest a key role for serglycin in disease progression

7. These results suggest functions for serglycin in endothelial cells trough interactions with partner molecules, in biological processes with relevance for diabetic complications, cardiovascular disease and cancer development.

8. These results suggest that different signaling pathways are involved in regulating secretion of serglycin and partner molecules in activated endothelial cells.

9. The reduced expression of SRGN was accompanied by elevated levels of E-cadherin (zeige CDH1 Proteine).

10. These studies provide direct evidence for a critical role for serglycin in MM pathogenesis and show that targeting serglycin may provide a novel therapeutic approach for MM.

Mouse (Murine) serglycin (SRGN) Interaktionspartner

1. serglycin produced in lipopolysaccharide-induced inflammation in normal mouse chondrocytes is able to modulate inflammation by interacting with CD44 (zeige CD44 Proteine) receptor, suggesting a possible key role in the cartilage inflammation.

2. Findings indicate that PRG-1 (zeige PTGR1 Proteine) deficiency led to over-excitability caused by an altered LPA/LPA2 (zeige LPAR2 Proteine)-R signaling inducing a behavioral phenotype typically observed in animal models for psychiatric disorders.

3. this study shows that the serglycin-deficient mice are more susceptible to Trichinella spiralis infection and display an unbalanced immune response

4. Data suggest that serglycin proteoglycans play a role in extravasation as well as colonization and growth of metastatic cells.

5. serglycin deficient mice exhibited elevated concentrations of serum LDL after feeding high-fat diet for 20 weeks.

6. serglycin plays a critical role in the maturation of dense-core cytotoxic granules in cytotoxic lymphocytes and the trafficking and storage of perforin (zeige PRF1 Proteine) and granzyme B, whereas granzyme A (zeige GZMA Proteine) is unaffected

7. Wild-type mast cells efficiently degraded exogenous or endogenously produced IL-13 (zeige IL13 Proteine) upon degranulation,whereas serglycin -/- mast cells completely lacked this ability.

8. Dopamine storage increased during mast cell maturation from bone marrow precursors, and was dependent on the presence of serglycin.

9. Cells lacking mouse mast cell protease 6 exhibited similar defects in apoptosis as observed in serglycin(-/-) cells, indicating that the pro-apoptotic function of serglycin is due to downstream effects of proteases that are complex-bound to serglycin

10. The PRG-1 (zeige PTGR1 Proteine) transcription is initiated at multiple transcription start site and no influence on expression in vivo by Nex1 (zeige NEUROD6 Proteine) deficiency.