serpin Peptidase Inhibitor, Clade D (Heparin Cofactor), Member 1 (SERPIND1) Kits ELISA

Human serpin Peptidase Inhibitor, Clade D (Heparin Cofactor), Member 1 (SERPIND1) interaction partners

1. Loss of Heparin Cofactor is associated with insulin resistance .

2. The plasma level of alpha2M was found positively correlated, while HCII level was negatively correlated with higher vulnerability of carotid plaques. Both proteins were efficient in differentiating stable and vulnerable carotid plaques. These provide potential new targets for the research of carotid plaque vulnerability. Plasma alpha2M and HCII may be potential biomarkers for evaluation of the vulnerability of carotid ...

3. We found that SERPIND1 may act as a potential oncogene in the development of ovarian cancer

4. Molecular modelling of HCII 1-75 predicted those portions of the acidic extension that had been previously visualized in crystal structures, and suggested that an alpha-helix found between residues 26 and 36 stabilizes one found between residues 61-67.

5. heparin co-factor II is a novel metastasis enhancer and may be used as a prognostic predictor for heparin treatment in non-small cell lung cancer

6. In this study, we demonstrate a previously unknown role for HCII in host defense.

7. HCII potentiates the activation of vascular endothelial cells and the promotion of angiogenesis in response to hindlimb ischemia via an AMPK-eNOS signaling pathway.

8. Plasma heparin cofactor II activity was independently and inversely associated with the development of cardiac remodeling, including cardiac concentric change, left atrial enlargement and left ventricular diastolic dysfunction.

9. [REVIEW]HCII protects against vascular remodeling, including atherosclerosis

10. potential for oversulfated disaccharides in controlling HCII-regulated thrombin generation

11. Aspartic acid residues 72 and 75 and tyrosine-sulfate 73 of heparin cofactor II promote

12. role of basic amino acids of the A helix of heparin cofactor II in heparin- or dermatan sulfate-mediated thrombin inhibition.

13. Altering heparin cofactor II at VAL439 (P6) either impairs inhibition of thrombin or confers elastase resistance.

14. The interactions of HCII with various heparins in solution competition experiments using SPR show that while calcium enhances this interaction, the activity of heparin-HCII complex against thrombin is not calcium dependent but can be enhanced by it.

15. structure analysis of the thrombin-heparin cofactor II complex

16. An asymptomatic Glu428Lys mutation affecting a conserved glutamate at the hinge (P17) of the reactive loop confirms the key structural role of the P17 glutamate in serpins.

17. after receiving stent for peripheral artery disease, patients with a high HCII activity had a 0.39-fold reduced risk for instent restenosis

18. HCII activity increases during pregnancy, and HCII levels are significantly decreased in women with severe pre-eclampsia.

19. These results suggest that transfer of the N-terminal acidic extension of HCII to alpha1-PI M358R enhanced its inhibition of thrombin by conferring the ability to bind exosite 1 on HAPI M358R.

20. Beta2-glycoprotein I (B2G1) protected thrombin against inactivation by HCII (heparin cofactor II)/heparin

Mouse (Murine) serpin Peptidase Inhibitor, Clade D (Heparin Cofactor), Member 1 (SERPIND1) interaction partners

1. Trancriptomic analysis shows that expression of the antithrombins serpin C1 and D1 is significantly reduced in Schwann cell-deficient mice. In the absence of peripheral neuromuscular activity, neurodegeneration is completely blocked, and expression of prothrombin in muscle is markedly reduced.

2. Loss of Heparin Cofactor is associated with insulin resistance .

3. In this study, we demonstrate a previously unknown role for HCII in host defense

4. HCII potentiates the activation of vascular endothelial cells and the promotion of angiogenesis in response to hindlimb ischemia via an AMPK-eNOS signaling pathway.

5. HCII mediates the antithrombotic effect of porcine skin dermatan sulfate after injury to the carotid arterial endothelium in mice.

6. In HCII(+/-) mice, prominent intimal hyperplasia with increased cellular proliferation was observed after tube cuff and wire vascular injury.

7. HCII deficiency promotes atherogenesis and neointima formation

8. The reactions with thrombin or APC of recombinant alpha(1)-PI M358R variants with or without the HCII extension were characterized electrophoretically and kinetically

9. These results support the hypothesis that HCII interacts with dermatan sulfate in the vessel wall after disruption of the endothelium and that this interaction regulates thrombus formation in vivo.