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Structure and Function of Cartilage
Published in Kyriacos A. Athanasiou, Eric M. Darling, Grayson D. DuRaine, Jerry C. Hu, A. Hari Reddi, Articular Cartilage, 2017
Kyriacos A. Athanasiou, Eric M. Darling, Grayson D. DuRaine, Jerry C. Hu, A. Hari Reddi
The N-terminal domain features two somatomedin B domains and a heparin binding domain. In vitronectin, the somatomedin B domain is able to bind plasminogen activator inhibitor 1 (PAI-1) (Keijer et al. 1991; Kost et al. 1992; Tomasini-Johansson et al. 1998) and inhibit plasmin; thus, SZP may have similar functions. The N-terminal domain undergoes heavy alternative splicing, which can result in the removal of these domains. Recent evidence suggests that the N-terminal domain also acts to bind the extracellular matrix (Zappone et al. 2007; DuRaine et al. 2011), resulting in a potential horseshoe conformation of SZP with each end bound and the mucin domain exposed.
Scaffold Vascularization
Published in Claudio Migliaresi, Antonella Motta, Scaffolds for Tissue Engineering, 2014
Lindsay E. Fitzpatrick, Alexandra Lisovsky, Ema C. Ciucurel, Michael V. Seftona
A quiescent EC layer is needed to create a non-thrombogenic surface.47,48 EC produce antithrombotic factors such as thrombomodulin, heparan sulfate, NO, and prostacyclin.47 Moreover, EC express tissue-type plasminogen activator, urokinase-type plasminogen activator, and plasminogen activator inhibitor 1, and play a key role in balancing fibrinolytic versus coagulation events. An intact, non-activated endothelium also provides a non-adherent surface for the platelets and leukocytes present in the blood, whereas activated EC upregulate the expression of adhesion molecules such as E-selectin, intercellular adhesion molecule 1 and vascular
Role of Streptokinase as a Thrombolytic Agent for Medical Applications
Published in Pankaj Bhatt, Industrial Applications of Microbial Enzymes, 2023
Hamza Rafeeq, Muhammad Anjum Zia, Asim Hussain, Ayesha Safdar, Muhammad Bilal, Hafiz M. N. Iqbal
Inhibitors of plasminogen activators (e.g., plasminogen activator inhibitor-1, PAI-1, a fast-acting inhibitor of tPA and uPA) and plasmin (e.g., a1-antiplasmin, a2 macroglobulin) modulate the fibrinolytic activity in circulation (Moore and Moore, 2020). In clinical intrusion, recombinant forms of normal human plasminogen activators tPA and uPA are used. Streptokinase (sPA) is another plasminogen activator frequently used. Streptokinase is a bacterial protein that is not present in human circulation naturally (Whyte and Mutch, 2020).
Conditioned medium from the three-dimensional culture of human umbilical cord perivascular cells accelerate the migration and proliferation of human keratinocyte and fibroblast
Published in Journal of Biomaterials Science, Polymer Edition, 2018
Min Ho Kim, Wen Hao Wu, Jee Hyun Choi, Ji Hyun Kim, Seok-Ho Hong, Jin Hyun Jun, Yong Ko, Jong Hun Lee
To analyze the protein components of PVC-CM, we performed 2-DE and MALDI-TOF. According to 2-DE, PVC-CM-2D and PVC-CM-3D detected 193 and 174 spots, respectively (Figure 5). Among these, PVC-CM-3D contained 9 spots with more than a 2-fold higher expression and 51 spots with less than a 2-fold lower expression compared with PVC-CM-2D, which showed 74 novel protein spots. With the exception of the near-70 kDa spots, some of these protein spots were analyzed using MALDI-TOF for protein mass fingerprinting (Table 1). Type I collagen and myosin heavy chain were more abundant in PVC-CM-3D than PVC-CM-2D, whereas carboxypeptidase A3, huntingtin interacting protein 1, and plasminogen activator inhibitor-1 (PAI-1) were expressed to a lesser extent. In addition, microtubule-actin cross-linked factor 1 (MACF1; KIAA0465), nebulin-related anchoring protein (N-RAP), thioredoxin, and drug-sensitive protein 1 were specifically expressed only in ADSC-CM-3D. Although KIAA0465 and N-RAP were also expressed in PVC-CM-2D, western analysis confirmed that the expression was high in PVC-CM-3D, and thioredoxin was expressed only in PVC-CM-3D (Figure 6).