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Full-Text Articles in Life Sciences
Advances In Cartilage Tissue Engineering Using Bioinks With Decellularized Cartilage And Three-Dimensional Printing, Roxanne N. Stone, Jonathon C. Reeck, Julia Thom Oxford
Advances In Cartilage Tissue Engineering Using Bioinks With Decellularized Cartilage And Three-Dimensional Printing, Roxanne N. Stone, Jonathon C. Reeck, Julia Thom Oxford
Biology Faculty Publications and Presentations
Osteoarthritis, a chronic, debilitating, and painful disease, is one of the leading causes of disability and socioeconomic burden, with an estimated 250 million people affected worldwide. Currently, there is no cure for osteoarthritis and treatments for joint disease require improvements. To address the challenge of improving cartilage repair and regeneration, three-dimensional (3D) printing for tissue engineering purposes has been developed. In this review, emerging technologies are presented with an overview of bioprinting, cartilage structure, current treatment options, decellularization, bioinks, and recent progress in the field of decellularized extracellular matrix (dECM)–bioink composites is discussed. The optimization of tissue engineering approaches using …
A Repeated Triple Lysine Motif Anchors Complexes Containing Bone Sialoprotein And The Type Xi Collagen A1 Chain Involved In Bone Mineralization, Jeff P. Gorski, Nichole T. Franz, Daniel Pernoud, Andrew Keightley, David R. Eyre, Julia Thom Oxford
A Repeated Triple Lysine Motif Anchors Complexes Containing Bone Sialoprotein And The Type Xi Collagen A1 Chain Involved In Bone Mineralization, Jeff P. Gorski, Nichole T. Franz, Daniel Pernoud, Andrew Keightley, David R. Eyre, Julia Thom Oxford
Biology Faculty Publications and Presentations
While details remain unclear, initiation of woven bone mineralization is believed to be mediated by collagen and potentially nucleated by bone sialoprotein (BSP). Interestingly, our recent publication showed that BSP and type XI collagen form complexes in mineralizing osteoblastic cultures. To learn more, we examined the protein composition of extracellular sites of de novo hydroxyapatite deposition which were enriched in BSP and Col11a1 containing an alternatively spliced “6b” exonal sequence. An alternate splice variant “6a” sequence was not similarly co-localized. BSP and Col11a1 co-purify upon ion-exchange chromatography or immunoprecipitation. Binding of the Col11a1 “6b” exonal sequence to bone sialoprotein was …
Enhanced Hyaluronan Signaling And Autophagy Dysfunction By Vps35 D620n, Abir A. Rahman, Alejandro Soto-Avellaneda, Iva Stojkovska, Nathan K. Lai, Joshua E. Albright, Abby R. Webb, Emily Oe, Jacob P. Valarde, Alexandra E. Oxford, Paige E. Urquhart, Brandon Wager, Connor Brown, Isabella Amado, Peyton Vasquez, Nicholas Lehning, Xinzhu Pu, Brad E. Morrison
Enhanced Hyaluronan Signaling And Autophagy Dysfunction By Vps35 D620n, Abir A. Rahman, Alejandro Soto-Avellaneda, Iva Stojkovska, Nathan K. Lai, Joshua E. Albright, Abby R. Webb, Emily Oe, Jacob P. Valarde, Alexandra E. Oxford, Paige E. Urquhart, Brandon Wager, Connor Brown, Isabella Amado, Peyton Vasquez, Nicholas Lehning, Xinzhu Pu, Brad E. Morrison
Biology Faculty Publications and Presentations
The motor features of Parkinson’s disease (PD) result from the loss of dopaminergic (DA) neurons in the substantia nigra with autophagy dysfunction being closely linked to this disease. A PD-causing familial mutation in VPS35 (D620N) has been reported to inhibit autophagy. In order to identify signaling pathways responsible for this autophagy defect, we performed an unbiased screen using RNA sequencing (RNA-Seq) of wild-type or VPS35 D620N-expressing retinoic acid-differentiated SH-SY5Y cells. We report that VPS35 D620N-expressing cells exhibit transcriptome changes indicative of alterations in extracellular matrix (ECM)-receptor interaction as well as PI3K-AKT signaling, a pathway known to regulate autophagy. Hyaluronan (HA) …
Beyond The Matrix: The Many Non-Ecm Ligands For Integrins, Bryce Lafoya, Jordan A. Munroe, Alison Miyamoto, Michael A. Detweiler, Jacob J. Crow, Tana Gazdik, Allan R. Albig
Beyond The Matrix: The Many Non-Ecm Ligands For Integrins, Bryce Lafoya, Jordan A. Munroe, Alison Miyamoto, Michael A. Detweiler, Jacob J. Crow, Tana Gazdik, Allan R. Albig
Biology Faculty Publications and Presentations
The traditional view of integrins portrays these highly conserved cell surface receptors as mediators of cellular attachment to the extracellular matrix (ECM), and to a lesser degree, as coordinators of leukocyte adhesion to the endothelium. These canonical activities are indispensable; however, there is also a wide variety of integrin functions mediated by non-ECM ligands that transcend the traditional roles of integrins. Some of these unorthodox roles involve cell-cell interactions and are engaged to support immune functions such as leukocyte transmigration, recognition of opsonization factors, and stimulation of neutrophil extracellular traps. Other cell-cell interactions mediated by integrins include hematopoietic stem cell …
Magp2 Controls Notch Via Interactions With Rgd Binding Integrins: Identification Of A Novel Ecm-Integrin-Notch Signaling Axis, Peter Deford, Kasey Brown, Rae Lee Richards, Aric King, Kristin Newburn, Katherine Westover, Allan R. Albig
Magp2 Controls Notch Via Interactions With Rgd Binding Integrins: Identification Of A Novel Ecm-Integrin-Notch Signaling Axis, Peter Deford, Kasey Brown, Rae Lee Richards, Aric King, Kristin Newburn, Katherine Westover, Allan R. Albig
Biology Faculty Publications and Presentations
Canonical Notch signaling involves Notch receptor activation via interaction with cell surface bound Notch ligand. Recent findings also indicate that Notch signaling may be modulated by cross-talk with other signaling mechanisms. The ECM protein MAGP2 was previously shown to regulate Notch in a cell type dependent manner, although the molecular details of this interaction have not been dissected. Here, we report that MAGP2 cell type specific control of Notch is independent of individual Notch receptor-ligand combinations but dependent on interaction with RGD binding integrins. Overexpressed MAGP2 was found to suppress transcriptional activity from the Notch responsive Hes1 promoter activity in …
Oncostatin M Binds To Extracellular Matrix In A Bioactive Conformation: Implications For Inflammation And Metastasis, Randall E. Ryan, Bryan Martin, Liliana Mellor, Reed B. Jacob, Ken Tawara, Owen M. Mcdougal, Julia Thom Oxford, Cheryl L. Jorcyk
Oncostatin M Binds To Extracellular Matrix In A Bioactive Conformation: Implications For Inflammation And Metastasis, Randall E. Ryan, Bryan Martin, Liliana Mellor, Reed B. Jacob, Ken Tawara, Owen M. Mcdougal, Julia Thom Oxford, Cheryl L. Jorcyk
Biology Faculty Publications and Presentations
Oncostatin M (OSM) is an interleukin-6-like inflammatory cytokine reported to play a role in a number of pathological processes including cancer. Full-length OSM is expressed as a 26 kDa protein that can be proteolytically processed into 24 kDa and 22 kDa forms via removal of C-terminal peptides. In this study, we examined both the ability of OSM to bind to the extracellular matrix (ECM) and the activity of immobilized OSM on human breast carcinoma cells. OSM was observed to bind to ECM proteins collagen types I and XI, laminin, and fibronectin in a pH-dependent fashion, suggesting a role for electrostatic …