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Publications

ADAM17-dependent proteolysis of L-selectin promotes early clonal expansion of cytotoxic T cells.

Mohammed RN. et al, (2019), Sci rep, 9

Heparan Sulfate Proteoglycan Synthesis Is Dysregulated in Human Osteoarthritic Cartilage.

Chanalaris A. et al, (2019), Am j pathol, 189, 632 - 647

LRP1 Controls TNF Release via the TIMP-3/ADAM17 Axis in Endotoxin-Activated Macrophages.

Schubert K. et al, (2019), J immunol, 202, 1501 - 1509

Effect of Polarization and Chronic Inflammation on Macrophage Expression of Heparan Sulfate Proteoglycans and Biosynthesis Enzymes.

Swart M. and Troeberg L., (2019), J histochem cytochem, 67, 9 - 27

Heparan sulfate as a regulator of inflammation and immunity.

Collins LE. and Troeberg L., (2019), J leukoc biol, 105, 81 - 92

Increased TIMP-3 expression alters the cellular secretome through dual inhibition of the metalloprotease ADAM10 and ligand-binding of the LRP-1 receptor.

Scilabra SD. et al, (2018), Sci rep, 8

Monoclonal antibodies targeting the disintegrin-like domain of ADAMDEC1 modulates the proteolytic activity and enables quantification of ADAMDEC1 protein in human plasma.

Lund J. et al, (2018), Mabs, 10, 118 - 128

Suramin Inhibits Osteoarthritic Cartilage Degradation by Increasing Extracellular Levels of Chondroprotective Tissue Inhibitor of Metalloproteinases 3.

Chanalaris A. et al, (2017), Mol pharmacol, 92, 459 - 468

Inhibition of Shedding of Low-Density Lipoprotein Receptor-Related Protein 1 Reverses Cartilage Matrix Degradation in Osteoarthritis.

Yamamoto K. et al, (2017), Arthritis rheumatol, 69, 1246 - 1256

Dissecting the interaction between tissue inhibitor of metalloproteinases-3 (TIMP-3) and low density lipoprotein receptor-related protein-1 (LRP-1): Development of a "TRAP" to increase levels of TIMP-3 in the tissue.

Scilabra SD. et al, (2017), Matrix biol, 59, 69 - 79

ADAMTS and ADAM metalloproteinases in osteoarthritis - looking beyond the ‘usual suspects’

Yang CY. et al, (2017), Osteoarthritis cartilage

MMP-13 is constitutively produced in human chondrocytes and co-endocytosed with ADAMTS-5 and TIMP-3 by the endocytic receptor LRP1.

Yamamoto K. et al, (2016), Matrix biol, 56, 57 - 73

Engineered Tissue Inhibitor of Metalloproteinases-3 Variants Resistant to Endocytosis Have Prolonged Chondroprotective Activity.

Doherty CM. et al, (2016), J biol chem, 291, 22160 - 22172

Brief Report: JNK-2 Controls Aggrecan Degradation in Murine Articular Cartilage and the Development of Experimental Osteoarthritis.

Ismail HM. et al, (2016), Arthritis rheumatol, 68, 1165 - 1171

Interleukin-1 Acts via the JNK-2 Signaling Pathway to Induce Aggrecan Degradation by Human Chondrocytes.

Ismail HM. et al, (2015), Arthritis rheumatol, 67, 1826 - 1836

Extracellular regulation of metalloproteinases.

Yamamoto K. et al, (2015), Matrix biol, 44-46, 255 - 263

Evidence for restricted reactivity of ADAMDEC1 with protein substrates and endogenous inhibitors.

Lund J. et al, (2015), J biol chem, 290, 6620 - 6629

Sulfated glycosaminoglycans control the extracellular trafficking and the activity of the metalloprotease inhibitor TIMP-3.

Troeberg L. et al, (2014), Chem biol, 21, 1300 - 1309

Low density lipoprotein receptor-related protein 1 (LRP1)-mediated endocytic clearance of a disintegrin and metalloproteinase with thrombospondin motifs-4 (ADAMTS-4): functional differences of non-catalytic domains of ADAMTS-4 and ADAMTS-5 in LRP1 binding.

Yamamoto K. et al, (2014), J biol chem, 289, 6462 - 6474

LRP-1-mediated endocytosis regulates extracellular activity of ADAMTS-5 in articular cartilage.

Yamamoto K. et al, (2013), Faseb j, 27, 511 - 521

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