Fibrillin-1 and -2 differentially modulate endogenous TGF-? and BMP bioavailability during bone formation

B12 SENGLEpublicationsNistala, H., Lee-Arteaga, S., Smaldone, S., Siciliano, G., Carta, L., Ono, R., Sengle, G., Arteaga- Solis, E., Levasseur, R., Ducy, P., Sakai, L., Karsenty, and G., Ramirez, F., J Cell Biol. 2010 Sep 20;190(6):1107-21. doi: 10.1083/jcb.201003089.

Abstract Extracellular regulation of signaling by transforming growth factor (TGF)-β family members is emerging as a key aspect of organ formation and tissue remodeling....   Read More

In vivo studies of mutant fibrillin-1 microfibrils

B12 SENGLEpublicationsCharbonneau, N.L., Carlson, E.J., Tufa, S., Sengle, G., Carlberg, V.M., Ramirez, F., Keene, D.R., and Sakai, L.Y., J Biol Chem. 2010 Aug 6;285(32):24943-55. doi: 10.1074/jbc.M110.130021. Epub 2010 Jun 7.

Abstract In humans, mutations in fibrillin-1 result in a variety of genetic disorders with distinct clinical phenotypes. While most of the known mutations in...   Read More

ADAMTSL-6 is a novel extracellular matrix protein that binds to fibrillin-1 and promotes fibrillin-1 fibril formation

B12 SENGLEpublicationsTsutsui, K., Manabe, R.I., Yamada, T., Nakano, I., Oguri, Y., Keene, D.R., Sengle, G., Sakai, L.Y., and Sekiguchi, K., J Biol Chem. 2010 Feb 12;285(7):4870-82. doi: 10.1074/jbc.M109.076919. Epub 2009 Nov 23.

Abstract ADAMTS (A disintegrin and metalloproteinase with thrombospondin motifs)-like (ADAMTSL) proteins, a subgroup of the ADAMTS superfamily, share several domains with ADAMTS proteinases, including...   Read More

Latent transforming growth factor beta-binding proteins and fibulins compete for fibrillin-1 and exhibit exquisite specificities in binding sites

B12 SENGLEpublicationsOno, R.N., Sengle, G., Charbonneau, N.L., Carlberg, V., Bächinger, H.P., Sasaki, T., Lee-Arteaga, S., Zilberberg, L., Rifkin, D.B., Ramirez, F., Chu, M.L., and Sakai, L.Y., J Biol Chem. 2009 Jun 19;284(25):16872-81. doi: 10.1074/jbc.M809348200. Epub 2009 Apr 6.

Abstract Latent transforming growth factor (TGF) beta-binding proteins (LTBPs) interact with fibrillin-1. This interaction is important for proper sequestration and extracellular control of TGFbeta....   Read More

A new model for growth factor activation: type II receptors compete with the prodomain for BMP-7

B12 SENGLEpublicationsSengle, G., Ono, R., Lyons, K.M., Bächinger, H.P., and Sakai, L.Y., J Mol Biol. 2008 Sep 12;381(4):1025-39. doi: 10.1016/j.jmb.2008.06.074. Epub 2008 Jul 2.

Abstract Bone morphogenetic proteins (BMPs) are morphogens with long-range signaling activities. BMP-7 is secreted as a stable complex consisting of a growth factor noncovalently...   Read More

Targeting of bone morphogenetic protein growth factor complexes to fibrillin

B12 SENGLEpublications Sengle, G., Charbonneau, N.L., Ono, R.N., Sasaki, T., Alvarez, J., Keene, D.R., Bächinger H.P., and Sakai, L.Y., J Biol Chem. 2008 May 16;283(20):13874-88. doi: 10.1074/jbc.M707820200. Epub 2008 Mar 13.

Abstract Both latent transforming growth factor-beta (TGF-beta)-binding proteins fibrillins are components of microfibril networks, and both interact with members of the TGF-beta family of...   Read More

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