The fibrillin microfibril scaffold: A niche for growth factors and mechanosensation?

Sengle G, Sakai LY Matrix Biol. 2015 Sep;47:3-12 PMID: 25957947 Abstract The fibrillins, large extracellular matrix molecules, are polymerized to form „microfibrils.“ The fibrillin...   Read More

Abnormal Activation of BMP Signaling Causes Myopathy in Fbn2 Null Mice

Sengle G, Carlberg V, Tufa SF, Charbonneau NL, Smaldone S, Carlson EJ, Ramirez F, Keene DR, Sakai LY PLoS Genet. 2015 Jun;11(6):e1005340 PMID: 26114882...   Read More

Modeling autosomal recessive cutis laxa type 1C in mice reveals distinct functions for Ltbp-4 isoforms

B12 SENGLEpublicationsBultmann-Mellin I, Conradi A, Maul AC, Dinger K, Wempe F, Wohl AP, Imhof T, Wunderlich FT, Bunck AC, Nakamura T, Koli K, Bloch W, Ghanem A, Heinz A, von Melchner H, Sengle G, Sterner-Kock A; Dis Model Mech. 2015 Apr;8(4):403-15. doi: 10.1242/dmm.018960. Epub 2015 Feb 20.

Abstract Recent studies have revealed an important role for LTBP-4 in elastogenesis. Its mutational inactivation in humans causes autosomal recessive cutis laxa type 1C...   Read More

Nanoscale structure of the BMP antagonist chordin supports cooperative BMP binding

B12 SENGLEpublicationsTroilo H, Zuk AV, Tunnicliffe RB, Wohl AP, Berry R, Collins RF, Jowitt TA, Sengle G, Baldock C; Proc Natl Acad Sci U S A. 2014 Sep 9;111(36):13063-8. doi: 10.1073/pnas.1404166111. Epub 2014 Aug 25.

Abstract Bone morphogenetic proteins (BMPs) orchestrate key cellular events, such as proliferation and differentiation, in development and homeostasis. Extracellular antagonists, such as chordin, are...   Read More

Molecular and cellular basis of scleroderma

Eckes B, Moinzadeh P, Sengle G, Hunzelmann N, Krieg T J. Mol. Med. 2014 Sep;92(9):913-24 PMID: 25030650 Abstract Systemic sclerosis (scleroderma) is a chronic...   Read More

AMACO is a component of the basement membrane-associated Fraser complex

B12 SENGLEB2 WAGENER/ PAULSSONpublicationsRichardson RJ, Gebauer JM, Zhang JL, Kobbe B, Keene DR, Karlsen KR, Richetti S, Wohl AP, Sengle G, Neiss WF, Paulsson M, Hammerschmidt M, Wagener R; J Invest Dermatol. 2014 May;134(5):1313-22. doi: 10.1038/jid.2013.492. Epub 2013 Nov 14.

Abstract Fraser syndrome (FS) is a phenotypically variable, autosomal recessive disorder characterized by cryptophthalmus, cutaneous syndactyly, and other malformations resulting from mutations in FRAS1,...   Read More

Gremlin-1 associates with fibrillin microfibrils in vivo and regulates mesothelioma cell survival through transcription factor slug

B12 SENGLEpublications Tamminen JA, Parviainen V, Rönty M, Wohl AP, Murray L, Joenväärä S, Varjosalo M, Leppäranta O, Ritvos O, Sengle G, Renkonen R, Myllärniemi M, Koli K; Oncogenesis. 2013 Aug 26;2:e66. doi: 10.1038/oncsis.2013.29.

Abstract Malignant mesothelioma is a form of cancer that is highly resistant to conventional cancer therapy for which no major therapeutic advances have been...   Read More

A correlative method for imaging identical regions of samples by micro-CT, light microscopy, and electron microscopy: imaging adipose tissue in a model system

B12 SENGLEpublicationsSengle G, Tufa SF, Sakai LY, Zulliger MA, Keene DR; J Histochem Cytochem. 2013 Apr;61(4):263-71. doi: 10.1369/0022155412473757. Epub 2012 Dec 20.

Abstract We present a method in which a precise region of interest within an intact organism is spatially mapped in three dimensions by non-invasive...   Read More

Microenvironmental regulation by fibrillin-1

B12 SENGLEpublicationsSengle, G., Tsutsui, K., Keene, D.R., Tufa, S.F., Carlson, E.J., Charbonneau, N.L., Ono, R.N., Sasaki, T., Wirtz, M.K., Samples, J.R., Fessler, L.I., Fessler, J.H., Sekiguchi, K.,Hayflick, S.J., and Sakai, L.Y., PLoS Genet. 2012 Jan;8(1):e1002425. doi: 10.1371/journal.pgen.1002425. Epub 2012 Jan 5.

Abstract   Fibrillin-1 is a ubiquitous extracellular matrix molecule that sequesters latent growth factor complexes. A role for fibrillin-1 in specifying tissue microenvironments has...   Read More

Prodomains of transforming growth factor beta (TGFbeta) superfamily members specify different functions: extracellular matrix interactions and growth factor bioavailability

B12 SENGLEpublicationsSengle, G., Ono, R.N., Sasaki, T., and Sakai, L.Y., J Biol Chem. 2011 Feb 18;286(7):5087-99. doi: 10.1074/jbc.M110.188615. Epub 2010 Dec 6.

Abstract The specific functions of the prodomains of TGFβ superfamily members are largely unknown. Interactions are known between prodomains of TGFβ-1-3 and latent TGFβ-binding...   Read More

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