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204. Fibrillin Assembly Requires Fibronectin

Author

Sabatier, Laetitia, primary, Chen, Daliang, additional, Fagotto-Kaufmann, Christine, additional, Hubmacher, Dirk, additional, McKee, Marc D., additional, Annis, Douglas S., additional, Mosher, Deane F., additional, and Reinhardt, Dieter P., additional

Published
2009
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216. Periostin and TGF- β -induced protein: Two peas in a pod?

Author

Mosher, Deane F., Johansson, Mats W., Gillis, Mary E., and Annis, Douglas S.

Subjects
*PERIOSTIN, *TRANSFORMING growth factors-beta, *ASTHMA, *CARBOXYLATION, *GOLGI apparatus, *INTEGRINS
Abstract

Periostin (PN) and TGF-β-induced protein (βig-h3) are paralogs that contain a single emilin and four fasciclin-1 modules and are secreted from cells. PN receives attention because of its up-regulation in cancer and degenerative and allergic diseases. βig-h3 is highly enriched in cornea and best known for harboring mutations in humans associated with corneal dystrophies. Both proteins are expressed widely, and many functions, some over-lapping, have been attributed to PN and βig-h3 based on biochemical, cell culture, and whole animal experiments. We attempt to organize this knowledge so as to facilitate research on these interesting and incompletely understood proteins. We focus particularly on whether PN and βig-h3 are modified by vitamin K-dependent γ-glutamyl carboxylation, a question of considerable importance given the profound effects of γ-carboxylation on structure and function of other proteins. We consider the roles of PN and βig-h3 in formation of extracellular matrix and as ligands for integrin receptors. We attempt to reconcile the contradictory results that have arisen concerning the role of PN, which has emerged as a marker of TH2 immunity, in murine models of allergic asthma. Finally, when possible we compare and contrast the structures and functions of the two proteins. [ABSTRACT FROM PUBLISHER]

Published
2015
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218. Biophysical Studies of the Type 1 Repeats of Human Thrombospondin-1 to Characterize the Structural Basis of its Angiostatic Effect

Author

WISCONSIN UNIV-MADISON, Huwiler, Kristin G., Mosher, Deane F., WISCONSIN UNIV-MADISON, Huwiler, Kristin G., and Mosher, Deane F.

Abstract

Thrombospondin-1 (TSP1) is a disulfide bonded trimer of 450kD; each monomer contains three type 1 repeats (T1Rs). TSP1 and fragments that include the T 1Rs have several documented functions including a role as an inhibitor of endothelial cell growth and migration, as well as an inducer of apoptosis. The purpose of this study was to express, purify, and biophysically characterize the T1Rs. Recombinant baculoviruses were generated that express the three T1Rs in tandem (P123) and the third T1R (P3) as secreted histidine-tagged fusion proteins. Protein purity, molecular mass determination, and di sulfide-bond content was determined using mass spectroscopy. Micro-heterogenity arising from differential glycosylation was determined by western blotting, HPLC, and mass spectroscopy. Circular dichroism was used to access secondary and tertiary structure as well as thermal stability. Fluorescence spectroscopy revealed that the conserved tryptophans were quenched and in a partial polar environment in the native state. The effect of TSP1 and the T1Rs on endothelial cell (EC) morphology and death was determined. The results indicate the T1R encodes an independently folding protein module with spectral properties dominated by the conserved tryptophans. The protein is heterogeneously glycosylated with C-linked and 0-linked sugars. The T1Rs are not responsible for the apoptotic effect on Ecs.

Published
1999

225. Biophysical Studies of the Type 1 Repeats of Human Thrombospondin-1 to Characterize the Structural Basis of its Angiostatic Effect.

Author

WISCONSIN UNIV-MADISON, Huwiler, Kristin G., Mosher, Deane F., WISCONSIN UNIV-MADISON, Huwiler, Kristin G., and Mosher, Deane F.

Abstract

Thrombospondin-1 (TSP1) is a disulfide bonded trimer of 450 kD); each monomer contains three type 1 repeats (T1Rs). TSP1 has several documented functions including its role as an angiogenic inhibitor. TSP1 and TSP1 fragments that include the T1Rs cause an endothelial cell-specific inhibition of growth and migration. The T1Rs were expressed using the baculovirus protein expression system. Recombinant baculoviruses were generated that express the three T1Rs in tandem (P123) and the third T1R (P3) as secreted histidine-tagged fusion proteins. N-terminal sequencing of P123 and P3 confirmed that the signal sequence was homogeneously removed. Protein purity, molecular mass determination, and disulfide-bond content was determined using mass spectroscopy. Circular Dichroism (CD) was used to access secondary and tertiary structure. The far-UV CD spectra for P3 and P123 are marked by distinctive positive ellipticity that is lost by thermal denaturation. The near-UV CD spectra are positive and upon heating approach zero ellipticity. Fluorescence spectroscopy revealed that the tryptophans were quenched and the maximum emission wavelength was red-shifted upon treatment with either DTT or guanidine hydrochloride. These results indicate that the T1R encodes an independently folding protein module with spectral properties dominated by the conserved tryptophans.

Published
1998

228. Biophysical Studies of the Type 1 Repeats of Human Thrormbospondin-1 to Characterize the Structural Basis of Its Angiostatic Effect.

Author

WISCONSIN UNIV-MADISON, Huwiler, Kristin G., Mosher, Deane F., WISCONSIN UNIV-MADISON, Huwiler, Kristin G., and Mosher, Deane F.

Abstract

Thrombospondin-1 (TSP1) is a modular trimeric protein wit several documented functions, including its role as an angiogenic inhibitor. TSP1, TSP1 fragments, and certain TSP1 conserved peptide sequences have been shown to exert an endothelial-specific inhibition of growth and migration. Peptides derived from conserved sequences within the type 1 repeats of TSP1 have been shown to block neo-vascularization in vivo, inhibit DNA synthesis, and migration of cultured endothelial cells in vitro. Our laboratory has shown that recombinantly expressed human TSP1 (hTSP1) type 1 repeats inhibit migration of bFGF stimulated bovine adrenal microvascular endothelial cells. This study seeks to define the structural basis for the angiostatic effect of the hTSP1 type 1 repeats. I will employ biophysical methods in a comparative study of TSP 1 type 1 repeats and active peptides based on type 1 sequences. I have successfully generated recombinant baculoviruses that express the three type 1 repeats in tandem (P123) and the third type 1 repeat (P3) as histidine-tagged fusion proteins. A purification scheme for the recombinant proteins including removal of the histidine-tag has been established. To date, N-terminal sequencing, carbohydrate analysis, and circular dichroism have been performed.

Published
1997

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