A comparative analysis of the fibulin protein family. Biochemical characterization, binding interactions, and tissue localization.

A comparative analysis of the fibulin protein family. Biochemical characterization, binding interactions, and tissue localization. Research Abstract Details 

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A comparative analysis of the fibulin protein family. Biochemical characterization, binding interactions, and tissue localization. Abstract Text:

Naoyuki Kobayashi, Kostka, Garbe,Douglas R Keene,Hans Peter ,Franz-Georg Hanisch,Dessislava Markova,Takeshi Tsuda,Rupert Timpl,Mon-Li Chu,Takako Sasaki,

Fibulins are a family of five extracellular matrix proteins characterized by tandem arrays of epidermal growth factor-like domains and a C-terminal fibulin-type module. They are widely distributed and often associated with vasculature and elastic tissues. In this study, we expressed the three more recently identified family members, fibulin-3, fibulin-4, and fibulin-5, as recombinant proteins in mammalian cells. The purified proteins showed short rod structures of approximately 20 nm with a globule at one end, after rotary shadowing and electron microscopy. Two forms of mouse fibulin-3 were purified, and the O-glycan profiles of the larger form were characterized. Polyclonal antibodies raised against the purified proteins did not show any cross-reactivity with other family members and were used to assess the levels and localization of the fibulins in mouse tissues. Their binding interactions, cell adhesive properties, and tissue localization were analyzed in parallel with the previously characterized fibulin-1 and -2. Binding to tropoelastin was strong for fibulin-2 and -5, moderate for fibulin-4 and -1, and relatively weak for fibulin-3. Fibulin-4, but not fibulin-3 and -5, exhibited distinct interactions with collagen IV and nidogen-2 and moderate binding to the endostatin domain from collagen XV. Cell adhesive activities were not observed for all fibulins, except mouse fibulin-2, with various cell lines tested. All five fibulins were found in perichondrium and various regions of the lungs. Immunoelectron microscopy localized fibulin-4 and -5 to fibrillin microfibrils at distinct locations. Our studies suggest there are unique and redundant functions shared by these structurally related proteins.

A comparative analysis of the fibulin protein family. Biochemical characterization, binding interactions, and tissue localization. Publishing Authors By Initials

N Kobayashi,G Kostka,JH Garbe,DR Keene,HP ,FG Hanisch,D Markova,T Tsuda,R Timpl,ML Chu,T Sasaki,

For similar proteins: protein precursors: tropoelastin research abstracts see: proteins: protein precursors: tropoelastin research

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A comparative analysis of the fibulin protein family. Biochemical characterization, binding interactions, and tissue localization. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 11805-16

Journal Abbreviation:

ISSN: 0021-9258

DAY: 26

MONTH: 02

YEAR: 2007

A comparative analysis of the fibulin protein family. Biochemical characterization, binding interactions, and tissue localization. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

A comparative analysis of the fibulin protein family. Biochemical characterization, binding interactions, and tissue localization. Keywords Mesh Terms:

KEYWORDS: Tropoelastin

MESH TERMS: chemistry

Chemical & Substance for Abstract: A comparative analysis of the fibulin protein family. Biochemical characterization, binding interactions, and tissue localization. Information

Substance Name: Glycoside Hydrolases

Registry Number: EC 3.2.1.-

Grant and Affiliation Information for A comparative analysis of the fibulin protein family. Biochemical characterization, binding interactions, and tissue localization.

AFFILIATION: Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany.

Country: United States

AGENCY: United States NIGMS

GRANT: GM55625

ACRONYM: GM

MEDLINETA: J Biol Chem

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