نتایج جستجو برای: collagen ix

تعداد نتایج: 79958  

Journal: :The Journal of biological chemistry 1988
P Bruckner M Mendler B Steinmann S Huber K H Winterhalter

Human collagen type IX was isolated from the media of organ cultures of fetal or infant hyaline cartilage. It consisted of three distinct, disulfide-bonded polypeptides of 115, 84, and 72 kDa, respectively. Digestion with chondroitinase ABC reduced the apparent molecular mass of the 115-kDa chain to about 65 kDa demonstrating that also human collagen type IX is a proteoglycan. In the electron m...

Journal: :Arthritis Research 2002
David Eyre

The extracellular framework and two-thirds of the dry mass of adult articular cartilage are polymeric collagen. Type II collagen is the principal molecular component in mammals, but collagens III, VI, IX, X, XI, XII and XIV all contribute to the mature matrix. In developing cartilage, the core fibrillar network is a cross-linked copolymer of collagens II, IX and XI. The functions of collagens I...

Journal: :Investigative ophthalmology & visual science 2004
Paul N Bishop David F Holmes Karl E Kadler David McLeod Kees Jan Bos

PURPOSE To determine whether aging vitreous collagen fibrils undergo ultrastructural changes that might underlie vitreous liquefaction and posterior vitreous detachment. METHODS Vitreous collagen fibrils from 21 human subjects (age range, 3-89 years) and from bovine eyes were isolated on electron microscopy grids. Cupromeronic blue labeling in the presence of 0.3 M MgCl(2) and immunogold labe...

2015
David Eyre

The extracellular framework and two-thirds of the dry mass of adult articular cartilage are polymeric collagen. Type II collagen is the principal molecular component in mammals, but collagens III, VI, IX, X, XI, XII and XIV all contribute to the mature matrix. In developing cartilage, the core fibrillar network is a cross-linked copolymer of collagens II, IX and XI. The functions of collagens I...

Journal: :The Biochemical journal 2001
F Zaucke R Dinser P Maurer M Paulsson

Primary chondrocytes dedifferentiate in serial monolayer with respect to their morphological and biosynthetic phenotype. They change from a round to a flattened fibroblast-like shape, and collagen I is secreted instead of the cartilage-specific collagen II. We analysed in detail the time course of dedifferentiation of mature bovine articular chondrocytes in monolayer for up to 32 weeks. Assessm...

Journal: :European cells & materials 2006
D R Eyre M A Weis J-J Wu

Adult articular cartilage by dry weight is two-thirds collagen. The collagen has a unique molecular phenotype. The nascent type II collagen fibril is a heteropolymer, with collagen IX molecules covalently linked to the surface and collagen XI forming the filamentous template of the fibril as a whole. The functions of collagens IX and XI in the heteropolymer are far from clear but, evidently, th...

Journal: :Journal of Thrombosis and Haemostasis 2009

Journal: :Molecular Vision 2008
Theodorus L. Ponsioen Marja J.A. van Luyn Roelofje J. van der Worp Hendri H. Pas Johanna M.M. Hooymans Leonoor I. Los

PURPOSE To investigate the capacity of cultured Müller cells to synthesize collagens, since previous studies indicated that Müller cells could be involved in collagen remodeling at the vitreoretinal border in adult human eyes. METHODS Spontaneously immortalized cultured human Müller cells were analyzed for the presence of mRNA of types I-VII, IX, XI, and XVII collagen by RT-PCR. Furthermore, ...

Journal: :The Journal of biological chemistry 1986
M H Irwin R Mayne

Recent results show that type IX collagen isolated from chicken cartilage is associated with one or perhaps two chondroitin sulfate chains. To locate the chondroitin sulfate chain(s) along the type IX collagen molecule, rotary shadowing was performed in the presence of monoclonal antibodies which recognize stubs of chondroitin sulfate generated after chondroitinase ABC digestion. Monoclonal ant...

Journal: :Investigative ophthalmology & visual science 1994
J M Fitch C M Linsenmayer T F Linsenmayer

PURPOSE The primary stroma of the developing avian cornea is a highly organized extracellular matrix composed largely of striated collagen fibrils synthesized by the epithelium. These fibrils are heterotypic structures consisting of at least two different fibrillar collagen types (I and II) and probably a fibril-associated collagen (type IX). The epithelial derivation and vectorial secretion of...

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