نتایج جستجو برای: collagen iv

تعداد نتایج: 235564  

Journal: :American journal of physiology. Gastrointestinal and liver physiology 2004
Matthew A Sanders Marc D Basson

Our previous work indicates intestinal epithelial cell ERK activation by collagen IV, a major component of the intestinal epithelial basement membrane, requires focal adhesion kinase (FAK) and suggests FAK and ERK may have important roles in regulating intestinal epithelial cell migration. We therefore sought to identify FAK downstream targets regulating intestinal epithelial cell spreading, mi...

Journal: :The Journal of Cell Biology 1990
J M Fitch D E Birk C Linsenmayer T F Linsenmayer

The organization of type IV collagen in the unconventional basement membrane of the corneal endothelium (Descemet's membrane) was investigated in developing chicken embryos using anti-collagen mAbs. Both immunofluorescence histochemistry and immunoelectron microscopy were performed. In mature embryos (greater than 15 d of development), the type IV collagen of Descemet's membrane was present as ...

Journal: :Arteriosclerosis, thrombosis, and vascular biology 2009
A Wayne Orr Monica Y Lee Julia A Lemmon Arif Yurdagul Maria F Gomez Pamela D Schoppee Bortz Brian R Wamhoff

OBJECTIVE Smooth muscle cell (SMC) phenotypic modulation, an important component of atherosclerosis progression, is critically regulated by the matrix, with normal components of the healthy SMC matrix limiting modulation and atherosclerosis-associated transitional matrix proteins promoting phenotypic modulation. We sought to determine how collagen IV (which comprises the healthy artery wall) an...

Journal: :Investigative ophthalmology & visual science 1989
E P Kay

Expression of type I and type IV collagen genes was studied in normal endothelial cells and in modulated endothelial cells (formerly designated as fibroblastic corneal endothelial cells: FCEC). There appear to be distinct collagen phenotypes in these cells; normal cells produce type IV collagen as a major type, while the modulated cells produce predominantly type I collagen. The absence of type...

Journal: :The Journal of Cell Biology 1988
T J Herbst J B McCarthy E C Tsilibary L T Furcht

Laminin and type IV collagen were compared for the ability to promote aortic endothelial cell adhesion and directed migration in vitro. Substratum-adsorbed IV promoted aortic endothelial cell adhesion in a concentration dependent fashion attaining a maximum level 141-fold greater than controls within 30 min. Aortic endothelial cell adhesion to type IV collagen was not inhibited by high levels (...

Journal: :The Journal of Cell Biology 1991
P J Lein D Higgins D C Turner L A Flier V P Terranova

We have examined the effects of collagen IV on the morphological development of embryonic rat sympathetic neurons in vitro. In short-term (less than or equal to 24 h) culture, collagen IV accelerated process outgrowth, causing increases in the number of neurites and total neuritic length. Analysis of proteolytic fragments of collagen IV indicated that the NC1 domain was nearly as active as the ...

Journal: :The Journal of Cell Biology 1986
M Aumailley R Timpl

Of ten different cell lines examined, three showed distinct attachment and spreading on collagen IV substrates, and neither attachment nor spreading was enhanced by adding soluble laminin or fibronectin. This reaction was not inhibited by cycloheximide or antibodies to laminin, indicating a direct attachment to collagen IV without the need of mediator proteins. Cell-binding sites were localized...

Journal: :Molecular human reproduction 1999
S Yamada H Fujiwara T Honda T Higuchi T Nakayama T Inoue M Maeda S Fujii

Previously, it has been shown that integrin alpha6beta1 expressed on human granulosa cells regulates luteinization in co-operation with its ligand, laminin. In this study, integrin alpha2 was immunohistochemically demonstrated to be expressed on granulosa and large luteal cells. It was also detected on luteinizing theca interna cells after ovulation. Immunoreactive collagen type IV, which is on...

Journal: :The Journal of Cell Biology 1985
A S Charonis E C Tsilibary P D Yurchenco H Furthmayr

A mixture of laminin and type IV collagen was analyzed by rotary shadowing using carbon/platinum and electron microscopy. Laminin was found to form distinct complexes with type IV collagen: one site of interaction is located 140 nm from the COOH-terminal, noncollagenous (NC1) domain and the other is located within the NH2-terminal region. The isolated NC1 fragment of type IV collagen does not a...

Journal: :Blood 1996
K Iwabuchi I Nagaoka A Someya T Yamashita

To isolate type IV collagen-binding proteins, 125I-labeled human-neutrophil extracts were chromatographed on a type IV collagen-Sepharose column. The affinity chromatography-separated fraction contained the four radioactive proteins with apparent molecular masses of 28, 49, 67, and 95 kD on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Western blot analysis indicated that the 95-kD...

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