Nidogen: a new, self‐aggregating basement membrane protein

Timpl, Rupert; Dziadek, Marie; Fujiwara, Sakuhei; Nowack, Hans; Wick, Georg

doi:10.1111/j.1432-1033.1983.tb07849.x

Cited by 253 publications

(98 citation statements)

References 37 publications

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“…BMs separate epithelial (or endothelial) cells from mesenchymal tissues and maintain the function and morphology of epithelial cells. In the BM, laminin and type IV collagen form meshes that are linked by nidogen (Carlin et al, 1981;Timpl et al, 1983). We found here that laminin and nidogen-1 accumulate normally in the BM of 9.5 dpc Hsp47…”

Section: Discussionsupporting

confidence: 59%

Accumulation of type IV collagen in dilated ER leads to apoptosis inHsp47-knockout mouse embryos via induction of CHOP

Marutani

Yamamoto

Nagai

et al. 2004

Journal of Cell Science

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Hsp47 is an endoplasmic reticulum (ER)-resident molecular chaperone that is specific for collagen. In Hsp47–/– mouse embryos at 9.5 days postcoitus (dpc), immunostaining indicated the absence of type IV collagen, but not of laminin and nidogen-1, in the basement membrane (BM). Electron immunomicroscopy revealed accumulation of type IV collagen in dilated ERs, but not in the BM of Hsp47–/– embryos, whereas it was only present in the BM in Hsp47+/+ embryos. The BM structures stained with anti-laminin and anti-nidogen-1 antibody became disrupted in Hsp47–/– embryos at 10.5 dpc. Thus, in the absence of type IV collagen in the BM owing to the lack of Hsp47, the structure of the BM cannot be maintained during the dramatic morphological changes that take place around 10.5 dpc. Type IV collagen is therefore indispensable for the maintenance of BM structures during the late-stage development of mouse embryos, although not essential for the initial formation of the BM. Just before the death of Hsp47–/– embryos, DNA fragmentation typical of apoptosis was observed at 10.5 dpc together with significantly upregulated CHOP mRNA expression. ER stress caused by the accumulation of misfolded collagen may have induced apoptosis in Hsp47-knockout embryos through the upregulation of CHOP.

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Section: Discussionsupporting

confidence: 59%

Accumulation of type IV collagen in dilated ER leads to apoptosis inHsp47-knockout mouse embryos via induction of CHOP

Marutani

Yamamoto

Nagai

et al. 2004

Journal of Cell Science

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“…Lack of staining was also consistently observed with visceral yolk sac, placenta, embryonic and adult skin, nerve ganglia and adult gut and kidney. All these mouse tissues, as shown previously [5,13,16,23,26,27], show strong basement membrane immunofluorescence when examined with antibodies against laminin, nidogen, proteoglycan and collagen IV.…”

Section: Tissue Distributionmentioning

confidence: 73%

“…Samples were hydrolyzed in 6 M HC1 (llOOC, 24 h) for amino acid analysis on a Biotronik analyzer and with 3 M HCl (llO°C, 16 h) for hexosamine analysis [23]. Values for threonine and serine were corrected by factors of 1.08 and 1.21 respectively, to account for hydrolytic losses.…”

Section: Analytical Methodrsmentioning

confidence: 99%

Purification and tissue distribution of a small protein (BM-40) extracted from a basement membrane tumor

et al. 1986

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A novel acidic glycoprotein, BM-40, with M , = 40000, was purified from the basement-membrane-producing mouse EHS tumor and characterized with regard to its unique chemical and antigenic properties. It was obtained from the tumor in a neutral salt-soluble form or as a component requiring extraction with 6M guanidine . HCI. This protein could also be identified in many other tissue extracts and cell and tissue cultures. The most intact form of BM-40 consists of a single polypeptide chain which undergoes limited proteolysis during extraction and purification. BM-40 exists in most tissues in stoichiometric amounts compared to other basement membrane proteins (laminin, nidogen) and is secreted by various teratocarcinoma and epithelial cells. It can be visualized by immunofluorescence in the extracellular matrix of the EHS tumor and Reichert's membrane. Other tissues which contain extractable BM-40 were negative in immunofluorescence.Basement membranes are characteristic extracellular matrices located in close vicinity to the cells and are considered to be highly integrated structures formed from a variety of different glycoproteins [l, 21. A major constituent is collagen IV which self-assembles into large networks [3,4] thus providing a scaffold to which several non-collagenous proteins may become attached. Most prominent among these proteins is laminin [5] which has the potential to bind to collagen IV, heparan sulfate proteoglycan and nidogen [6-91 and BM-40, which is present in the extracellular matrix of this tumor. MATERIALS AND METHODS Extraction and purification of protein BM-40EHS tumor tissue [21], obtained from about 150 C57BI mice, was washed with 3.4 M NaCl and extracted four times (4"C, 1 day) with 0.5 M NaC1,0.05 M Tris/HCl, pH 7.4, containing 20 mg/l of p-hydroxymercuribenzoate (OH-BzHgOH) and phenylmethanesulfonyl fluoride (PhMeS02F) as protease inhibitors [5]. The insoluble residue was dialyzed against water (6 h, 4"C), lyophilized and extracted in aliquots with 6 M guanidine . HC1 containing the protease inhibitors, 10 mM EDTA, 2 mM N-ethylmaleimide (MalNEt) and 2 mM PhMeS02F [9, 1 1 . The guanidine . HC1 extraction was repeated once and both supernatants were combined, dialyzed at 4°C against 7 M urea, 0.05 M Tris/HCl, pH 8.6, 2.5 mM EDTA, 0.5 mM MalNEt and 0.5 mM PhMeS02F [17] and passed over a DEAE-cellulose column (2.5 x 25 cm) equilibrated in the same buffer. The column was eluted with a linear gradient of 0-0.6 M NaCl (1200 ml) and the position of components detected by electrophoresis or radioimmunoassays. Rechromatography of BM-40 on CM-cellulose in 7 M urea and on Sephacryl S-300 in 6 M guanidine . HCl followed previously used procedures [17].Purified preparations were concentrated by ultrafiltration (Amicon filter PMlO), dialyzed against 1 M ammonium bicarbonate, pH 7.9 (without protease inhibitors) and stored at -20°C. Complete reduction of BM-40, purified from the guanidine . HCl extract, was done by incubation for 5 h at 37°C in 6 M guanidine * HC1, 0.25 M ammonium bicarbonate, pH 7....

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“…Fibronectin ensures the adhesion of mesenchymal cells to interstitial collagens and to some proteoglycans (1)(2)(3)(4). Laminin is involved in the interaction between epithelial cells and basement membrane components, such as collagen type IV (5,6). Elastin was originally considered to be an isotropic and inert constituent, but physicochemical studies have pointed to a more dynamic structure and to possible interactions with other connective tissue proteins (7,8).…”

mentioning

confidence: 99%

Inducible adhesion of mesenchymal cells to elastic fibers: elastonectin.

Hornebeck¹,

Tixier²,

Robert³

1986

Proc. Natl. Acad. Sci. U.S.A.

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The addition of highly purified elastic fibers to confluent human skin fibroblast or porcine aorta smooth muscle cell cultures resulted in a time-dependent, strong adhesion of the fibrils to the cell surface. The kinetics of adhesion was studied by video/time-lapse cinematography. After a 0.5-1 hr lag period, adhesion progressed to a maximum amount in 3-6 hr in the described conditions. Adhesion is strongly accelerated by the prior addition of soluble elastin peptides (K-elastin) to the cultures. Cycloheximide inhibits this induced adhesion. Adherent elastic fibers can be detached by treatment with elastase and trypsin but not with collagenase. The radioactive proteins adhering to elastic fibers, after a 6-hr incubation of the induced cultures in presence of [35S]methionine, were extracted and analyzed by NaDodSO4/PAGE. The proteins strongly adhering to the elastic fibers had apparent molecular sizes of about 120, 67, 60, and 45 kDa. Only the 120-kDa protein band showed a significant increase of its associated radioactivity in the induced cultures as compared to the noninduced cultures. We propose that the 120-kDa protein is responsible for the induced adhesion of mesenchymal cells to elastic fibers and designate it "elastonectin."In the past years, specific adhesive proteins that mediate cell attachment to the extracellular matrix have been identified and characterized. Fibronectin ensures the adhesion of mesenchymal cells to interstitial collagens and to some proteoglycans (1-4). Laminin is involved in the interaction between epithelial cells and basement membrane components, such as collagen type IV (5, 6). Elastin was originally considered to be an isotropic and inert constituent, but physicochemical studies have pointed to a more dynamic structure and to possible interactions with other connective tissue proteins (7,8). Elastin peptides were also shown to be able to interact with several other cell types (9, 10). Mecham et al. (11) studied the acquisition of chemotactic responsiveness to elastin peptides and the expression of the elastin phenotype by fetal bovine ligamentum fibroblasts during cell differentiation and showed that they were closely related events. Therefore, the investigation of whether specific protein(s) could mediate the adhesion of mesenchymal cells to elastic fibers was undertaken.In the present report, we have investigated the interactions between purified bovine ligamentum nuchae elastic fibers and human skin fibroblasts or pig aorta smooth muscle cells in culture and show that elastic fibers adhere strongly to both cell types. Fibronectin has been shown not to be involved in this process. Biosynthetic experiments carried out with human skin fibroblasts cultured in presence or absence of elastic fibers enabled us to carry out preliminary identification of an inducible protein closely associated with the added elastic fibers. We have designated this adhesive protein "elastonectin."MATERIAL AND METHODS Fibroblasts and smooth muscle cells were obtained from human dermis and porci...

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Nidogen: a new, self‐aggregating basement membrane protein

Cited by 253 publications

References 37 publications

Accumulation of type IV collagen in dilated ER leads to apoptosis inHsp47-knockout mouse embryos via induction of CHOP

Accumulation of type IV collagen in dilated ER leads to apoptosis inHsp47-knockout mouse embryos via induction of CHOP

Purification and tissue distribution of a small protein (BM-40) extracted from a basement membrane tumor

Inducible adhesion of mesenchymal cells to elastic fibers: elastonectin.

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