A complex of platelet glycoproteins Ic and IIa identified by a rat monoclonal antibody.

Sonnenberg, A.; Janssen, Hans; Hogervorst, Frans B.L.; Calafat, Jero; Hilgers, J.

doi:10.1016/s0021-9258(18)61123-8

Cited by 293 publications

(56 citation statements)

References 39 publications

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“…In this way, cells cultured in Matrigel with Ha2/5 were indistinguishable from control samples. Similar observations were made upon inhibition of integrin α6 and assessment of YAP localisation (Figure S3B and C) (Sonnenberg et al, 1987).…”

Section: Resultssupporting

confidence: 81%

“…In this way, cells cultured in Matrigel with Ha2/5 were indistinguishable from control samples. Similar observations were made upon inhibition of integrin 6 and assessment of YAP localisation (Figure S3B and C) (Sonnenberg et al, 1987). Furthermore, upon genetic ablation of Itgb1, integrin 1-deficient cells were refractory to the effects of Matrigel (Raghavan et al, 2000).…”

Section: Integrin 1 Activity Is Required For Ecm-induced Icm Specificationsupporting

confidence: 80%

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ECM-integrin signalling instructs cellular position-sensing to pattern the early mouse embryo

Kim

Sorokin²,

Hiiragi

2021

Preprint

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Development entails patterned emergence of diverse cell types within the embryo. In mammals, cells positioned inside the embryo gives rise to the inner cell mass (ICM) that eventually forms the embryo proper. Yet the molecular basis of how these cells recognise their inside position to instruct their fate is unknown. Here we show that cells perceive their position through extracellular matrix (ECM) and integrin-mediated adhesion. Provision of ECM to isolated embryonic cells induces ICM specification and alters subsequent spatial arrangement between epiblast (EPI) and primitive endoderm (PrE) cells that emerge within the ICM. Notably, this effect is dependent on integrin β 1 activity and involves apical to basal conversion of cell polarity. We demonstrate that ECM-integrin activity is sufficient for inside positional signalling and it is required for proper sorting of EPI/PrE cells. Our findings thus highlight the significance of ECM-integrin adhesion in enabling position-sensing by cells to achieve tissue patterning.

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Section: Resultssupporting

confidence: 81%

Section: Integrin 1 Activity Is Required For Ecm-induced Icm Specificationsupporting

confidence: 80%

ECM-integrin signalling instructs cellular position-sensing to pattern the early mouse embryo

Kim

Sorokin²,

Hiiragi

2021

Preprint

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“…Old, New York, NY); 102DF5 to Int ␤ 1 -subunit (Ylänne and Virtanen 1989); and 3E1 to Int ␤ 4 -subunit (Chemicon; Temecula, CA). In double immunolabeling experiments, rat MAbs to Ln ␣ 2-chain (4H8-2; Schuler and Sorokin 1995) and to Int ␣ 6 -subunit (GoH3; Sonnenberg et al 1987; Chemicon) were used. Affinity-purified rabbit antibody (Tiger et al 1997; kindly provided by D. Gullberg, Uppsala, Sweden) was used to identify Ln ␣ 1-chain and tetramethylrhodamine isothiocyanate-coupled Ulex europaeus -I agglutinin (TRITC-UEA-I; Vector Laboratories, Burlingame, CA) was used to demonstrate endothelial cells (Holthöfer et al 1982).…”

Section: Antibodiesmentioning

confidence: 99%

Localization of Laminin α4-Chain in Developing and Adult Human Tissues

Petäjäniemi

Korhonen

Kortesmaa

et al. 2002

J Histochem Cytochem.

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S U M M A R YRecent studies suggest important functions for laminin-8 (Ln-8; ␣ 4 ␤ 1 ␥ 1) in vascular and blood cell biology, but its distribution in human tissues has remained elusive. We have raised a monoclonal antibody (MAb) FC10, and by enzyme-linked immunoassay (EIA) and Western blotting techniques we show that it recognizes the human Ln ␣ 4-chain. Immunoreactivity for the Ln ␣ 4-chain was localized in tissues of mesodermal origin, such as basement membranes (BMs) of endothelia, adipocytes, and skeletal, smooth, and cardiac muscle cells. In addition, the Ln ␣ 4-chain was found in regions of some epithelial BMs, including epidermis, salivary glands, pancreas, esophageal and gastric glands, intestinal crypts, and some renal medullary tubules. Developmental differences in the distribution of Ln ␣ 4-chain were detected in skeletal muscle, walls of vessels, and intestinal crypts. Ln ␣ 4-and Ln ␣ 2-chains co-localized in BMs of fetal skeletal muscle cells and in some epithelial BMs, e.g., in gastric glands and acini of pancreas. Cultured human pulmonary artery endothelial (HPAE) cells produced Ln ␣ 4-chain as M r 180,000 and 200,000 doublet and rapidly deposited it to the growth substratum. In cell-free extracellular matrices of human kidney and lung, Ln ␣ 4-chain was found as M r 180,000 protein.

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“…Expression of collagen VII was evaluated using monoclonal antibody (MoAb) LH7:2 (Cymbus Bioscience, Southampton, U.K.). Immunomapping of the epidermal basement membrane components was performed using the anti-laminin 5 MoAb GB3 (gift from G. Meneguzzi, INSERM U385, Nice, France) (Verrando et al, 1991); MoAb G0H3, directed against the α6 integrin subunit (gift from A. Sonnenberg, the Netherland Cancer Institute, Amsterdam, The Netherlands) (Sonnenberg et al, 1987); the anti-β4 integrin subunit MoAb 3E1 (Telios, San Diego, CA); MoAb HD121 and 1A8C, recognizing the hemidesmosomal proteins HD1 and BP180 (180 kDa bullous pemphigoid antigen, BPAG2), respectively (gift from K. Owaribe, Nagoya University, Nagoya, Japan) (Owaribe et al, 1991). The rabbit anti-serum to type IV collagen was purchased from Institut Pasteur (Lyon, France).…”

Section: Immunofluorescence Analysismentioning

confidence: 99%

Compound Heterozygosity for a Recessive Glycine Substitution and a Splice Site Mutation in the COL7A1 Gene Causes an Unusually Mild Form of Localized Recessive Dystrophic Epidermolysis Bullosa

Terracina

Posteraro

Schubert

et al. 1998

Journal of Investigative Dermatology

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Type VII collagen is the major component of anchoring fibrils, adhesion structures of stratified epithelia that span the basement membrane region and papillary dermis. Mutations in the gene COL7A1 encoding type VII collagen cause dystrophic epidermolysis bullosa, a clinically heterogeneous autosomal dominant or recessive blistering disorder of the skin and mucous membranes. In this report, we investigate three siblings affected by an unusually mild form of localized recessive dystrophic epidermolysis bullosa who were shown to be compound heterozygotes for novel mutations affecting COL7A1. The maternally inherited mutation is a G-->C transversion that converts a codon for glycine to a codon for arginine (G1347R). The paternal mutation is a neutral G-->A transition at the last base of exon 70(5820G-->A) that alters the correct splicing of COL7A1 pre-mRNA, giving rise to an aberrant mRNA carrying the in-frame skipping of exon 70 in addition to the full-length RNA transcript carrying the G-->A substitution. Consistent with the normal levels of COL7A1 mRNA transcripts detected by northern analysis, immunoblotting and immunofluorescence studies evidenced that the patient keratinocytes synthesize and secrete normal amounts of stable type VII collagen, which is correctly deposited at the dermal-epidermal junction. In addition, mutated type VII collagen molecules assemble to form numerous, normally shaped anchoring fibrils, as shown by electron microscopic examination. The combination of a recessive glycine substitution with a splice site mutation that permits partially correct splicing therefore leads to a normal expression of mutated type VII collagen molecules with marginally altered biologic activity, and to the extremely mild phenotype observed in our patients.

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A complex of platelet glycoproteins Ic and IIa identified by a rat monoclonal antibody.

Cited by 293 publications

References 39 publications

ECM-integrin signalling instructs cellular position-sensing to pattern the early mouse embryo

ECM-integrin signalling instructs cellular position-sensing to pattern the early mouse embryo

Localization of Laminin α4-Chain in Developing and Adult Human Tissues

Compound Heterozygosity for a Recessive Glycine Substitution and a Splice Site Mutation in the COL7A1 Gene Causes an Unusually Mild Form of Localized Recessive Dystrophic Epidermolysis Bullosa

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