A murine tumor producing a matrix of basement membrane.

Orkin, Roslyn W.; Gehron, P; McGoodwin, Ermona B.; Martin, George R.; Valentine, T; Swarm, Richard L.

doi:10.1084/jem.145.1.204

Cited by 559 publications

(239 citation statements)

References 44 publications

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“…It contains numerous structural proteins and growth factors that can impact cell biology assays (16)(17)(18). As published assays of CD271-associated melanoma tumorigenesis used different commercially available preparations of Matrigel [standard (5,6) or high concentration (HC; ref.…”

Section: Effects Of Matrigel Formulation On Pdx Tumor Formation Frommentioning

confidence: 99%

CD271 Expression on Patient Melanoma Cells Is Unstable and Unlinked to Tumorigenicity

et al. 2016

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The stability of markers that identify cancer cells that propagate disease is important to the outcomes of targeted therapy strategies. In human melanoma, conflicting data exist as to whether hierarchical expression of CD271/p75/NGFR (nerve growth factor receptor) marks cells with enriched tumorigenicity, which would compel their specific targeting in therapy. To test whether these discrepancies relate to differences among groups in assay approaches, we undertook side-by-side testing of published methods of patient-derived melanoma xenografting (

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Section: Effects Of Matrigel Formulation On Pdx Tumor Formation Frommentioning

confidence: 99%

CD271 Expression on Patient Melanoma Cells Is Unstable and Unlinked to Tumorigenicity

et al. 2016

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“…19 Matrigel, produced by Engelbreth-Holm-Swarm mouse sarcoma cells 20 has been used as a model basement membrane-like extracellular matrix in many studies (eg [21][22][23] ). Therefore, we tested whether neoepitopes recognized by anti-Pg RIBS mAbs were also exposed in Glu-Pg when bound to Matrigel.…”

Section: Org Frommentioning

confidence: 99%

Monoclonal antibodies detect receptor-induced binding sites in Glu-plasminogen

Han¹,

Baik²,

Kim³

et al. 2011

Blood

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When Glu-plasminogen binds to cells, its activation to plasmin is markedly enhanced compared with the reaction in solution, suggesting that Glu-plasminogen on cell surfaces adopts a conformation distinct from that in solution. However, direct evidence for such conformational changes has not been obtained. Therefore, we developed anti-plasminogen mAbs to test the hypothesis that Gluplasminogen undergoes conformational changes on its interaction with cells. Six anti-plasminogen mAbs (recognizing 3 distinct epitopes) that preferentially recognized receptor-induced binding sites (RIBS) in Glu-plasminogen were obtained. The mAbs also preferentially recognized Glu-plasminogen bound to the C-terminal peptide of the plasminogen receptor, Plg-R KT , and to fibrin, plasmin-treated fibrinogen, and Matrigel. We used trypsin proteolysis, immunoaffinity chromatography, and tandem mass spectrometry and

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“…The source of type IV collagen was the Engelbreth-Holm-Swarn (EHS) tumor (16) grown subcutaneously in mice which were rendered lathyritic by the addition of 0.25 % I~-aminopropionitrile fumarate (Sigma Chemical Co., St. Louis, MO) in their drinking water. Type IV collagen was isolated by a modification of previously described methods (4,12).…”

Section: Preparation Of L~pe I V Collagenmentioning

confidence: 99%

The role of the main noncollagenous domain (NC1) in type IV collagen self-assembly.

Tsilibary¹,

Charonis²

1986

The Journal of Cell Biology

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Abstract. Type IV collagen incubated at elevated temperatures in physiologic buffers self-associates (a) via its carboxy-terminal (NC1) domain, (b) via its aminoterminal (7S) domain, and (c) laterally; and it forms a network. When examined with the technique of rotary shadowing, isolated domain NC1 was found to bind along the length of type IV collagen to four distinct sites located at intervals of •100 nm each. The same 100-nm distance was observed in domain NC1 of intact type IV collagen bound along the length of the collagen molecules during initial steps of network formation and in complete networks. The presence of anti-NC1 Fab fragments in type IV collagen solutions inhibited lateral association and network formation in rotary shadow images. During the process of selfassociation type IV collagen develops turbidity; addition of isolated domain NC1 inhibited the development of turbidity in a concentration-dependent manner. These findings indicate that domain NC1 of type IV collagen plays an important role in the process of selfassociation and suggest that alterations in the structure of NC1 may be partially responsible for impaired functions of basement membranes in certain pathological conditions. T YPE IV collagen is one of the exclusive macromolecular components of basement membranes (11). Structurally, it consists of three a-chains [tIl(IV)2-t12(IV)] and has in its monomeric form a molecular weight of 500,000 (1, 5). When compared to the a-chains of the other collagen types, the a-chains of type IV collagen are of higher molecular weight and contain along their length many short interruptions of the GIy-X-Y repeating unit (9, 18). Therefore, type IV collagen has multiple short non-triple-helical domains along its length and also has a large globular domain (NC1) l at its carboxy-terminal end (22).Type IV collagen molecules have the ability to selfassemble by interacting via their carboxy termini (NC1) (22), via their amino termini (7S) (22), and laterally (26). The end product of these interactions is a closed network, as visualized with the rotary shadowing technique (26). Pepsintreated type IV collagen molecules which lack their globular NC1 domain are not able to form networks (26). This observation suggested that the carboxy-terminal globule might play an important role in type IV collagen self-assembly. In this study, we present evidence that domain NC1 is critically involved in lateral association and network formation of type IV collagen.1. Abbreviation used in this paper: NC1, noncollagenous domain 1 (carboxy terminal) of type IV collagen. Materials and Methods Preparation of l~pe I V CollagenThe source of type IV collagen was the Engelbreth-Holm-Swarn (EHS) tumor (16) grown subcutaneously in mice which were rendered lathyritic by the addition of 0.25 % I~-aminopropionitrile fumarate (Sigma Chemical Co., St. Louis, MO) in their drinking water. Type IV collagen was isolated by a modification of previously described methods (4, 12). Briefly, the tissue was extracted first with 3.4 M NaCI in 0.05 M ...

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A murine tumor producing a matrix of basement membrane.

Cited by 559 publications

References 44 publications

CD271 Expression on Patient Melanoma Cells Is Unstable and Unlinked to Tumorigenicity

CD271 Expression on Patient Melanoma Cells Is Unstable and Unlinked to Tumorigenicity

Monoclonal antibodies detect receptor-induced binding sites in Glu-plasminogen

The role of the main noncollagenous domain (NC1) in type IV collagen self-assembly.

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