Two different laminin domains mediate the differentiation of human endothelial cells into capillary-like structures in vitro

Grant, Derrick S.; Tashiro, Kensuke; Seguí‐Real, Bartolomé; Yamada, Yoshihiko; Martin, George R.; Kleinman, Hynda K.

doi:10.1016/0092-8674(89)90945-8

Cited by 695 publications

(406 citation statements)

References 41 publications

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“…Proteolysis is a common mechanism in interacting protein systems but usually does not involve proteases such as pepsin working at acidic pH. Recent data ( [30,31] and our unpublished results) with endothelial cells interacting with laminin substrates at neutral pH show interference by RGD peptides suggesting that these cells may possess a functional activation mechanism. The elucidation of such mechanisms will be crucial in understanding the role of this cell adhesion reaction.…”

Section: Resultsmentioning

confidence: 74%

Identification of the Arg‐Gly‐Asp sequence in laminin A chain as a latent cell‐binding site being exposed in fragment P1

et al. 1990

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A single RGD-containing sequence present within an epidermal growth factor-like repeat of the short arms of laminin is shown by peptide inhibition to block integrin receptors recognizing a latent cell-binding site of laminin. Based on proteolysis data it is proposed that masking occurs by folding of the globular domain IVa over the cell-binding site in the adjacent rod-like structures of laminin A chain.Basement membrane; Cell attachment; Integrin; Proteolytic fragment; Synthetic peptide I~RODUCTIONFragment P 1 generated from laminin by pepsin treatment was the first domain of the protein shown to be involved in cellular interactions [1,2]. Various cells have been found which bind fragment Pl with high affinity (KD -l-4 nM) to an apparently homogenous class of receptors [3-51. It was later shown that this binding site is latent both within laminin and within a larger PI-related fragment produced by cleavage with elastase [6], The Pl fragment (about 200 kDa) comprises the inner rod-like structure of the short arms of laminin and contains some 28 EGF-like repeats contributed by the A, Bl and B2 chains of laminin [7-91. Its A chain segment also possesses the only RGD (ArgGly-Asp) sequence present in mouse laminin [9]. Similar sequences are involved in cell binding to several other proteins including fibronectin, vitronectin and collagens [lo]. Here, we show by peptide and antibody inhibition and by proteolytic inactivation that the laminin RGD sequence very likely corresponds to the latent cell-binding site identified previously [6], and is recognized by cellular receptors of the integrin family. EXPERIMENTALThe mouse EHS tumor laminin-nidogen complex ill] and its large tryptic fragment Tl (121 were prepared as previously described. Both Abbreviations: EGF, epidermal growth factor; EHS, EngelbrethHolm-Swarm tumor; HPLC, high performance liquid chromatography; TLCK, tosyl lysyl chloromethane components were cleaved in 0.1 M glycine-HCl, pH 1.9 with pepsin (24 h, 25"C, enzyme-substrate ratio 1:iOO) to generate fragment PI which was then purified on a molecular sieve fl2]. Some small peptides in the pepsin digest were bound to heparin-Sepharose (Pharmacia) equilibrated in 0.1 M NaCl, 0.05 M Tris-HCl, pH 7.4 and eluted with 0.5 M NaCl. This material was separated into 25 distinct peaks by reversed phase HPLC and individual peptides were identified by Edman degradation [13]. Trypsin inactivation of PI some synthetic peptides was performed at 37°C in 0.2 M NH4HCOa (enzyme-substrate ratio 1:lOO) and the reaction was stopped by adding TLCK. Laminin fragment Pl was also isolated from human placenta [14]. Human plasma fibronectin (Behringwerke) was further purified on haparin-Sepharose. Synthetic peptides GRGDS (Promega) and ROES (Peninsula) were from commercial sources. Other RGD-cont~~ng peptides (see fig. 1) were synthesized according to sequences of mouse [P] and human fl5] laminin A chain, mouse laminin Bl chain 1161 and mouse nidogen (171 and kindly suppiied by Drs J. Knolle, S. Henke (Hoechst AG) and W. Sttiber (Behri...

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Section: Resultsmentioning

confidence: 74%

Identification of the Arg‐Gly‐Asp sequence in laminin A chain as a latent cell‐binding site being exposed in fragment P1

et al. 1990

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“…Finally, the ability to produce a cytokine either in diffusible, cell surface-bound, or matrix-bound forms may give a cell some control over that cytokine's sphere of influence (Rathjen et al, 1990). Since matrix can present cytokines, and since binding of ceils to matrix proteins can both induce cytokines and synergize with them, it is possible that the apparent induction of cell differentiation by matrix proteins alone (Ingber and Folkman, 1989a,b;Grant et al, 1989) may sometimes result from the combined action of matrix proteins with cytokines acting in an autocrine or paracrine manner. Thus, combined control of cell function by matrix proteins and cytokines may be a widespread phenomenon.…”

Section: Resultsmentioning

confidence: 99%

Cytokines in context.

Nathan

Sporn

1991

The Journal of Cell Biology

771

283

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“…Regarding the decision between proliferation and differentiation (i.e., capillary formation), laminin and fibronectin appear to exert a n important function (Grant et al, 1989;Ingber, 1991). Experiments in vitro suggest that fibronectin leads to a flattening of the angioblast which eventually results in the entry into the S-phase of the cell cycle.…”

Section: The Influence Of the Grafting Sitementioning

confidence: 99%

Blood vessel formation in the avian limb bud involves angioblastic and angiotrophic growth

Brand‐Saberi

Seifert

Grim³

et al. 1995

Developmental Dynamics

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The vasculature of the avian limb bud takes its origin from the intersomitic vessels as can be shown by ink perfusion of the embryo. While the primitive vessels form a central network in the early limb bud, an area of about 100 p m in width from the ectoderm inward remains free from lumenized vessels. However, this subectodermal avascular zone contains isolated angioblasts, which can be demonstrated by confocal laser scanning microscopy in connection with QH-1-staining. QH-1-positive cells from the avascular zone are capable of giving rise to endothelial cells when grafted ectopically into a "permissive" environment such as the dorso-lateral paraxial mesoderm. Several grafting sites are compared regarding their permissiveness for capillary formation. In order to investigate the origin of the QH-1-positive angioblasts we carried out injections of DiI-Ac-LDL, which is specifically taken up by endothelial cells and macrophages, and found the lumenized vessels and a few isolated cells in the peripheral limb mesoderm stained. In double-labelling studies combining DiI-Ac-LDL and QH-1, it can be shown that there exists a pool of isolated angioblasts that are only QH-l-positive, but have not incorporated DiI-Ac-LDL. In contrast to the lumenized vessels in the core of the limb bud, we found that angioblasts in the avascular zone do not proliferate, as shown by proliferation studies applying the BrdU-method to semithin sections in connection with QH-l-labelled parallel sections. We conclude that the vascularization of the avian limb bud is achieved by a combination of angiotrophic growth (sprouting of vessels) and angioblastic growth (recruitment of angioblasts from the limb mesoderm).0 1995 Wiley-Liss, Inc.

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Two different laminin domains mediate the differentiation of human endothelial cells into capillary-like structures in vitro

Cited by 695 publications

References 41 publications

Identification of the Arg‐Gly‐Asp sequence in laminin A chain as a latent cell‐binding site being exposed in fragment P1

Identification of the Arg‐Gly‐Asp sequence in laminin A chain as a latent cell‐binding site being exposed in fragment P1

Cytokines in context.

Blood vessel formation in the avian limb bud involves angioblastic and angiotrophic growth

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