Integrins

Kleiman, Tovah A.; Mosher, Deane F.

doi:10.1002/0471203076.emm0656

Cited by 1 publication

(2 citation statements)

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“…The particular combination of α-and β-subunits determines the ligand specificity and function of the integrin (Giancotti and Ruoslahti, 1999;Hynes, 2002;Kleiman and Mosher, 2002). Therefore, we tried to identify an α-subunit of β 1 -integrin capable of binding to MK, using COS-7 cells and mouse 13-day embryos.…”

Section: Results β 1 -Integrin Binds To Mkmentioning

confidence: 99%

“…The ligands of α 4 β 1 -integrin are fibronectin, a major component of the ECM, and VCAM, a member of the immunoglobulin superfamily. α 4 β 1 -Integrin recognizes LDV in the alternatively spliced III CS domain of fibronectin (Guan and Hynes, 1990;Kleiman and Mosher, 2002). α 4 β 1 -Integrin plays important roles in cell migrationit governs lymphocyte migration (Rose et al, 2001), is involved in recruitment of neutrophils to inflammatory sites (Burns et al, 2001;Henderson et al, 2001) and is essential for the migration of epicardial progenitor cells to the surface of the heart to form the epicardium (Sengbusch et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

α4β1- and α6β1-integrins are functional receptors for midkine, a heparin-binding growth factor

Muramatsu

Zou

Suzuki

et al. 2004

Journal of Cell Science

108

110

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Midkine is a heparin-binding growth factor that promotes the growth, survival, migration and differentiation of various target cells. So far, receptor-type protein tyrosine phosphatase ζ, low-density-lipoprotein-receptor-related protein and anaplastic lymphoma kinase have been identified as receptors for midkine. We found β1 integrin in midkine-binding proteins from 13-day-old mouse embryos. β1-Integrin bound to a midkine-agarose column and was eluted mostly with EDTA. Further study revealed that the α-subunits capable of binding to midkine were α4 and α6. Purified α4β1- and α6β1-integrins bound midkine. Anti-α4 antibody inhibited the midkine-dependent migration of osteoblastic cells, and anti-α6 antibody inhibited the midkine-dependent neurite outgrowth of embryonic neurons. After midkine treatment, tyrosine phosphorylation of paxillin, an integrin-associated molecule, was transiently increased in osteoblastic cells. Therefore, we concluded that α4β1- and α6β1-integrins are functional receptors for midkine. We observed that the low-density-lipoprotein-receptor-related-protein-6 ectodomain was immunoprecipitated with α6β1-integrin and α4β1-integrin. The low-density-lipoprotein-receptor-related-protein-6 ectodomain was also immunoprecipitated with receptor-type protein tyrosine phosphatase ζ. α4β1- and α6β1-Integrins are expected to co-operate with other midkine receptors, possibly in a multimolecular complex that contains other midkine receptors.

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Section: Results β 1 -Integrin Binds To Mkmentioning

confidence: 99%