Role of multiple β1 integrins in cell adhesion to the disintegrin domains of ADAMs 2 and 3

Tomczuk, Monika; Takahashi, Yûji; Huang, Jing; Murase, Shin; Mistretta, Marie; Klaffky, Erin J.; Sutherland, Ann; Bolling, Laura; Coonrod, Scott A.; Marcinkiewicz, Cezary; Sheppard, Dean; Stepp, Mary Ann; White, Judith M.

doi:10.1016/s0014-4827(03)00307-0

Cited by 49 publications

(43 citation statements)

References 58 publications

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“…Specific residues in the ␤ 1 subunit are required for invasin binding (55). The disintegrin domains of ADAMs-2 and -3 were also shown to have broad binding specificity for ␤ 1 integrins (56). Finally, cell adhesion to several fibronectin type 3 repeats that lack the RGD sequence could be stimulated by TS2/16 or by PMA and was sensitive to ␤ 1 blocking antibodies but not to any ␣-specific blocking antibodies tested (57).…”

Section: Discussionmentioning

confidence: 98%

Identification of Novel β1 Integrin Binding Sites in the Type 1 and Type 2 Repeats of Thrombospondin-1

Calzada

Annis

Zeng

et al. 2004

Journal of Biological Chemistry

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In addition to the three known ␤ 1 integrin recognition sites in the N-module of thrombospondin-1 (TSP1), we found that ␤ 1 integrins mediate cell adhesion to the type 1 and type 2 repeats. The type 1 repeats of TSP1 differ from typical integrin ligands in that recognition is pan-␤ 1 -specific. Adhesion of cells that express one dominant ␤ 1 integrin on immobilized type 1 repeats is specifically inhibited by antagonists of that integrin, whereas adhesion of cells that express several ␤ 1 integrins is partially inhibited by each ␣-subunit-specific antagonist and completely inhibited by combining the antagonists. ␤ 1 integrins recognize both the second and third type 1 repeats, and each type 1 repeat shows pan-␤ 1 specificity and divalent cation dependence for promoting cell adhesion. Adhesion to the type 2 repeats is less sensitive to ␣-subunit antagonists, but a ␤ 1 blocking antibody and two disintegrins inhibit adhesion to immobilized type 2 repeats. ␤ 1 integrin expression is necessary for cell adhesion to the type 1 or type 2 repeats, and ␤ 1 integrins bind in a divalent cation-dependent manner to a type 1 repeat affinity column. The widely used TSP1 function blocking antibody A4.1 binds to a site in the third type 2 repeat. A4.1 proximally inhibits ␤ 1 integrin-dependent adhesion to the type 2 repeats and indirectly inhibits integrin-dependent adhesion mediated by the TSP1 type 1 repeats. Although antibody A4

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Section: Discussionmentioning

confidence: 98%

Identification of Novel β1 Integrin Binding Sites in the Type 1 and Type 2 Repeats of Thrombospondin-1

Calzada

Annis

Zeng

et al. 2004

Journal of Biological Chemistry

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“…This integrin has been shown to interact with a wide variety of ligands, including the endothelial counter receptor VCAM-1 (36), tenascin C (37), osteopontin (38,39), cellular fibronectin (40), several members of the a disintegrin and metalloprotease (ADAM) family (41)(42)(43), coagulation factor XIII (44), tissue transglumatinase (44), VEGFA (45, 46), VEGFC and VEGFD (47), and von Willebrand factor (44). Our current findings suggest that integrin α 9 β 1 ligation is required for inhibition of airway smooth muscle contraction, since blocking antibody that inhibits interactions with ligands was as effective as KO or knockdown of the integrin in enhancing airway smooth muscle contraction.…”

Section: Discussionmentioning

confidence: 99%

Integrin α9β1 in airway smooth muscle suppresses exaggerated airway narrowing

Chen¹,

Kudo²,

Rutaganira³

et al. 2012

J. Clin. Invest.

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Exaggerated contraction of airway smooth muscle is the major cause of symptoms in asthma, but the mechanisms that prevent exaggerated contraction are incompletely understood. Here, we showed that integrin α 9 β 1 on airway smooth muscle localizes the polyamine catabolizing enzyme spermidine/spermine N 1 -acetyltransferase (SSAT) in close proximity to the lipid kinase PIP5K1γ. As PIP5K1γ is the major source of PIP2 in airway smooth muscle and its activity is regulated by higher-order polyamines, this interaction inhibited IP3-dependent airway smooth muscle contraction. Mice lacking integrin α 9 β 1 in smooth muscle had increased airway responsiveness in vivo, and loss or inhibition of integrin α 9 β 1 increased in vitro airway narrowing and airway smooth muscle contraction in murine and human airways. Contraction was enhanced in control airways by the higher-order polyamine spermine or by cell-permeable PIP2, but these interventions had no effect on airways lacking integrin α 9 β 1 or treated with integrin α 9 β 1 -blocking antibodies. Enhancement of SSAT activity or knockdown of PIP5K1γ inhibited airway contraction, but only in the presence of functional integrin α 9 β 1 . Therefore, integrin α 9 β 1 appears to serve as a brake on airway smooth muscle contraction by recruiting SSAT, which facilitates local catabolism of polyamines and thereby inhibits PIP5K1γ. Targeting key components of this pathway could thus lead to new treatment strategies for asthma.

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“…These data could not, however, completely exclude a role for the integrin ␣6␤1. This integrin has been suggested to mediate the binding of fertilin ␤ (ADAM 2) and cyritestin (ADAM 3), two members of the ADAM family (A Disintegrin And Metalloprotease) expressed on sperm Chen and Sampson, 1999;Takahashi et al, 2001;Tomczuk et al, 2003), but others have concluded that fertilin ␤ interacts with an alternate, but as yet unidentified, ␤1 integrin on the egg (Evans et al, 1997;Zhu and Evans, 2002).…”

Section: Introductionmentioning

confidence: 99%

CD9 controls the formation of clusters that contain tetraspanins and the integrin α6β1, which are involved in human and mouse gamete fusion

Ziyyat

Rubinstein

Monier-Gavelle

et al. 2006

Journal of Cell Science

121

109

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Role of multiple β1 integrins in cell adhesion to the disintegrin domains of ADAMs 2 and 3

Cited by 49 publications

References 58 publications

Identification of Novel β1 Integrin Binding Sites in the Type 1 and Type 2 Repeats of Thrombospondin-1

Identification of Novel β1 Integrin Binding Sites in the Type 1 and Type 2 Repeats of Thrombospondin-1

Integrin α9β1 in airway smooth muscle suppresses exaggerated airway narrowing

CD9 controls the formation of clusters that contain tetraspanins and the integrin α6β1, which are involved in human and mouse gamete fusion

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