The Leukocyte Integrins

Harris, Estelle S.; McIntyre, Thomas M.; Prescott, Stephen M.; Zimmerman, Guy A.

doi:10.1074/jbc.r000004200

Cited by 300 publications

(268 citation statements)

References 85 publications

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“…Ln-1 has been shown to bind to several integrins (␣ 1 ␤ 1 , (59,60). Although the identity of the receptor remains to be determined, preliminary data suggest that the laminin ␣1 and ␣5 peptides use the same receptor for chemotaxis (data not shown).…”

Section: Discussionmentioning

confidence: 98%

A Site on Laminin α5, AQARSAASKVKVSMKF, Induces Inflammatory Cell Production of Matrix Metalloproteinase-9 and Chemotaxis

Adair-Kirk

Atkinson

Broekelmann

et al. 2003

The Journal of Immunology

102

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Several peptide sequences in laminin α1, the α-chain of laminin (Ln)-1, mediate biological responses in vitro, but Ln-1 is rare in vivo. Since Ln-5 and Ln-10, which contain the α3 and α5 chains, respectively, are the most prominent laminin heterotrimers in normal adult tissues and few functional domains in other laminin chains have been identified, we are investigating the α3 and α5 chains for biological activities. Incubation of mouse macrophages with the laminin α5 peptide AQARSAASKVKVSMKF resulted in marked increase in matrix metalloproteinase (MMP)-9 mRNA and gelatinolytic activity in the conditioned media, whereas the corresponding α3 peptide QQARDAANKVAIPMRF had no effect. AQARSAASKVKVSMKF also induced expression of MMP-14, while MMP-2, MMP-3, MMP-7, MMP-12, and MMP-13 were not induced by this peptide. Deletion analyses indicated that a minimal sequence of ASKVKVSMKF was sufficient for increasing MMP-9 expression. AQARSAASKVKVSMKF was also chemotactic for neutrophils and macrophages in vitro, and induced accumulation of neutrophils and macrophages in lung airspaces in vivo following intranasal instillation into mice. Comparable accumulation occurred in MMP-9-deficient mice, indicating that MMP-9 was not required for AQARSAASKVKVSMKF-induced inflammatory cell emigration in the lung. A scrambled version of the minimal peptide, KAKSFVMVSK, was inactive. These data indicate that laminin α5-derived peptides can induce inflammatory cell chemotaxis and metalloproteinase activity.

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Section: Discussionmentioning

confidence: 98%

A Site on Laminin α5, AQARSAASKVKVSMKF, Induces Inflammatory Cell Production of Matrix Metalloproteinase-9 and Chemotaxis

Adair-Kirk

Atkinson

Broekelmann

et al. 2003

The Journal of Immunology

102

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“…Neutrophils express predominantly b 2 -integrins, but also low amounts of b 1 -and b 3 -integrins. Monocytes express b 1 -and b 2 -integins, whereas lymphocytes possess a pattern of b 1 -, b 2 -, and b 7 -integrins varying with subtype and state of activation (9). We focus in this review on b 2 -integrins and a 4 b 1 , as these are the predominant molecules mediating interactions with the endothelium.…”

Section: Integrin Physiognomymentioning

confidence: 99%

Integrin Regulation during Leukocyte Recruitment

Herter

Zarbock

2013

The Journal of Immunology

168

138

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Integrins are recognized as vital players in leukocyte recruitment. Integrin malfunction causes severe disease patterns characterized by the inability to fight pathogens. Although inflammatory reactions are beneficial and necessary for host defense, these reactions have to be controlled to prevent tissue destruction and harmful sequelae. In this review, we discuss the different signaling pathways leading to the change of integrin adhesiveness in neutrophils, monocytes, and lymphocytes. We thereby focus on the importance of integrin activation for the different steps of the leukocyte recruitment cascade, including rolling, adhesion, postadhesion strengthening, intravascular crawling, and transmigration, as each step necessitates the proper functioning of a distinct set of integrin molecules that has to be activated specifically. Additionally, we discuss endogenous mechanisms that balance and counteract integrin activation and limit leukocyte recruitment at the site of inflammation. Further insight into these complex mechanisms may provide new approaches for developing new anti-inflammatory therapies.

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“…[12][13][14][15][16] The b 2 integrins are heterodimeric proteins that consist of a common beta subunit (CD18) noncovalently attached to different alpha subunits (CD11a-d). 17 The b 2 integrin family, or CD18 integrins, consists of four different adhesion proteins LFA-1 (CD11a/CD18), Mac-1 (CD11b/ CD18), p150/95 (CD11c/CD18), and CD11d/CD18. Importantly, expression of the b 2 integrins is limited to leukocytes, which indicates their importance for immune responses.…”

Section: Inflammatory Bowel Diseases (Ibd) Includingmentioning

confidence: 99%