Sage Journals: Discover world-class research

Abstract

Extracellular matrix molecules are recognized by several integrin subtypes, making identification of cross-talk among different integrin subtypes difficult. Here, we evaluated the cross-talk of integrin subtypes using four different integrin-binding peptides (FIB1; integrin αvβ3/α5β1, A2G10; integrin α6β1, EF1zz; integrin α2β1, or 531; integrin α3β1) derived from extracellular matrix molecules. Various combinations of two different integrin-binding peptides were mixed and conjugated on a chitosan matrix at various molar ratios and were evaluated for cell attachment activity. FIB1/A2G10 (molar ratio 5:5; total 10 nmol/well)-chitosan matrix significantly enhanced cell attachment activity compared with sum of the cell attachment activity on FIB1 (5 nmol/well)-chitosan matrices and A2G10 (5 nmol/well)-chitosan matrices, respectively. However, none of the other peptides showed a significant activity change when they were mixed and conjugated on a chitosan matrix. We investigated the mechanisms of this enhancement. FIB1/A2G10 (8:2 or 6:4)-chitosan matrix increased the cell spreading, phosphorylation of focal adhesion kinase at Y397, and slightly decreased phosphorylation of caveolin-1 at Y14 in fibroblasts compared with FIB1-chitosan and A2G10-chitosan matrices. These results indicate that FIB1/A2G10 (8:2 or 6:4)-chitosan matrix synergistically enhances cell attachment, suggesting that integrins αvβ3/α5β1 and α6β1 are involved in a cross-talk and synergistically enhance cell attachment. These findings also suggest that the mixed peptide-chitosan matrix system can regulate the ratio of two different peptides and is useful for evaluating cellular functions through receptor-specific cross-talk. Further, FIB1/A2G10 (8:2 or 6:4)-chitosan matrix could be a useful material for tissue engineering.

Keywords

Extracellular matrix chitosan cross-talk integrin peptide scaffold cell adhesion

Get full access to this article

View all access options for this article.

References

Hynes

Integrins: bidirectional, allosteric signaling machines. Cell 2002; 110: 673–687.

Legate

Wickstrom

Fassler

Genetic and cell biological analysis of integrin outside-in signaling. Genes Dev 2009; 23: 397–418.

Berrier

Yamada

KM.

Cell-matrix adhesion. J Cell Physiol 2007; 213: 565–573.

Gonzalez

Bhattacharya

deHart

et al . Transdominant regulation of integrin function: mechanisms of crosstalk. Cell Signal 2010; 22: 578–583.

Nethe

Hordijk

PL.

A model for phospho-caveolin-1-driven turnover of focal adhesions. Cell Adhes Migr 2014; 5: 59–64.

Salanueva

Cerezo

Guadamillas

et al . Integrin regulation of caveolin function. J Cellular Mol Med 2007; 11: 969–980.

Porter

Hogg

Integrins take partners: cross-talk between integrins and other membrane receptors. Trends Cell Biol 1998; 8: 390–396.

Huveneers

Danen

Adhesion signaling – crosstalk between integrins, Src and Rho. J Cell Sci 2009; 122: 1059–1069.

Streuli

Akhtar

Signal co-operation between integrins and other receptor systems. Biochem J 2009; 418: 491–506.

10.

Brakebusch

Fassler

beta 1 integrin function in vivo: adhesion, migration and more. Cancer Metastasis Rev 2005; 24: 403–411.

11.

Yamada

Adhesive recognition sequences. J Biol Chem 1991; 266: 12809–12812.

12.

Sreejalekshmi

Nair

PD.

Biomimeticity in tissue engineering scaffolds through synthetic peptide modifications-altering chemistry for enhanced biological response. J Biomed Mater Res 2011; 96: 477–491.

13.

Kikkawa

Hozumi

Katagiri

et al . Laminin-111-derived peptides and cancer. Cell Adhes Migr 2013; 7: 150–256.

14.

Ruoslahti

Integrins as signaling molecules and targets for tumor therapy. Kidney Int 1997; 51: 1413–1417.

15.

Frith

Mills

Cooper-White

JJ.

Lateral spacing of adhesion peptides influences human mesenchymal stem cell behaviour. J Cell Sci 2012; 125: 317–327.

16.

Yamada

Hozumi

Nomizu

Construction and activity of a synthetic basement membrane with active laminin peptides and polysaccharides. Chem Eur J 2011; 17: 10500–10508.

17.

Yamada

Hozumi

Katagiri

et al . Laminin-111-derived peptide-hyaluronate hydrogels as a synthetic basement membrane. Biomaterials 2013; 34: 6539–6547.

18.

Hozumi

Nakamura

Hori

et al . Mixed fibronectin-derived peptides conjugated to a chitosan matrix effectively promotes biological activities through integrins, alpha4beta1, alpha5beta1, alphavbeta3, and Syndecan. Biores Open Access 2016; 5: 356–366.

19.

Hozumi

Fujimori

Katagiri

et al . Suppression of cell adhesion through specific integrin crosstalk on mixed peptide-polysaccharide matrices. Biomaterials 2015; 37: 73–81.

20.

Hozumi

Sasaki

Yamada

et al . Reconstitution of laminin-111 biological activity using multiple peptide coupled to chitosan scaffolds. Biomaterials 2012; 33: 4241–4250.

21.

Urushibata

Hozumi

Ishikawa

et al . Identification of biologically active sequences in the laminin alpha2 chain G domain. Arch Biochem Biophys 2010; 497: 43–54.

22.

Hozumi

Suzuki

Nielsen

et al . Laminin alpha1 chain LG4 module promotes cell attachment through syndecans and cell spreading through integrin alpha2beta1. J Biol Chem 2006; 281: 32929–32940.

23.

Hozumi

Yamagata

Otagiri

et al . Mixed peptide-chitosan membranes to mimic the biological activities of a multifunctional laminin alpha1 chain LG4 module. Biomaterials 2009; 30: 1596–1603.

24.

Yamada

Pankov

Cukierman

Dimensions and dynamics in integrin function. Braz J Med Biol Res 2003; 36: 959–966.

25.

Schiller

Hermann

M-R

Polleux

et al . β1- and αv-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments. Nat Cell Biol 2013; 15: 625–636.

26.

Gonzalez

Gonzales

Herron

et al . Complex interactions between the laminin alpha 4 subunit and integrins regulate endothelial cell behavior in vitro and angiogenesis in vivo. Proc Natl Acad Sci USA 2002; 99: 16075–16080.

27.

Kohno

Sorgente

Ishibashi

et al . Immunofluorescent studies of fibronectin and laminin in the human eye. Invest Ophthalmol Vis Sci 1987; 28: 506–514.

28.

Otis

Campbell

Payet

et al . Expression of extracellular matrix proteins and integrins in rat adrenal gland: importance for ACTH-associated functions. J Endocrinol 2007; 193: 331–347.

29.

Lukjanenko

Jung

Hegde

et al . Loss of fibronectin from the aged stem cell niche affects the regenerative capacity of skeletal muscle in mice. Nat Med 2016; 22: 897–905. 2016/07/05.

30.

Saiki

Makabe

Yoneda

et al . Inhibitory effect of fibronectin and its recombinant polypeptides on the adhesion of metastatic melanoma cells to laminin. Jpn J Cancer Res 1991; 82: 1112–1119.

31.

Goetz

Lajoie

Wiseman

et al . Caveolin-1 in tumor progression: the good, the bad and the ugly. Cancer Metastasis Rev 2008; 27: 715–735.

32.

Echarri

Del Pozo

MA.

Caveolae internalization regulates integrin-dependent signaling pathways. Cell Cycle 2006; 5: 2179–2182.

33.

Ortiz

Diaz

et al . Extracellular matrix-specific Caveolin-1 phosphorylation on tyrosine 14 is linked to augmented melanoma metastasis but not tumorigenesis. Oncotarget 2016; 7: 40571–40593.

34.

Echarri

Muriel

Pavon

et al . Caveolar domain organization and trafficking is regulated by Abl kinases and mDia1. J Cell Sci 2012; 125: 3097–3113.

Supplementary Material

Please find the following supplemental material available below.

For Open Access articles published under a Creative Commons License, all supplemental material carries the same license as the article it is associated with.

For non-Open Access articles published, all supplemental material carries a non-exclusive license, and permission requests for re-use of supplemental material or any part of supplemental material shall be sent directly to the copyright owner as specified in the copyright notice associated with the article.

0.09 MB

0.00 MB

Identification of specific integrin cross-talk for dermal fibroblast cell adhesion using a mixed peptide-chitosan matrix

Abstract

Keywords

Get full access to this article

References

Supplementary Material