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Human B lymphocytes define an alternative mechanism of adhesion to fibronectin. The interaction of the alpha 4 beta 1 integrin with the LHGPEILDVPST sequence of the type III connecting segment is sufficient to promote cell attachment.
J Immunol. 1990 May 01; 144(9):3361-6.JI

Abstract

In this report we have studied the mechanism of human B lymphocyte adhesion to fibronectin and to proteolytic fragments of this protein. B cells adhered to fibronectin and to a 38-kDa fragment, derived from the A chain, containing the Hep II domain and most of the type III connecting segment, IIICS, of fibronectin. Cells did not bind to an 80-kDa fragment containing the RGD adhesive sequence of fibronectin. Attachment to fibronectin or to the 38-kDa fragment was not affected by the 80-kDa fragment, the GRGDSPC synthetic peptide, or by a mAb specific for the alpha chain of the RGD-dependent fibronectin receptor, alpha 5 beta 1. However, B cell adhesion to fibronectin was inhibited by the synthetic peptides CS-1, comprising the first 25 amino acids of IIICS and B12, containing the sequence LHGPEILDVPST of CS-1 (residues 14-25). Moreover, this sequence was shown to be sufficient to induce stable cell adhesion when coated on plastic surfaces. A mAb specific for the alpha-subunit of the alpha 4 beta 1 integrin, completely inhibited B cell attachment to B12, CS-1, 38 kDa, and fibronectin coated substrata. These data clearly indicate that adhesion of B lymphocytes to fibronectin is exclusively mediated by the interaction of alpha 4 beta 1 with residues 14-25 of the IIICS region in fibronectin. Therefore this interaction constitutes an alternative pathway of adhesion to fibronectin, independent of RGD and alpha 5 beta 1.

Authors+Show Affiliations

Mononuclear Cell Biology, New York Blood Center, NY 10021.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

2139453

Citation

Garcia-Pardo, A, et al. "Human B Lymphocytes Define an Alternative Mechanism of Adhesion to Fibronectin. the Interaction of the Alpha 4 Beta 1 Integrin With the LHGPEILDVPST Sequence of the Type III Connecting Segment Is Sufficient to Promote Cell Attachment." Journal of Immunology (Baltimore, Md. : 1950), vol. 144, no. 9, 1990, pp. 3361-6.
Garcia-Pardo A, Wayner EA, Carter WG, et al. Human B lymphocytes define an alternative mechanism of adhesion to fibronectin. The interaction of the alpha 4 beta 1 integrin with the LHGPEILDVPST sequence of the type III connecting segment is sufficient to promote cell attachment. J Immunol. 1990;144(9):3361-6.
Garcia-Pardo, A., Wayner, E. A., Carter, W. G., & Ferreira, O. C. (1990). Human B lymphocytes define an alternative mechanism of adhesion to fibronectin. The interaction of the alpha 4 beta 1 integrin with the LHGPEILDVPST sequence of the type III connecting segment is sufficient to promote cell attachment. Journal of Immunology (Baltimore, Md. : 1950), 144(9), 3361-6.
Garcia-Pardo A, et al. Human B Lymphocytes Define an Alternative Mechanism of Adhesion to Fibronectin. the Interaction of the Alpha 4 Beta 1 Integrin With the LHGPEILDVPST Sequence of the Type III Connecting Segment Is Sufficient to Promote Cell Attachment. J Immunol. 1990 May 1;144(9):3361-6. PubMed PMID: 2139453.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Human B lymphocytes define an alternative mechanism of adhesion to fibronectin. The interaction of the alpha 4 beta 1 integrin with the LHGPEILDVPST sequence of the type III connecting segment is sufficient to promote cell attachment. AU - Garcia-Pardo,A, AU - Wayner,E A, AU - Carter,W G, AU - Ferreira,O C,Jr PY - 1990/5/1/pubmed PY - 2001/3/28/medline PY - 1990/5/1/entrez SP - 3361 EP - 6 JF - Journal of immunology (Baltimore, Md. : 1950) JO - J Immunol VL - 144 IS - 9 N2 - In this report we have studied the mechanism of human B lymphocyte adhesion to fibronectin and to proteolytic fragments of this protein. B cells adhered to fibronectin and to a 38-kDa fragment, derived from the A chain, containing the Hep II domain and most of the type III connecting segment, IIICS, of fibronectin. Cells did not bind to an 80-kDa fragment containing the RGD adhesive sequence of fibronectin. Attachment to fibronectin or to the 38-kDa fragment was not affected by the 80-kDa fragment, the GRGDSPC synthetic peptide, or by a mAb specific for the alpha chain of the RGD-dependent fibronectin receptor, alpha 5 beta 1. However, B cell adhesion to fibronectin was inhibited by the synthetic peptides CS-1, comprising the first 25 amino acids of IIICS and B12, containing the sequence LHGPEILDVPST of CS-1 (residues 14-25). Moreover, this sequence was shown to be sufficient to induce stable cell adhesion when coated on plastic surfaces. A mAb specific for the alpha-subunit of the alpha 4 beta 1 integrin, completely inhibited B cell attachment to B12, CS-1, 38 kDa, and fibronectin coated substrata. These data clearly indicate that adhesion of B lymphocytes to fibronectin is exclusively mediated by the interaction of alpha 4 beta 1 with residues 14-25 of the IIICS region in fibronectin. Therefore this interaction constitutes an alternative pathway of adhesion to fibronectin, independent of RGD and alpha 5 beta 1. SN - 0022-1767 UR - https://www.unboundmedicine.com/medline/citation/2139453/Human_B_lymphocytes_define_an_alternative_mechanism_of_adhesion_to_fibronectin__The_interaction_of_the_alpha_4_beta_1_integrin_with_the_LHGPEILDVPST_sequence_of_the_type_III_connecting_segment_is_sufficient_to_promote_cell_attachment_ L2 - https://www.jimmunol.org/lookup/pmidlookup?view=long&pmid=2139453 DB - PRIME DP - Unbound Medicine ER -