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Alpha 4 beta 1 recognition of the Hep II domain of fibronectin is constitutive on some hemopoietic cells but requires activation on others [corrected].
J Immunol. 1993 Apr 15; 150(8 Pt 1):3506-14.JI

Abstract

Leukocyte adhesion to the carboxyl-terminal region of fibronectin, a major component of extracellular matrices, involves recognition of the CS-1 site and the Hep II domain. We have previously shown that cultured T and B lymphoid cells constitutively attach via the alpha 4 beta 1 integrin to a 38-kDa fibronectin fragment that contains CS-1 and Hep II, and to a 58-kDa fragment that contains Hep II only. In this report we have studied the adhesion of other hemopoietic cells to the CS-1 and Hep II regions of fibronectin. Cultured monocytic cells and peripheral blood T lymphocytes constitutively bound to the 38-kDa fragment indicating that alpha 4 beta 1 was functional. These cells, however, were unable to bind to the 58-kDa fragment. On lymphoid cells both fragments were shown to bind to very close regions of alpha 4 beta 1 as indicated by the inhibition pattern of mAb to various alpha 4 epitopes, and by the good inhibitory capacity of soluble 38-kDa fragment on cell adhesion to 58-kDa fragment. These results suggested that alpha 4 beta 1 is present on certain cell populations as a partially active form able to recognize the "high affinity" ligand CS-1 but not the "low affinity" ligand Hep II. Binding of monocytic cells and peripheral blood T lymphocytes to the Hep II domain could be induced by several agents: first, long (48-h) and short (20-min) treatment with phorbol esters; second, cell incubation with the divalent cation Mn2+; third, and most effective, cell incubation with the mAb TS2/16, which is directed to the beta 1 integrin subunit. Binding to the 58-kDa fragment in all three cases was completely inhibited by mAb anti-alpha 4, thus confirming the involvement of alpha 4 beta 1 in the recognition of the Hep II domain. No major changes on alpha 4 beta 1 surface expression were observed after these treatments as determined by immunofluorescence analyses. Our results indicate that hemopoietic cells may differentially bind the CS-1 and Hep II ligands in fibronectin depending on the activation state of alpha 4 beta 1, a fact that may be relevant for the migration and function of leukocytes.

Authors+Show Affiliations

Unidad de Inmunología, Centro de Investigaciones Biológicas, CSIC, Madrid, Spain.No affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

8280202

Citation

Sánchez-Aparicio, P, et al. "Alpha 4 Beta 1 Recognition of the Hep II Domain of Fibronectin Is Constitutive On some Hemopoietic Cells but Requires Activation On Others [corrected]." Journal of Immunology (Baltimore, Md. : 1950), vol. 150, no. 8 Pt 1, 1993, pp. 3506-14.
Sánchez-Aparicio P, Ferreira Júnior OC, Garcia-Pardo A. Alpha 4 beta 1 recognition of the Hep II domain of fibronectin is constitutive on some hemopoietic cells but requires activation on others [corrected]. J Immunol. 1993;150(8 Pt 1):3506-14.
Sánchez-Aparicio, P., Ferreira Júnior, O. C., & Garcia-Pardo, A. (1993). Alpha 4 beta 1 recognition of the Hep II domain of fibronectin is constitutive on some hemopoietic cells but requires activation on others [corrected]. Journal of Immunology (Baltimore, Md. : 1950), 150(8 Pt 1), 3506-14.
Sánchez-Aparicio P, Ferreira Júnior OC, Garcia-Pardo A. Alpha 4 Beta 1 Recognition of the Hep II Domain of Fibronectin Is Constitutive On some Hemopoietic Cells but Requires Activation On Others [corrected]. J Immunol. 1993 Apr 15;150(8 Pt 1):3506-14. PubMed PMID: 8280202.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Alpha 4 beta 1 recognition of the Hep II domain of fibronectin is constitutive on some hemopoietic cells but requires activation on others [corrected]. AU - Sánchez-Aparicio,P, AU - Ferreira Júnior,O C, AU - Garcia-Pardo,A, PY - 1993/4/15/pubmed PY - 1993/4/15/medline PY - 1993/4/15/entrez SP - 3506 EP - 14 JF - Journal of immunology (Baltimore, Md. : 1950) JO - J Immunol VL - 150 IS - 8 Pt 1 N2 - Leukocyte adhesion to the carboxyl-terminal region of fibronectin, a major component of extracellular matrices, involves recognition of the CS-1 site and the Hep II domain. We have previously shown that cultured T and B lymphoid cells constitutively attach via the alpha 4 beta 1 integrin to a 38-kDa fibronectin fragment that contains CS-1 and Hep II, and to a 58-kDa fragment that contains Hep II only. In this report we have studied the adhesion of other hemopoietic cells to the CS-1 and Hep II regions of fibronectin. Cultured monocytic cells and peripheral blood T lymphocytes constitutively bound to the 38-kDa fragment indicating that alpha 4 beta 1 was functional. These cells, however, were unable to bind to the 58-kDa fragment. On lymphoid cells both fragments were shown to bind to very close regions of alpha 4 beta 1 as indicated by the inhibition pattern of mAb to various alpha 4 epitopes, and by the good inhibitory capacity of soluble 38-kDa fragment on cell adhesion to 58-kDa fragment. These results suggested that alpha 4 beta 1 is present on certain cell populations as a partially active form able to recognize the "high affinity" ligand CS-1 but not the "low affinity" ligand Hep II. Binding of monocytic cells and peripheral blood T lymphocytes to the Hep II domain could be induced by several agents: first, long (48-h) and short (20-min) treatment with phorbol esters; second, cell incubation with the divalent cation Mn2+; third, and most effective, cell incubation with the mAb TS2/16, which is directed to the beta 1 integrin subunit. Binding to the 58-kDa fragment in all three cases was completely inhibited by mAb anti-alpha 4, thus confirming the involvement of alpha 4 beta 1 in the recognition of the Hep II domain. No major changes on alpha 4 beta 1 surface expression were observed after these treatments as determined by immunofluorescence analyses. Our results indicate that hemopoietic cells may differentially bind the CS-1 and Hep II ligands in fibronectin depending on the activation state of alpha 4 beta 1, a fact that may be relevant for the migration and function of leukocytes. SN - 0022-1767 UR - https://www.unboundmedicine.com/medline/citation/8280202/Alpha_4_beta_1_recognition_of_the_Hep_II_domain_of_fibronectin_is_constitutive_on_some_hemopoietic_cells_but_requires_activation_on_others_[corrected]_ L2 - https://www.jimmunol.org/lookup/pmidlookup?view=long&pmid=8280202 DB - PRIME DP - Unbound Medicine ER -