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Differential induction of gelatinase B (MMP-9) and gelatinase A (MMP-2) in T lymphocytes upon alpha(4)beta(1)-mediated adhesion to VCAM-1 and the CS-1 peptide of fibronectin.
Exp Cell Res. 2000 Oct 10; 260(1):73-84.EC

Abstract

Integrin alpha(4)beta(1) on the surface of T lymphocytes interacts with vascular cell adhesion molecule-1 (VCAM-1) and fibronectin during migration of lymphocytes from the blood to sites of inflammation. Migrating lymphocytes actively modify their environment through a number of mechanisms including proteolysis of the extracellular matrix by matrix metalloproteinases (MMP) synthesized by the cells. In this study, expression of MMP upon alpha(4)beta(1)-mediated adhesion of leukocytes to two major ligands, the IIICS-1 domain of fibronectin and VCAM-1, has been examined. Adhesion of T lymphoblastoid Jurkat cells to the CS-1 peptide induced expression of mRNA for two MMPs, gelatinase A (MMP-2) and gelatinase B (MMP-9). As evaluated by relative RT-PCR and Northern blot analyses, the level of mRNA was upregulated about 4- to 5-fold for both MMPs compared to control cells maintained in suspension. With time, both enzymes were detected in conditioned media and inside the cells, and their identities were verified by Western blotting and gelatin zymography. Adhesion of Jurkat cells to the second major alpha(4)beta(1) ligand, VCAM-1, upregulated mRNA for MMP-2 (3.5-fold) and failed to induce expression of mRNA for MMP-9. Accordingly, only MMP-2 protein was detected in conditioned media of cells adherent to VCAM-1. Occupancy of alpha(4)beta(1) on the surface of suspended cells with soluble CS-1 peptide or VCAM-1 did not upregulate synthesis and release of MMPs. A similar pattern of induction of MMPs after adhesion to CS-1 and VCAM-1 was observed in T lymphocytes isolated from human blood. These results demonstrate that adhesion of T lymphocytes through alpha(4)beta(1) to different ligands, which bind to similar or overlapping sites in the integrin, induces intracellular events leading to distinct patterns of MMPs biosynthesis.

Authors+Show Affiliations

Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Lerner Research Institute of the Cleveland Clinic Foundation, Cleveland, Ohio 44195, USA.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

11010812

Citation

Yakubenko, V P., et al. "Differential Induction of Gelatinase B (MMP-9) and Gelatinase a (MMP-2) in T Lymphocytes Upon Alpha(4)beta(1)-mediated Adhesion to VCAM-1 and the CS-1 Peptide of Fibronectin." Experimental Cell Research, vol. 260, no. 1, 2000, pp. 73-84.
Yakubenko VP, Lobb RR, Plow EF, et al. Differential induction of gelatinase B (MMP-9) and gelatinase A (MMP-2) in T lymphocytes upon alpha(4)beta(1)-mediated adhesion to VCAM-1 and the CS-1 peptide of fibronectin. Exp Cell Res. 2000;260(1):73-84.
Yakubenko, V. P., Lobb, R. R., Plow, E. F., & Ugarova, T. P. (2000). Differential induction of gelatinase B (MMP-9) and gelatinase A (MMP-2) in T lymphocytes upon alpha(4)beta(1)-mediated adhesion to VCAM-1 and the CS-1 peptide of fibronectin. Experimental Cell Research, 260(1), 73-84.
Yakubenko VP, et al. Differential Induction of Gelatinase B (MMP-9) and Gelatinase a (MMP-2) in T Lymphocytes Upon Alpha(4)beta(1)-mediated Adhesion to VCAM-1 and the CS-1 Peptide of Fibronectin. Exp Cell Res. 2000 Oct 10;260(1):73-84. PubMed PMID: 11010812.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Differential induction of gelatinase B (MMP-9) and gelatinase A (MMP-2) in T lymphocytes upon alpha(4)beta(1)-mediated adhesion to VCAM-1 and the CS-1 peptide of fibronectin. AU - Yakubenko,V P, AU - Lobb,R R, AU - Plow,E F, AU - Ugarova,T P, PY - 2000/9/30/pubmed PY - 2001/2/28/medline PY - 2000/9/30/entrez SP - 73 EP - 84 JF - Experimental cell research JO - Exp Cell Res VL - 260 IS - 1 N2 - Integrin alpha(4)beta(1) on the surface of T lymphocytes interacts with vascular cell adhesion molecule-1 (VCAM-1) and fibronectin during migration of lymphocytes from the blood to sites of inflammation. Migrating lymphocytes actively modify their environment through a number of mechanisms including proteolysis of the extracellular matrix by matrix metalloproteinases (MMP) synthesized by the cells. In this study, expression of MMP upon alpha(4)beta(1)-mediated adhesion of leukocytes to two major ligands, the IIICS-1 domain of fibronectin and VCAM-1, has been examined. Adhesion of T lymphoblastoid Jurkat cells to the CS-1 peptide induced expression of mRNA for two MMPs, gelatinase A (MMP-2) and gelatinase B (MMP-9). As evaluated by relative RT-PCR and Northern blot analyses, the level of mRNA was upregulated about 4- to 5-fold for both MMPs compared to control cells maintained in suspension. With time, both enzymes were detected in conditioned media and inside the cells, and their identities were verified by Western blotting and gelatin zymography. Adhesion of Jurkat cells to the second major alpha(4)beta(1) ligand, VCAM-1, upregulated mRNA for MMP-2 (3.5-fold) and failed to induce expression of mRNA for MMP-9. Accordingly, only MMP-2 protein was detected in conditioned media of cells adherent to VCAM-1. Occupancy of alpha(4)beta(1) on the surface of suspended cells with soluble CS-1 peptide or VCAM-1 did not upregulate synthesis and release of MMPs. A similar pattern of induction of MMPs after adhesion to CS-1 and VCAM-1 was observed in T lymphocytes isolated from human blood. These results demonstrate that adhesion of T lymphocytes through alpha(4)beta(1) to different ligands, which bind to similar or overlapping sites in the integrin, induces intracellular events leading to distinct patterns of MMPs biosynthesis. SN - 0014-4827 UR - https://www.unboundmedicine.com/medline/citation/11010812/Differential_induction_of_gelatinase_B__MMP_9__and_gelatinase_A__MMP_2__in_T_lymphocytes_upon_alpha_4_beta_1__mediated_adhesion_to_VCAM_1_and_the_CS_1_peptide_of_fibronectin_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0014-4827(00)95002-X DB - PRIME DP - Unbound Medicine ER -