Sequences within Fibrinogen and Intercellular Adhesion Molecule-1 (ICAM-1) Modulate Signals Required for Mitogenesis

Gardiner, Elizabeth E.; D’Souza, Stanley E.

doi:10.1074/jbc.274.17.11930

Cited by 31 publications

(42 citation statements)

References 42 publications

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“…We had earlier observed the tyrosine phosphorylation of proteins migrating at 70 kDa, upon Fg-ICAM-1 ligation in TNF␣-stimulated ECs and in B-lymphoid Raji cells (14,15). By immunoprecipitation of TNF␣-stimulated ECs, one of the proteins was identified as SHP-2 (Fig.…”

Section: The Adhesion Of Tnf␣-stimulated Ecs To Fg Results In Thementioning

confidence: 99%

“…The reduced association with SHP-2 in ICAM-1(Y485A) expressing cells results in the dampened activation of ERK-1/2, 2 which is likely to compromise the ability of the cell to survive. In this respect, we have noted the activation of ERK-1/2 as an important component in Fg-mediated Raji mitogenesis (14).…”

Section: Discussionmentioning

confidence: 99%

“…Aliquots of these peptides were also biotinylated. The peptides were purified on HPLC, and purity was confirmed by mass spectrometry and amino acid composition (10,13,14).…”

Section: Methodsmentioning

confidence: 99%

“…Moreover, ICAM-1 lacks the motifs resembling the Src homology domains (SH) that can recruit phosphorylated proteins at the cytoplasmic, membrane-proximal site (16). Nevertheless, Fg-ICAM-1 ligation in Raji B-cells results in proliferative signals that causes 2-3-fold increase in the phosphorylation of pp60Src and of the extracellular signal-regulated kinase (ERK) (13,14). However, the ligation of TNF␣-stimulated ECs to Fg results in a dramatic increase (8 -10-fold) in ERK phosphorylation, which is implicated in EC survival and in preventing TNF␣-mediated apoptosis (15).…”

mentioning

confidence: 99%

“…Src and of the extracellular signal-regulated kinase (ERK) (13,14). However, the ligation of TNF␣-stimulated ECs to Fg results in a dramatic increase (8 -10-fold) in ERK phosphorylation, which is implicated in EC survival and in preventing TNF␣-mediated apoptosis (15).…”

mentioning

confidence: 99%

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Src Homology Domain 2-containing Tyrosine Phosphatase 2 Associates with Intercellular Adhesion Molecule 1 to Regulate Cell Survival

Pluskota

Chen

D’Souza

2000

Journal of Biological Chemistry

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Intracellular adhesion molecule-1 (ICAM-1, also termed CD54)1 is a receptor expressed on diverse cell types and belongs to the Ig-like family of proteins. Endothelial cells (ECs) express very low amounts of ICAM-1 and require stimulation with cytokines tumor necrosis factor-␣ (TNF␣) or interleukin-1 to upregulate ICAM-1 levels (1-3). ICAM-1 functions as a costimulatory molecule on antigen-presenting cells to activate major histocompatability complex class II restricted T-cells and on other cell types in association with major histocompatability complex class I to activate cytotoxic T-cells. The recognition of ICAM-1 by ␤ 2 -integrins results in the adhesion of leukocytes to the endothelium and in the extravasation of leukocytes to sites of inflammation (3-5). The extravasation of leukocytes also occurs through a process involving ICAM-1 and the plasma protein fibrinogen (Fg). In this process, the integrin-bound Fg interacts with ICAM-1, mediating the bridging between blood cells and ECs (6 -9). TNF␣-stimulated ECs interact with Fg primarily through ICAM-1 (2, 10). A region within the first Ig-like motif of ICAM-1, ICAM-1-(8 -21), and a segment within the ␥-chain of Fg, Fg ␥-(117-133), participate in Fg-ICAM-1-mediated cellular bridging, cell survival, and proliferation (10 -15).The 28-amino acid cytoplasmic tail of ICAM-1 lacks the consensus sequence required for intrinsic kinase activity. Moreover, ICAM-1 lacks the motifs resembling the Src homology domains (SH) that can recruit phosphorylated proteins at the cytoplasmic, membrane-proximal site (16). Nevertheless, Fg-ICAM-1 ligation in Raji B-cells results in proliferative signals that causes 2-3-fold increase in the phosphorylation of pp60Src and of the extracellular signal-regulated kinase (ERK) (13,14). However, the ligation of TNF␣-stimulated ECs to Fg results in a dramatic increase (8 -10-fold) in ERK phosphorylation, which is implicated in EC survival and in preventing TNF␣-mediated apoptosis (15). In other studies, the ligation of ICAM-1 from EC derived from rat brain microvessels with ␤ 2 -integrins from activated T-cells resulted in the phosphorylation of a Src kinase substrate, cortactin (17). The activation of the small molecular weight GTPase Rho, following cross-linking of ECs with ICAM-1 antibodies, has been implicated in leukocyte transmigration (18,19). ICAM-1 cross-linking in Blymphoma and in T-cells activated the Src family kinase Lyn and inactivated Cdc2 kinase, respectively (20,21).The cytoplasmic sequence of several Ig-like receptors such as CD22 (22-24), CD33 (25), platelet endothelial cell adhesion molecule-1 (PECAM-1) (26,27), Fc␥RIIB (28,29), and the killer cell inhibitory receptor (30, 31) contain module(s) termed immune receptor tyrosine-binding inhibition motifs (ITIM). The ITIM consensus sequence (I/V/L)XYXX(L/V), when phosphorylated, associates with the Src homology 2 (SH2) domain-containing phosphatases SHP-1, SHP-2, and SHIP-1 (SH2-containing inositol polyphosphate 5-phosphatase). These cytosolic phosphatases down-regulate tyrosi...

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Section: The Adhesion Of Tnf␣-stimulated Ecs To Fg Results In Thementioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

“…Aliquots of these peptides were also biotinylated. The peptides were purified on HPLC, and purity was confirmed by mass spectrometry and amino acid composition (10,13,14).…”

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Src Homology Domain 2-containing Tyrosine Phosphatase 2 Associates with Intercellular Adhesion Molecule 1 to Regulate Cell Survival

Pluskota

Chen

D’Souza

2000

Journal of Biological Chemistry

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ICAM-1: A master regulator of cellular responses in inflammation, injury resolution, and tumorigenesis

Bui

Wiesolek

Sumagin

2020

Journal of Leukocyte Biology

601

318

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ICAM‐1 is a cell surface glycoprotein and an adhesion receptor that is best known for regulating leukocyte recruitment from circulation to sites of inflammation. However, in addition to vascular endothelial cells, ICAM‐1 expression is also robustly induced on epithelial and immune cells in response to inflammatory stimulation. Importantly, ICAM‐1 serves as a biosensor to transduce outside‐in‐signaling via association of its cytoplasmic domain with the actin cytoskeleton following ligand engagement of the extracellular domain. Thus, ICAM‐1 has emerged as a master regulator of many essential cellular functions both at the onset and at the resolution of pathologic conditions. Because the role of ICAM‐1 in driving inflammatory responses is well recognized, this review will mainly focus on newly emerging roles of ICAM‐1 in epithelial injury‐resolution responses, as well as immune cell effector function in inflammation and tumorigenesis. ICAM‐1 has been of clinical and therapeutic interest for some time now; however, several attempts at inhibiting its function to improve injury resolution have failed. Perhaps, better understanding of its beneficial roles in resolution of inflammation or its emerging function in tumorigenesis will spark new interest in revisiting the clinical value of ICAM‐1 as a potential therapeutic target.

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ICAM gene cluster SNPs and prostate cancer risk in African Americans

et al. 2006

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Intercellular adhesion molecules (ICAMs) are known to be involved in various human cancers. An ICAM gene cluster lying within a 26 kb region on chromosome 19p13.2, and containing ICAM1, ICAM4, and ICAM5 has recently been identified as harboring a breast and prostate cancer susceptibility locus in two populations of European ancestry from Germany and Australia. The objective of this study was to confirm the ICAM association with prostate cancer in a sample of African American prostate cancer cases (N = 286) and controls (N = 391). Six single nucleotide polymorphisms (SNPs) within the three ICAM genes were genotyped. To control for potential population stratification an ancestry-adjusted association analysis was performed. We found that ICAM1 SNPs, -9A/C (rs5490) and K469E (rs5498) were associated with prostate cancer risk in men with a family history of prostate cancer (P = 0.008). Specifically, increased risk was observed for individuals who possessed the CC genotype of the -9 A/C variant (odds ratio = 2.5; 95% CI = 1.0-6.3) and at least one G allele of non-synonymous K469E variant (odds ratio = 1.8; 95% CI = 1.2-3.1). Strong linkage disequilibrium was observed across the ICAM region (P < 0.001). A common haplotype within the ICAM gene cluster, harboring the -9A/C variant was significantly associated with prostate cancer (P = 0.03), mainly due to men with family history (P = 0.01). Our results replicate previous findings of association of the ICAM gene cluster with prostate cancer and suggest that common genetic variation within ICAM1 and not ICAM5 may be an important risk factor for prostate cancer.

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Sequences within Fibrinogen and Intercellular Adhesion Molecule-1 (ICAM-1) Modulate Signals Required for Mitogenesis

Cited by 31 publications

References 42 publications

Src Homology Domain 2-containing Tyrosine Phosphatase 2 Associates with Intercellular Adhesion Molecule 1 to Regulate Cell Survival

Src Homology Domain 2-containing Tyrosine Phosphatase 2 Associates with Intercellular Adhesion Molecule 1 to Regulate Cell Survival

ICAM-1: A master regulator of cellular responses in inflammation, injury resolution, and tumorigenesis

ICAM gene cluster SNPs and prostate cancer risk in African Americans

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