Betulinic acid and oleanolic acid, natural pentacyclic triterpenoids, interfere with N-linked glycan modifications to intercellular adhesion molecule-1, but not its intracellular transport to the cell surface

2015 ◽  
Vol 767 ◽  
pp. 126-134 ◽  
Author(s):  
Reiko Hiramatsu ◽  
Sayuri Fukuhara ◽  
Satoshi Mitsuda ◽  
Tomonobu Yokomichi ◽  
Takao Kataoka
Keyword(s):  
Cell Surface ◽  
Oleanolic Acid ◽  
Adhesion Molecule ◽  
Betulinic Acid ◽  
Intracellular Transport ◽  
Intercellular Adhesion ◽  
Intercellular Adhesion Molecule ◽  
Intercellular Adhesion Molecule 1 ◽  
Pentacyclic Triterpenoids

scholarly journals Association of intercellular adhesion molecule-1 (ICAM-1) with actin-containing cytoskeleton and alpha-actinin.

1992 ◽  
Vol 118 (5) ◽  
pp. 1223-1234 ◽  
Author(s):  
O Carpén ◽  
P Pallai ◽  
D E Staunton ◽  
T A Springer
Keyword(s):  
Cell Surface ◽  
Adhesion Molecule ◽  
Intercellular Adhesion ◽  
Cytoskeletal Proteins ◽  
Surface Proteins ◽  
Intercellular Adhesion Molecule ◽  
Wild Type ◽  
Intercellular Adhesion Molecule 1 ◽  
Surface Distribution ◽  
Western Blots

We have studied the cytoskeletal association of intercellular adhesion molecule-1 (ICAM-1, CD54), an integral membrane protein that functions as a counterreceptor for leukocyte integrins (CD11/CD18). A linkage between ICAM-1 and cytoskeletal elements was suggested by studies showing a different ICAM-1 staining pattern for COS cells transfected with wild-type ICAM-1 or with an ICAM-1 construct that replaces the cytoplasmic and transmembrane domains of ICAM-1 with a glycophosphatidylinositol (GPI) anchor. Wild-type ICAM-1 appeared to localize most prominently in microvilli whereas GPI-ICAM-1 demonstrated a uniform cell surface distribution. Disruption of microfilaments with cytochalasin B (CCB) changed the localization of wild-type ICAM-1 but had no effect on GPI-ICAM-1. Some B-cell lines demonstrated a prominent accumulation of ICAM-1 into the uropod region whereas other cell surface proteins examined were not preferentially localized. CCB also induced redistribution of ICAM-1 in these cells. For characterization of cytoskeletal proteins interacting with ICAM-1, a 28-residue peptide that encompasses the entire predicted cytoplasmic domain (ICAM-1,478-505) was synthesized, coupled to Sepharose-4B, and used as an affinity matrix. One of the most predominant proteins eluted either with soluble ICAM-1,478-505-peptide or EDTA, was 100 kD, had a pI of 5.5, and in Western blots reacted with alpha-actinin antibodies. A direct association between alpha-actinin and ICAM-1 was demonstrated by binding of purified alpha-actinin to ICAM-1,478-505-peptide and to immunoaffinity purified ICAM-1 and by a strict colocalization of ICAM-1 with alpha-actinin, but not with the cytoskeletal proteins talin, tensin, and vinculin. The region of ICAM-1,478-505 interacting with alpha-actinin was mapped to the area close to the membrane spanning region. This region contains several positively charged residues and appears to mediate a charged interaction with alpha-actinin which is not highly dependent on the order of the residues.

scholarly journals Intercellular adhesion molecule-1 dimerization and its consequences for adhesion mediated by lymphocyte function associated-1.

1995 ◽  
Vol 182 (5) ◽  
pp. 1231-1241 ◽  
Author(s):  
J Miller ◽  
R Knorr ◽  
M Ferrone ◽  
R Houdei ◽  
C P Carron ◽  
...  
Keyword(s):  
Cell Surface ◽  
Adhesion Molecule ◽  
Solid Phase ◽  
Intercellular Adhesion ◽  
Intercellular Adhesion Molecule ◽  
High Avidity ◽  
Lymphocyte Function ◽  
Intercellular Adhesion Molecule 1 ◽  
Interaction Sites ◽  
Complement Receptor 3

Intercellular adhesion molecule-1 (ICAM-1, CD54) is a ligand for the integrins lymphocyte function associated-1 (LFA-1, CD11a/CD18) and complement receptor-3 (Mac-1, CD11b/CD18) making it an important participant in many immune and inflammatory processes. Modified recombinant soluble ICAM-1 formed dimers. This result indicated that the ectodomain of ICAM-1 contains homophilic interaction sites. Soluble ICAM-1 dimers bind to solid-phase purified LFA-1 with high avidity (dissociation constant [Kd] = 8 nM) in contrast to soluble ICAM-1 monomers whose binding was not measurable. Cell surface ICAM-1 was found to be dimeric based on two distinct criteria. First, a monoclonal antibody specific for monomeric soluble ICAM-1, CA7, binds normal ICAM-1 poorly at the cell surface; this antibody, however, binds strongly to two mutant forms of ICAM-1 when expressed at the cell surface, thus identifying elements required for dimer formation. Second, chemical cross-linking of cell surface ICAM-1 on transfected cells and tumor necrosis factor-activated endothelial cells results in conversion of a portion of ICAM-1 to a covalent dimer. Cell surface ICAM-1 dimers are more potent ligands for LFA-1-dependent adhesion than ICAM-1 monomers. While many extracellular matrix-associated ligands of integrins are multimeric, this is the first evidence of specific, functionally important homodimerization of a cell surface integrin ligand.

scholarly journals Transcriptional Activation of mRNA of Intercellular Adhesion Molecule 1 and Induction of Its Cell Surface Expression in Normal Human Gingival Fibroblasts by Mycoplasma salivarium andMycoplasma fermentans

1999 ◽  
Vol 67 (6) ◽  
pp. 3061-3065 ◽  
Author(s):  
Li Dong ◽  
Ken-Ichiro Shibata ◽  
Yoshihiko Sawa ◽  
Akira Hasebe ◽  
Yuji Yamaoka ◽  
...  
Keyword(s):  
Cell Surface ◽  
Adhesion Molecule ◽  
Transcriptional Activation ◽  
Surface Expression ◽  
Intercellular Adhesion ◽  
Cell Surface Expression ◽  
Intercellular Adhesion Molecule ◽  
Gingival Tissue ◽  
Intercellular Adhesion Molecule 1 ◽  
Normal Human

ABSTRACT Lipoproteins in the cell membranes of both Mycoplasma salivarium and Mycoplasma fermentans were demonstrated to trigger the transcription of intercellular adhesion molecule-1 mRNA in normal fibroblasts isolated from human gingival tissue and to induce its cell surface expression by a mechanism distinct from that of Escherichia coli lipopolysaccharide. The lipid moiety of the lipoproteins was suggested to play a key role in the expression of the activity.

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