Identification and partial characterization of the human erythrocyte membrane component(s) that express the antigens of the LW blood-group system

Mallinson, Gary; Martin, Peter; Anstee, David J.; Tanner, Michael; Merry, Anthony H.; Tills, D.; Sonneborn, H.‐H.

doi:10.1042/bj2340649

Cited by 152 publications

(63 citation statements)

References 21 publications

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“…(10). Moreover, the presence of disulfide bonds between pairs of cysteine (Cys-39/Cys-83, Cys-123/ Cys-180, and Cys-43/Cys-87), as predicted below, correlated well with the loss of BS46 antigenic activity when LW was reduced with dithiothreitol (7).…”

Section: Resultssupporting

confidence: 54%

“…Whether the secreted form is released or remains attached to the cell surface by protein interaction with the membrane-bound LW or with another membrane protein is presently unknown. However, immune precipitation and Western blot analysis of human red cell membrane proteins with anti-LW antibodies (human or murine) consistantly detected a single band of 42-46 kDa, without any trace of a related protein of lower mass (6)(7)(8). This may suggest, but not prove, that the secreted isoform of the LW protein is released from the cells.…”

Section: Discussionmentioning

confidence: 93%

“…Biochemical investigations indicate that the LW antigens are carried by a 40-to 42-kDa glycoprotein that is linked to the membrane skeleton (6)(7)(8) and requires intramolecular disulfide bonds for antigenic reactivity (9). When deglycosylated, the LW protein is reduced to a 25-kDa apoprotein that is still reactive with anti-LW antibodies (8,10).…”

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confidence: 99%

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The LW blood group glycoprotein is homologous to intercellular adhesion molecules

1995

Transfusion Medicine Reviews

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The LW blood group antigens reside on a 42-kDa erythrocyte membrane glycoprotein that was purified by immunoaffinity and partiafly sequenced. From this information, a specific PCR-amplifled DNA fragment was used to screen a Agtll human bone marrow cDNA library. LW(a-b-). This showed that the protein encoded by these clones was LW gene product and suggested that the N terminus of the LW protein is oriented extracellularly. Most interestingly, the LW protein was found to exhibit sequence similarities (with -30% identity) with intercellular adhesion molecules ICAM-1, -2, and -3, which are the counterreceptors for the lymphocyte functionassociated antigens LFA-1. The extraceflular domain of LW consists, like that of ICAM-2, of two immunoglobulin-like doins, and the critical residues involved in the binding of LFA-1 to ICAMs were partially conserved in LW.The LW and Rh (rhesus) blood group systems were discovered simultaneously and were confused for a long time (reviews, refs. 1-3 Affinity Purification of the LW Protein. Membranes from two units of LW(a+b-) red cells were solubilized with 1% (wt/vol) Triton X-100 in phosphate-buffered saline (PBS) and applied to a specific affinity matrix column, prepared by binding 9 mg of purified murine monoclonal IgG antibody anti-LW (BS46) to 2 ml of protein A-agarose followed by cross-linking of the complex with dimethylpimelimidate (ImmunoPure IgG orientation kit, Pierce). After washing, the LW antigenic material bound was eluted with a glycine buffer (pH 2.8) and immediately brought to near neutrality.

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Section: Resultssupporting

confidence: 54%

Section: Discussionmentioning

confidence: 93%

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The LW blood group glycoprotein is homologous to intercellular adhesion molecules

1995

Transfusion Medicine Reviews

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“…4 The LW blood group glycoprotein, or ICAM-4, is a member of the IgSF subfamily known as intercellular adhesion molecules (ICAMs). It has 2 predicted IgSF I-set domains, [5][6][7] and within the subfamily it is most similar to ICAM-2. ICAM-4 has been found expressed only on erythroid cells and weakly in placenta.…”

Section: Introductionmentioning

confidence: 99%

Intercellular adhesion molecule-4 binds α4β1 and αV-family integrins through novel integrin-binding mechanisms

Spring

Parsons

Ortlepp

et al. 2001

Blood

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The LW blood group glycoprotein, ICAM-4, is a member of the intercellular adhesion molecule (ICAM) family expressed in erythroid cells. To begin to address the function of this molecule, ligands for ICAM-4 on hemopoietic and nonhemopoietic cell lines were identified. Peptide inhibition studies suggest that adhesion of cell lines to an ICAM-4-Fc construct is mediated by an LDV-inhibitable integrin on hemopoietic cells and an RGD-inhibitable integrin on nonhemopoietic cells. Antibody inhibition studies identified the hemopoietic integrin as ␣ 4 ␤ 1. Antibody inhibition studies on ␣ 4 ␤ 1 -negative, nonhemopoietic cell lines suggested that adhesion of these cells is mediated by ␣ V integrins (notably ␣ V ␤ 1 and ␣ V ␤ 5 ). The structure of ICAM-4 modeled on the crystal structure of ICAM-2 was used to identify surfaceexposed amino acid residues for sitedirected mutagenesis. Neither an unusual LETS nor an LDV motif in the first domain of ICAM-4 was critical for integrin binding. ICAM-4 is the first ICAM family member shown to be a ligand for integrins other than those of the ␤ 2 family, and the data suggest that ICAM-4 has a novel integrin-binding site(s). These findings suggest a role for ICAM-4 in normal erythropoiesis and may also be relevant to the adhesive interactions of sickle cells. ( IntroductionKnowledge of cell-cell and cell-extracellular matrix interactions in bone marrow is essential for an understanding of the formation of blood cells and their migration into the peripheral circulation. Such interactions are also relevant to the biology of diseases like sickle cell disease and malaria where adhesive interactions involving red cells and damaged endothelium are crucial features of the pathology. [1][2][3] These adhesive interactions frequently involve molecules belonging to the immunoglobulin superfamily (IgSF) of proteins and the family of proteins known as integrins. Integrins are heterodimers composed of 2 noncovalently associated transmembrane subunits denoted "␣" and "␤." Eight different ␤ subunits combine in a restricted manner with 18 ␣ subunits to form some 22 different integrins. Beta subunits complex with several different ␣ subunits, while most ␣ subunits (with the exception of ␣ V , ␣ 4 , and ␣ 6 ) combine with only one ␤ subunit. 4 The LW blood group glycoprotein, or ICAM-4, is a member of the IgSF subfamily known as intercellular adhesion molecules (ICAMs). It has 2 predicted IgSF I-set domains, [5][6][7] and within the subfamily it is most similar to ICAM-2. ICAM-4 has been found expressed only on erythroid cells and weakly in placenta. 8,9 ICAM-1, -2, and -3 function in inflammation and immune responses, 10 but no function for ICAM-4 has been defined.The ICAMs are ligands for ␤ 2 integrins, and all family members, including ICAM-4, are reported to bind ␣ L ␤ 2 . [10][11][12][13] ICAM-1 and ICAM-4 are also ligands for ␣ M ␤ 2 , 10,11 while the preferred ligand for ICAM-3 is ␣ D ␤ 2 . 14 Unlike ICAM-1, -2, -3, -5, which have the ␣ L ␤ 2 -binding motif (L/I)ET(P/S)L (Figure 1), ICAM-4 has th...

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“…Immunoblotting was as described by Mallinson et al (1986), except that 5 % (w/v) bovine milk powder, resuspended in PBS at pH 7.3, was used as the blocking agent.…”

Section: Production Of Antiseramentioning

confidence: 99%

Localization of the protein 4.1-binding site on human erythrocyte glycophorins C and D

Ltd¹

1994

Biochemical Journal

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Identification and partial characterization of the human erythrocyte membrane component(s) that express the antigens of the LW blood-group system

Cited by 152 publications

References 21 publications

The LW blood group glycoprotein is homologous to intercellular adhesion molecules

The LW blood group glycoprotein is homologous to intercellular adhesion molecules

Intercellular adhesion molecule-4 binds α4β1 and αV-family integrins through novel integrin-binding mechanisms

Localization of the protein 4.1-binding site on human erythrocyte glycophorins C and D

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