Evidence that CDw108 membrane protein bears the JMH blood group antigen

Mudad, Raja; Rao, Neeraja; Angelisová, Pavla; Hořejšı́, Václav; Telen, Marilyn J.

doi:10.1046/j.1537-2995.1995.35795357878.x

Cited by 32 publications

(14 citation statements)

References 13 publications

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“…37 The sema4D knockout impairs collagen-induced platelet aggregation in vitro and inhibits platelet accumulation after vascular injury in vivo. 15,38 Sema7A (CD108) was originally identified in the immune system 39 and as the JMH antigen on erythrocytes, 40 but it is also expressed by neurons and has a role in axon guidance. 41 Known binding partners for sema7A include plexin C1 42 and integrin ␣ 1 ␤ 1 .…”

Section: The Impact Of Sheddingmentioning

confidence: 99%

Deciphering the human platelet sheddome

Fong

Barry

Tran

et al. 2011

Blood

146

130

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Activated platelets shed surface proteins, potentially modifying platelet function as well as providing a source of bioactive fragments. Previous studies have identified several constituents of the platelet sheddome, but the full extent of shedding is unknown. Here we have taken a global approach, analyzing protein fragments in the supernate of activated platelets using mass spectroscopy and looking for proteins originating from platelet membranes. After removing plasma proteins and microparticles, 1048 proteins were identified, including 69 membrane proteins. Nearly all of the membrane proteins had been detected previously, but only 10 had been shown to be shed in platelets. The remaining 59 are candidates subject to confirmation. Based on spectral counts, protein representation in the sheddome varies considerably. As proof of principle, we validated one of the less frequently detected proteins, semaphorin 7A, which had not previously been identified in platelets. Surface expression, cleavage, and shedding of semaphorin 7A were demonstrated, as was its association with ␣-granules. Finally, cleavage of semaphorin 7A and 12 other proteins was substantially reduced by an inhibitor of ADAM17, a known sheddase. These results define a subset of membrane proteins as sheddome candidates, forming the basis for further studies examining the impact of ectodomain shedding on platelet function. (Blood. 2011;117(1): e15-e26)

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Section: The Impact Of Sheddingmentioning

confidence: 99%

Deciphering the human platelet sheddome

Fong

Barry

Tran

et al. 2011

Blood

146

130

View full text Add to dashboard Cite

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“…Semaphorin-7A (CDw108) is a GPI-linked protein carrying the John-Milton-Hagen blood group antigen (Mudad et al, 1995) whose expression has also been observed on activated leucocytes as well as in the spleen, thymus, testis, placenta, brain and spinal cord (Xu et al, 1998;Yamada et al, 1999). Semaphorin-7A has an important role in the development of both the nervous and immune systems where it promotes axon outgrowth through integrins (Pasterkamp et al, 2003), and has also been implicated in the regulation of T-cell function (Czopik et al, 2006;Suzuki et al, 2007;Gras et al, 2013), bone cell differentiation (Delorme et al, 2005), spreading and dendricity in human skin melanocytes (Scott et al, 2008), nerve regeneration and inflammation processes in the cornea (Namavari et al, 2012), and GnRH-1 neuron development (Messina et al, 2011).…”

Section: Semaphorin-7a: An Erythrocyte Receptor For P Falciparum Mtrapmentioning

confidence: 99%

Identifying novelPlasmodium falciparumerythrocyte invasion receptors using systematic extracellular protein interaction screens

et al. 2013

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The invasion of host erythrocytes by the parasite Plasmodium falciparum initiates the blood stage of infection responsible for the symptoms of malaria. Invasion involves extracellular protein interactions between host erythrocyte receptors and ligands on the merozoite, the invasive form of the parasite. Despite significant research effort, many merozoite surface ligands have no known erythrocyte binding partner, most likely due to the intractable biochemical nature of membrane-tethered receptor proteins and their interactions. The few receptor–ligand pairs that have been described have largely relied on sourcing erythrocytes from patients with rare blood groups, a serendipitous approach that is unsatisfactory for systematically identifying novel receptors. We have recently developed a scalable assay called AVEXIS (for AVidity-based EXtracellular Interaction Screen), designed to circumvent the technical difficulties associated with the identification of extracellular protein interactions, and applied it to identify erythrocyte receptors for orphan P. falciparum merozoite ligands. Using this approach, we have recently identified Basigin (CD147) and Semaphorin-7A (CD108) as receptors for RH5 and MTRAP respectively. In this essay, we review techniques used to identify Plasmodium receptors and discuss how they could beapplied in the future to identify novel receptors both for Plasmodium parasites but also other pathogens.

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“…Monoclonal antibodies of the CD108 cluster of differentiation may also be considered anti -JMH [9] . A monoclonal antibody (H8), produced from a mouse immunised with a human lymphoid cell line derived from a patient with acute lymphocytic leukaemia, appeared to have the same specifi city as anti -JMH5 [23,24] .…”

Section: Monoclonal Antibodiesmentioning

confidence: 99%