Mechanism of target cell recognition by CD3− LGL

Bino, Tamar; Frey, Joyce L.; Ortaldo, John R.

doi:10.1016/0008-8749(92)90266-r

Cited by 7 publications

(4 citation statements)

References 18 publications

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“…Moreover, a cyclophylin-related 150 kDa protein was described as a component of a putative tumour-recognition complex [36]. This protein was recognized by an anti-idiotypic serum against a MoAb [37] that was produced against NK target membrane glycoproteins of K562 tumour cells [5]. On the other hand, we cannot make any decision at present on whether the receptors specific for acetylated sugars and responsible for lytic target recognition are specific for a common epitope present in all inhibitory sugar acetates or whether these receptors show some polymorphism.…”

Section: Discussionmentioning

confidence: 99%

“…Promising candidate molecules with target antigen specificity have been shown to be present in high-molecular weight glycoproteins isolated from various target cells [3,4). In one study monoclonal antibodies (MoAb) developed against these glycoproteins yielded a MoAb 36 that inhibited conjugate formation between LGL and K562 target cells and also lysis of K562 cells [5]. Similarly, a MoAb developed against NC-37, a human B cell lymphoma, inhibited binding and lysis of sensitive target cells by NK as well as LAK cells [61.…”

Section: Introductionmentioning

confidence: 99%

“…Similarly, a MoAb developed against NC-37, a human B cell lymphoma, inhibited binding and lysis of sensitive target cells by NK as well as LAK cells [61. Both inhibiting MoAb were recognizing the carbohydrate moiety of the respective target antigens [5,6] thus indicating that specific carbohydrate structures on target cells might carry the chemospecificity of target cell recogtiition.…”

Section: Introductionmentioning

confidence: 99%

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Chemospecificity and Cross‐Reactivity of Target Cell Recognition by Human CD56⁺ NK and LAK Cells

et al. 1995

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Inhibition of specific cytotoxicity of highly purified (> 95%) human CD56+ NK and LAK cells against K562 tumour cells was studied with various sugar acetates. Maximum inhibitory specificity was obtained with 60%-deacetylated penta-acetates of mannose, galactose, glucose, or 80%-deacetylated penta-O-acetate of N-acetyl neuraminic acid. The inhibition was strictly dosedependent and 100% inhibition was achieved in the concentration range of 500-1000 nmoles/ml with all four sugar acetate samples. Enhancement of specific cytotoxicity in the presence of rhamnogalacturonan (RG; 500 ng/ml), acting as a bridging molecule, was also inhibited in a dose-dependent manner with the same inhibitory specificity and within the same concentration range indicating involvement of the same number of sugar acetate-specific receptors. Moreover, formation of lytic CD56+ effector cell/tumour cell (E/T) conjugates was equally well inhibited whereas formation of total E/T conjugates was only partially inhibited (NK: 44-73%; LAK: 46-50%). E/T conjugate formation in the presence of RG was enhanced. Inhibition of the enhancement of formation of lytic E/T conjugates in the presence of RG was again completely accomplished with the same inhibitory specificity and within the same concentration ranges as recorded for E/T conjugate formation in the absence of RG. However, inhibition of total E/T conjugate formation was again only partially achieved at the given concentrations. The data support the assumption of an NK cell receptor with specificity for acetylated carbohydrate moieties on target cells or on bridging molecules such as RG.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Chemospecificity and Cross‐Reactivity of Target Cell Recognition by Human CD56⁺ NK and LAK Cells

et al. 1995

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“…To define the molecule(s) responsible for tumor-cell recognition by NK cells, a technique was used that involved the production of anti-idiotypic (ID) antisera to a monoclonal antibody that recognized a variety of NK-cell-susceptible tumor targets and blocked NK-cell-mediated lysis (11). The anti-ID antiserum was shown by immunofluorescence to bind specifically to CD3, CD16+ NK cells, and it blocked the binding of LGL to NK-susceptible targets, thereby preventing lysis (12).…”

mentioning

confidence: 99%

A cyclophilin-related protein involved in the function of natural killer cells.

Anderson

Gallinger

Roder

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

106

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Natural killer cells are non-major histocompatibility complex-restricted large granular lymphocytes that can recognize and destroy tumor cells without prior stimulation. A 150-kDa molecule on the surface of human natural killer cells was identified as a component of a putative tumorrecognition complex. We report here the isolation of cDNAs coding for the 150-kDa tumor-recognition molecule from human and mouse cDNA libraries. The amino terminus of the predicted protein contains a large hydrophobic region followed by a domain that is highly homologous to cyclophilin/peptidylprolyl ci-trans isomerase. The remainder of the protein is extremely hydrophilic and contains three homologous positively charged clusters. There are also three regions that contain extensive arginine-and serine-rich repeats. Comparison of the human and mouse predicted amino acid sequences revealed >80% homology.

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Signal Transduction During NK Cell Activation: Balancing Opposing Forces

Brumbaugh

Binstadt

Leibson

1998

Specificity, Function, and Development of NK Cells

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Mechanism of target cell recognition by CD3− LGL

Cited by 7 publications

References 18 publications

Chemospecificity and Cross‐Reactivity of Target Cell Recognition by Human CD56⁺ NK and LAK Cells

Chemospecificity and Cross‐Reactivity of Target Cell Recognition by Human CD56⁺ NK and LAK Cells

A cyclophilin-related protein involved in the function of natural killer cells.

Signal Transduction During NK Cell Activation: Balancing Opposing Forces

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Mechanism of target cell recognition by CD3− LGL

Cited by 7 publications

References 18 publications

Chemospecificity and Cross‐Reactivity of Target Cell Recognition by Human CD56+ NK and LAK Cells

Chemospecificity and Cross‐Reactivity of Target Cell Recognition by Human CD56+ NK and LAK Cells

A cyclophilin-related protein involved in the function of natural killer cells.

Signal Transduction During NK Cell Activation: Balancing Opposing Forces

Contact Info

Product

Resources

About

Chemospecificity and Cross‐Reactivity of Target Cell Recognition by Human CD56⁺ NK and LAK Cells

Chemospecificity and Cross‐Reactivity of Target Cell Recognition by Human CD56⁺ NK and LAK Cells