A single gene encodes soluble and membrane-bound forms of the major histocompatibility Qa-2 antigen: Anchoring of the product by a phospholipid tail

Stroynowski, Iwona; Soloski, Mark J.; Low, Martin G.; Hood, Leroy

doi:10.1016/0092-8674(87)90334-5

Cited by 117 publications

(74 citation statements)

References 44 publications

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“…Mouse LB6 cells (Corsaro and Pearson, 1981), mouse Ltk-cells (Stroynowski et al, 1987) and Simian COS-7 cells (Gluzman, 1981) were cultured in Dulbecco's modified Eagle's medium with added glutamine, penicillin, streptomycin and 10% fetal calf serum. For cultivation of stably transfected cells, the medium was supplemented with 0.4 mg geneticin/ ml.…”

Section: Cell Culturementioning

confidence: 99%

“…For this purpose, we studied the properties of the protein after stable transfection of mouse Ltk-cells with human wild-type human u-PAR cDNA. This cell line has been shown to be incapable of expressing glycosyl-PtdIns-anchored proteins on the cell surface (Stroynowski et al, 1987). Controls included similarly transfected murine LB6 cells which do not carry this deficiency.…”

Section: Expression Of Human U-par In a Glycosyl-ptdins-ancbor-deficimentioning

confidence: 99%

See 1 more Smart Citation

Structural requirements for glycosyl‐phosphatidylinositol‐anchor attachment in the cellular receptor for urokinase plasminogen activator

Møller

Ploug

Blasi

1992

European Journal of Biochemistry

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The urokinase-plasminogen-activator receptor (u-PAK) is a glycosyl-phosphatidylinositol(g1y-cosyl-Ptd1ns)-anchored membrane protein. Using site-directed mutagenesis, we have studied features in the u-PAR sequence important for successful glycosyl-PtdIns attachment. Two critical sequence elements were identified. In the sequence Ser282-Gly283-Ala284, simultaneous substitution of all of these residues prevented membrane anchoring. Individual substitution of each of the residues indicated that Gly283 is the more critical residue and the likely attachment site. However, it was unexpectedly found that mutation of this residue gave rise only to a partial impairment of glycosyl-PtdIns attachment. We therefore propose that more than one residue within this sequence can be utilized as glycosyl-PtdIns-attachment site. In the last eight COOH-terminal amino acids encoded in u-PAR cDNA, deletion of this sequence (residues 306 -31 3) completely prevented glycosyl-PtdIns attachment. However, the remaining COOH-terminal region proved still to possess a potential glycosylPtdIns signal activity; it could be converted to a new functional glycosyl-PtdIns signal by substitution of a single positively charged residue (Arg304). Substitution of Arg304 by Leu converted this truntaced u-PAR to a glycosyl-PtdTns-anchored protein. indistinguishable from the wild type. Substitution of Arg304 by a negatively charged residue (Glu) led to a partial aquisition of the glycosyl-PtdInsanchoring ability. These findings show that charged amino acids placed in the COOH-terminus interfere negatively with glycosyl-Ptdlns-anchoring, and, furthermore, that this effect is more pronounced for positively charged than for negatively charged amino acid residues.

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Section: Cell Culturementioning

confidence: 99%

Section: Expression Of Human U-par In a Glycosyl-ptdins-ancbor-deficimentioning

confidence: 99%

Structural requirements for glycosyl‐phosphatidylinositol‐anchor attachment in the cellular receptor for urokinase plasminogen activator

Møller

Ploug

Blasi

1992

European Journal of Biochemistry

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“…The Q7/Q9 is GPIlinked and sensitive to cleavage with phospholipases (37). The Q6/Q8 proteins have phospholipase-resistant C termini, which are truncated due to a premature stop codon in exon 5.…”

Section: Discussionmentioning

confidence: 99%

The Role of Structurally Conserved Class I MHC in Tumor Rejection: Contribution of the Q8 Locus

Chiang

Stroynowski

2006

The Journal of Immunology

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The mouse multimember family of Qa-2 oligomorphic class I MHC genes is continuously undergoing duplications and deletions that alter the number of the two “prototype” Qa-2 sequences, Q8 and Q9. The frequent recombination events within the Q region lead to strain-specific modulation of the cumulative Qa-2 expression levels. Q9 protects C57BL/6 hosts from multiple disparate tumors and functions as a major CTL restriction element for shared tumor-associated Ags. We have now analyzed functional and structural properties of Q8, a class I MHC that differs significantly from Q9 in the peptide-binding, CTL-interacting α1 and α2 regions. Unexpectedly, we find that the extracellular domains of Q8 and Q9 act similarly during primary and secondary rejection of tumors, are recognized by cross-reactive antitumor CTL, have overlapping peptide-binding motifs, and are both assembled via the transporter associated with the Ag processing pathway. These findings suggest that shared Ag-presenting functions of the “odd” and “even” Qa-2 loci may contribute to the selective pressures shaping the haplotype-dependent quantitative variation of Qa-2 protein expression.

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“…However, the Q genes differ from classical transplantation genes, which function as restriction elements for cytotoxic T lymphocytes, in several respects. Unlike the classical class I antigens all of which are transmembrane proteins, the Q region products are found in two different forms: as secreted molecules (Kress et al 1983;Devlin et al 1985a) and as cell surface molecules anchored in the membrane via phosphatidylinositol (PI) linkage (Stiernberg et al 1987;Stroynowski et al 1987;Waneck et al 1988). In addition, their expression is limited to only a few tissues of hematopoietic origin.…”

Section: Introductionmentioning

confidence: 99%

Developmental and tissue-specific expression of the Q5 k gene

Schwemmle¹,

Bevec²,

Brem³

et al. 1991

Immunogenetics

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Abstract. Expression of the Q5 k gene was examined by northern blot analysis and polymerase chain reaction (PCR) in the AKR mouse and various cell lines, each of the H-2 ~ haplotype. Our results show that Q5 k mRNA is present during the whole postimplantational development of the AKR embryo/fetus (gestation day 6 to 15). In the juvenile mouse (week 2 to 4) transcription of the Q5 ~ gene persisted in all organs examined. In contrast, in the adult animal expression of the Q5 ~ gene was limited to the thymus and uterus of the pregnant mouse. Upon malignant transformation, the amount of Q5k-specific mRNA increased dramatically in thymus and could also be observed in the spleen of thymoma bearing animals. Expression of the Q5 k gene was also detectable in several transformed mouse cell lines. Mitogen stimulation or treatment with cytokines induced Q5 k expression in primary spleen cell cultures. A possible explanation for the tissue-restricted expression in the adult AKR mouse is discussed.

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A single gene encodes soluble and membrane-bound forms of the major histocompatibility Qa-2 antigen: Anchoring of the product by a phospholipid tail

Cited by 117 publications

References 44 publications

Structural requirements for glycosyl‐phosphatidylinositol‐anchor attachment in the cellular receptor for urokinase plasminogen activator

Structural requirements for glycosyl‐phosphatidylinositol‐anchor attachment in the cellular receptor for urokinase plasminogen activator

The Role of Structurally Conserved Class I MHC in Tumor Rejection: Contribution of the Q8 Locus

Developmental and tissue-specific expression of the Q5 k gene

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