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Electronic Resource

Evidence for cholecystokinin receptor subtype in endocrine pancreas

Verspohl, E.J. ; Hafner, B. ; He, X. ; [et al.]

Amsterdam : Elsevier

Peptides 15 (1994), S. 1353-1360

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ISSN: 0196-9781

Keywords: Cholecystokinin receptor subtype ; Endocrine pancreas ; Exocrine pancreas

Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002

Topics: Chemistry and Pharmacology

Type of Medium: Electronic Resource

URL: http://linkinghub.elsevier.com/retrieve/pii/0196-9781(94)90108-2

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Disialoganglioside GD2 in human neuroectodermal tumor cell lines and gliomas (1991)

Longee, D. C. ; Wikstrand, C. J. ; M»nsson, J. -E. ; [et al.]

Springer

Acta neuropathologica 82 (1991), S. 45-54

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ISSN: 1432-0533

Keywords: GD2 ; Monoclonal antibodies ; Gliomas ; Ganglisides ; Medulloblastomas

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Summary Monoclonal antibodies (mAbs) recognizing the disialoganglioside II3(NeuAc)2GgOse3Cer (GD2) were produced by immunizing mice with the GD2-expressing neuroblastoma cell line LAN-1 and a prefusion boost with purified GD2 coupled to Salmonella minnesota. Two IgM mAbs were isolated which demonstrated high levels of reactivity (binding ratios in excess of 100) with GD2 by solid-phase radioimmunoassay and positivity in high-performance thin-layer chromatography (HPTLC) immunostain; only one (DMAb-20) was subsequently shown by analysis with a panel of defined ganglioside species to be specific for the minimum epitope of GD2, GalNAcβ1-4(NeuAcα2-8NeuAcα2-3)Gal-. DMAb-20 was used to evaluate the expression of GD2 by malignant glioma and medulloblastoma cell lines using cell surface radioimmunoassay, indirect membrane immunofluorescence, HPTLC immunostain, and densitometric analysis of extracted gangliosides from selected cell lines. Sixteen of 20 (80%) malignant glioma and 5 of 5 medulloblastoma cell lines reacted with DMAb-20; in agreement with previous studies, 5 of 5 neuroblastoma and 2 of 3 melanoma cell lines also reacted with DMAb-20. GD2 was proportionally increased in the glioma and medulloblastoma cell lines relative to levels in normal brain, as determined by densitometric analysis. In a phenotypic survey of malignant glioma biopsies, tumor cells in 24 of 30 (80%) cases stained positively with DMAb-20. Reactive astrocytes, both within and adjacent to tumors, were frequently intensely stained. Among the morphological variants of glioblastoma examined, the most intense staining with DMAb-20 was observed in neoplastic gemistocytes, with the weakest or absent staining in small cell glioblastomas. As GD2 is a commonly expressed surface antigen of gliomas and medulloblastomas, expression of which is retained in tissue culture, DMAb-20 will be useful in determining the functional role of GD2 in cell-cell interaction, adhesion, and invasion, and in defining altered growth control mechanisms of central nervous system neoplasms in in vitro models.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00310922

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Differences in crystal properties and ligand affinities of an antifluorescyl fab (4-4-20) in two solvent systems (1988)

Gibson, A. L. ; Herron, J. N. ; He, X.-M. ; [et al.]

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 3 (1988), S. 155-160

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ISSN: 0887-3585

Keywords: monoclonal antibodies ; high-affinity combining sites ; MPD ; Effects of fluorescein binding ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Medicine

Notes: An antigen-binding fragment (Fab) from a murine monoclonal antibody (4-4-20) with high affinity for fluorescein was cocrystallized with ligand in polyethylene glycol (PEG) and 2-methl-2,4-pentanediol (MPD) in forms suitable for X-ray analyses. In MPD the affinity of the intact antibody for fluorescein was 300 times lower than the value (3.4 × 1010 M-1) obtained in aqueous buffers. This decreased affinity was manifested by the partial release of bound fluorescein when MPD was added to solutions of liganded Feb during crystallization trials, In PEG, the ligand remained firmly bound to the protein. The liganded Feb crystallized in the monoclinic space group P21 in PEG, with a = 58.6, b = 97.2, c = 44.5 Å and β = 95.2°. In MPD the space group was triclinic P1, with a = 58.3, b = 43.4, c = 42.3 Å, α = 83.9°, β = 87.6°, and γ = 84.5°. X-ray diffraction data were collected for both forms to 2.5-Å resolution. Surprisingly, the triclinic form of the liganed antifluorescyl Feb had the same space group, closely similar cell dimensions, and practically the same orientation in the unit cell as an unliganded Fab (BV04-01) with activity against single-stranded DNA.

Additional Material: 3 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/prot.340030304

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An autoantibody to single-stranded DNA: Comparison of the three-dimensional structures of the unliganded fab and a deoxynucleotide-fab complex (1991)

Herron, J. N. ; He, X. M. ; Ballard, D. W. ; [et al.]

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 11 (1991), S. 159-175

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ISSN: 0887-3585

Keywords: anti-ss-DNA autoantibody ; deoxynucleotide-Fab complex ; conformational changes in protein when ligand is bound ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Medicine

Notes: Crystal structures of the Fabs from an autoantibody (BV04-01) with specificity for single-stranded DNA have been determined in the presence and absence of a trinucleotide of deoxythymidylic acid, d(pT)3. Formation of the ligand-protein complex was accompanied by small adjustments in the orientations of the variable (VL and VH) domains. In addition, there were local conformational changes in the first hypervariable loop of the light chain and the third hypervariable loop of the heavy chain, which together with the domain shifts led to an improvement in the complementarity of nucleotide and Fab. The sugar-phosphate chain adopted an extended and “open” conformation, with the base, sugar, and phosphate components available for interactions with the protein. Nucleotide 1 (5′-end) was associated exclusively with the heavy chain, nucleotide 2 was shared by both heavy and light chains, and nucleotide 3 was bound by the light chain. The orientation of phosphate 1 was stabilized by hydrogen bonds with serine H52a and asparagine H53. Phosphate 2 formed an ion pair with arginine H52, but no other charge-charge interactions were observed. Insertion of the side chain of histidine L27d between nucleotides 2 and 3 resulted in a bend in the sugar-phosphate chain. The most dominant contacts with the protein involved the central thymine base, which was immobilized by cooperative stacking and hydrogen bonding interactions. This base was intercalated between a tryptophan ring (no. H100a) from the heavy chain and a tyrosine ring (no. L32) from the light chain. The resulting orientation of thymine was favorable for the simultaneous formation of two hydrogen bonds with the backbone carbonyl oxygen and the side chain hydroxyl group of serine L91 (the thymine atoms were the hydrogen on nitrogen 3 and keto oxygen 4).

Additional Material: 7 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/prot.340110302

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