Mr75,000 PROTEIN, A TUMOR MARKER IN RENAL ADENOCARCINOMA, REACTING WITH ANTIBODIES TO A SYNTHETIC PEPTIDE BASED ON A CLONED HUMAN ENDOGENOUS RETROVIRAL NUCLEOTIDE SEQUENCE

1985 ◽  
Vol 36 (3) ◽  
pp. 379-382 ◽  
Author(s):  
T. WAHLSTRÖM ◽  
A. NÄRVÄNEN ◽  
J. SUNI ◽  
R. PAKKANEN ◽  
T. LEHTONEN ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Tumor Marker ◽  
Synthetic Peptide ◽  
Protein A ◽  
Renal Adenocarcinoma

scholarly journals Peptide Blocking CTLA-4 and B7-1 Interaction

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 253
Author(s):  
Stepan V. Podlesnykh ◽  
Kristina E. Abramova ◽  
Anastasia Gordeeva ◽  
Andrei I. Khlebnikov ◽  
Andrei I. Chapoval
Keyword(s):  
Cancer Immunotherapy ◽  
Functional Activity ◽  
Synthetic Peptide ◽  
Checkpoint Inhibitors ◽  
Specific Interaction ◽  
Protein A ◽  
Tumor Rejection ◽  
Immune Checkpoints ◽  
3D Computer Model ◽  
Molecular Compounds

Discovery of the B7 family immune checkpoints such as CTLA-4 (CD152), PD-1 (CD279), as well as their ligands B7-1 (CD80), B7-2 (CD86), B7-H1 (PD-L1, CD274), and B7-DC (PD-L2, CD273), has opened new possibilities for cancer immunotherapy using monoclonal antibodies (mAb). The blockade of inhibitory receptors (CTLA-4 and PD-1) with specific mAb results in the activation of cancer patients’ T lymphocytes and tumor rejection. However, the use of mAb in clinics has several limitations including side effects and cost of treatment. The development of new low-molecular compounds that block immune checkpoints’ functional activity can help to overcome some of these limitations. In this paper, we describe a synthetic peptide (p344) containing 14 amino acids that specifically interact with CTLA-4 protein. A 3D computer model suggests that this peptide binds to the 99MYPPPY104 loop of CTLA-4 protein and potentially blocks the contact of CTLA-4 receptor with B7-1 ligand. Experimental data confirm the peptide-specific interaction with CTLA-4 and its ability to partially block CTLA-4/B7-1 binding. The identified synthetic peptide can be used for the development of novel immune checkpoint inhibitors that can block CTLA-4 functional activity for cancer immunotherapy.

Nucleotide sequence of a variant protein A ofStaphylococcus aureus suggests molecular heterogeneity among strains

1991 ◽  
Vol 31 (5) ◽  
pp. 337-345 ◽  
Author(s):  
Marcelo De Macedo Brígido ◽  
Célia Regina Monte Barardi ◽  
Claudio A. Bonjardin ◽  
Cecília Luiza Simões Santos ◽  
Maria De Lourdes Junqueira ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Protein A ◽  
Molecular Heterogeneity ◽  
Ofstaphylococcus Aureus ◽  
Variant Protein

scholarly journals Presence in human eosinophils of a lysophospholipase similar to that found in the pancreas

1995 ◽  
Vol 309 (1) ◽  
pp. 141-144 ◽  
Author(s):  
F W Holtsberg ◽  
L E Ozgur ◽  
D E Garsetti ◽  
J Myers ◽  
R W Egan ◽  
...  
Keyword(s):  
Synthetic Peptide ◽  
Protein A ◽  
Pancreatic Enzyme ◽  
Gel Filtration ◽  
Pancreatic Tissue ◽  
Supernatant Fraction ◽  
Polyadenylated Rna ◽  
Rabbit Polyclonal Antibody ◽  
Dna Fragment ◽  
Lysophospholipase Activity

The supernatant fraction from lysed human eosinophils, when separated by gel-filtration chromatography, contains a protein with lysophospholipase activity of approximate molecular mass 74 kDa. This mass differs substantially from the 17 kDa of a previously cloned eosinophil lysophospholipase (Charcot-Leyden crystal protein), but is similar to that reported for a pancreatic enzyme. We have therefore further characterized this pancreatic-like lysophospholipase in human eosinophils. A rabbit polyclonal antibody was produced against a synthetic peptide consisting of amino acids 325-349 from the 74 kDa rat pancreatic lysophospholipase. Western-blot analysis of eosinophil extracts indicate that this antibody recognizes a single 74 kDa band in these preparations. Incubation of the supernatant fraction from sonified eosinophils with this antibody, followed by precipitation of antibody-antigen complexes with Protein A, removes the majority of the lysophospholipase activity. Indirect immunofluorescence examination with this antibody indicates this protein to be localized to granules of eosinophils and not in other leucocytes. Moreover, reverse transcriptase PCR of polyadenylated RNA from eosinophils and from rat pancreatic tissue with primers to rat pancreatic lysophospholipase resulted in readily detectable 1 kb DNA products in both samples. Sequencing revealed this DNA fragment to be identical with the human pancreatic lysophospholipase cDNA sequence. Taken together, these data indicate that eosinophils contain a lysophospholipase that is similar to the human pancreatic enzyme.

SYNTHETIC PEPTIDE ANTIBODIES RECOGNIZE PLASMA AND RECOMBINANT FVIII

1987 ◽  
Author(s):  
N Pancham ◽  
M Dumas ◽  
J Brown ◽  
T C Michaud ◽  
W J Knowles
Keyword(s):  
Synthetic Peptide ◽  
Protein A ◽  
Fluid Phase ◽  
Activity Assay ◽  
Preliminary Screening ◽  
Fviii Activity ◽  
Polyclonal Igg ◽  
Capture Antibody ◽  
Recombinant Fviii ◽  
Antipeptide Antibody

Monoclonal antibodies were raised against synthetic peptides corresponding to the N-termini of the 90kd and 80kd subunits of human FVIII. Preliminary screening was performed directly against the peptides (linked to albumin) coated onto polystyrene wells. IgG was purified by Protein A-Sepharose and affinity purified using the immunogen peptides linked to Sepharose. Immunoreactivity with both plasma and recombinant FVIII was compared by Western blotting, two-site ELISA employing a neutralizing rabbit anti-FVIII IgG as capture antibody, and inhibition in a fluid phase FVIII activity assay. None of the antibodies neutralized clotting or amidolytic activities associated with either FVIII protein. All of the antibodies immunoblotted intacl or thrombin digested FVIII polypeptides according to their anticipated epitope recognition sites; this was useful in determining identity between the two types of FVIII protein. Furthermore, when either FVIII protein was bound to polyclonal IgG coated onto polystyrene microtiter wells, the 80kd antipeptide antibody was capable of detecting both antigens with equal affinity. These results, coupled with results using the 90k antipeptide suggest that epitope accessibility for these antipeptide antibodies is the same for plasma and recombinant FVIII under the conditions tested.

scholarly journals Purification, from cultured human choriocarcinoma cells, of a 75000-Mr protein reacting with antibodies to a synthetic peptide based on a cloned human endogenous provirus nucleotide sequence

1985 ◽  
Vol 231 (1) ◽  
pp. 53-57 ◽  
Author(s):  
A Närvänen
Keyword(s):  
Nucleotide Sequence ◽  
Synthetic Peptide ◽  
Present Report ◽  
First Trimester ◽  
Cell Protein ◽  
Ionic Detergent ◽  
Choriocarcinoma Cells ◽  
Immunohistological Staining ◽  
Human Choriocarcinoma Cells ◽  
Hydrophilic Molecule

We previously detected in cultured choriocarcinoma cells a 75000-Mr polypeptide defined by immunoblotting with antibody to a synthetic peptide Sp23 (Cys-Glu-Asn-Pro-Ser-Gln-Phe-Tyr-Glu-Asp-Leu) based on a cloned human endogenous proviral nucleotide sequence. On immunohistological staining, anti-Sp23 stains antigen(s) in the syncytiotrophoblasts of first-trimester placentas and in renal-cell adenocarcinoma tissues. The present report describes purification to homogeneity of the protein from cultured choriocarcinoma cells. The procedure involves extraction with non-ionic detergent and h.p.l.c. using, sequentially, gel-permeation, anion-exchange and reverse-phase columns. The yield was 110 micrograms/g of total choriocarcinoma-cell protein. The results indicate that the purified protein is a monomeric and relatively hydrophilic molecule of Mr 75000.

Affinity purification of polyclonal antibodies using a new all-D synthetic peptide ligand: comparison with protein A and protein G

2002 ◽  
Vol 271 (1-2) ◽  
pp. 77-88 ◽  
Author(s):  
Antonio Verdoliva ◽  
Filomena Pannone ◽  
Maria Rossi ◽  
Sergio Catello ◽  
Vincenzo Manfredi
Keyword(s):  
Synthetic Peptide ◽  
Polyclonal Antibodies ◽  
Affinity Purification ◽  
Protein A ◽  
Protein G ◽  
Peptide Ligand

Amylase Secretion by Nasal Glands

1986 ◽  
Vol 95 (3) ◽  
pp. 284-287 ◽  
Author(s):  
Masayoshi Tachibana ◽  
Hiroyuki Morioka ◽  
Fumiko Tanimura ◽  
Mitsuo MacHino ◽  
Osamu Mizukoshi
Keyword(s):  
Tumor Marker ◽  
Nasal Cavity ◽  
Nasal Mucosa ◽  
Protein A ◽  
Amylase Secretion ◽  
Nasal Secretions ◽  
First Time ◽  
Nasal Glands

Amylase, an enzyme that hydrolyzes starch, has been localized in the nasal mucosa for the first time by the protein A-gold technique. The amylase appeared to be produced by serous cells of the nasal glands. This enzyme has the potential for use as a tumor marker for cancer of the nasal cavity. The function of amylase in the physiology of nasal secretions is discussed.

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