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M R Price

Publications and source records attributed to M R Price.

At least 199 records · Page 11Linked to original sources
PubMed1973

Detection of circulating hepatoma D23 antigen and immune complexes in tumour bearer serum.

Serum from rats bearing progressively growing aminoazo dye-induced rat hepatomata has been fractionated by Sephadex G150 gel filtration chromatography and isolated fractions have been examined by indirect membrane immunofluorescence techniques to detect tumour specific antigen and antibody. Hepatoma D23-specific antigenic activity was associated with material (of approximate molecular weight <150,000) isolated in the included volume of the gel at pH 7·3. The fraction excluded from the gel (of approximate molecular weight >150,000) was adjusted to pH 3·0 and further separated by Sephadex G150 gel filtration chromatography at pH 3·0 into gel included and excluded fractions. Hepatoma D23 specific antibody, demonstrable by membrane immunofluorescence staining of hepatoma D23 cells, was found to be eluted in the excluded volume and specific antigenic activity was retarded into the included volume of the gel. These results indicate that hepatoma D23 bearer serum contains free circulating tumour specific antigen in excess, together with specific immune complexes. The presence of these factors in tumour bearer serum is discussed in terms of "blocking" phenomena whereby serum factors may protect tumour cells from sensitized lymphocyte cytotoxic attack.

Animals↗
PubMedDate not supplied

Tumour rejection antigens associated with carcinogen-induced tumours.

The most important immunological characteristic of tumours induced with chemical carcinogens is the expression of highly polymorphic tumour specific antigens. These cell surface components are primarily concerned with immune rejection reactions to these types of tumour, and current evidence strongly suggests that they are related to normal alloantigen.

2-Acetylaminofluorene↗
PubMedDate not supplied

Immunoconjugate design: a predictive approach for coupling of daunomycin to monoclonal antibodies.

There is increasing interest in the development of daunomycin-antibody immunoconjugates for the targeting of drug to specific cells or tissues. To this end, we have examined the factors influencing the synthesis of daunomycin-monoclonal antibody conjugates linked covalently by an acid-labile cis-aconitic spacer (which is considered to aid drug release from immunoconjugates in the lysosomes and thus enhance their cytotoxic potential). A rapid and efficient procedure for the purification of drug from contaminants and stabilizers was first developed; conditions for the optimal preparation of cis-aconityldaunomycin were established; products were analyzed and identified by TLC and HPLC. The coupling of cis-aconityldaunomycin to antibody was accomplished by activating the modified drug with a carbodiimide before addition to antibody. Several factors were identified which influenced the efficiency of the conjugation; in particular, the compositional features of the antibody which determine its electrophoretic charge characteristics were of profound effect. However, by appropriate choice and control of buffer pH during conjugation, it was possible to define conditions resulting in the controlled substitution of antibody with drug. The consequent effects upon the cell-binding activity of immunoconjugates were established and related to the extent of substitution. The procedures described enable appropriate reaction conditions to be selected for the linkage of daunomycin to antibody (at set drug/antibody molar ratios) and in good yield, based upon consideration of the compositional and charge properties of the antibody.

Antibodies, Monoclonal↗
PubMedDate not supplied

Detection of circulating mammary mucin (Muc1) and MUC1 immune complexes (Muc1-CIC) in healthy women.

There is convincing epidemiological evidence that multiparity provides protection against the development of breast cancer. In the present study we evaluated the levels of MUC1 and MUC1 circulating immune complexes (MUC1-CIC) in 135 serum samples obtained from healthy women. The study population included 13 women who had never been pregnant, 31 primiparous pregnant women, 36 multiparous pregnant women who had lactated, 5 multiparous pregnant women who had never lactated, 24 multiparous non-pregnant women who were lactating at the time of the study, 24 multiparous non-pregnant women who had lactated, and 2 multiparous non-pregnant women who had never lactated. The purpose of this work was to detect MUC1 variations during pregnancy and lactation as well as to study the possible induction of a humoral immune response against MUC1 in these conditions. We employed ELISA techniques to measure MUC1 (CASA test) and MUC1-CIC (IgM and IgG) using two anti-MUC1 monoclonal antibodies (MAbs): C595 and SM3. Statistical analysis was performed using the ANOVA test. The pooled results pertaining to pregnant versus non-pregnant women were compared and significant differences were observed in MUC1 and MUC1-CIC-lgM levels detected with both MAbs; the MUC1-CIC-lgG levels detected with C595 were increased in the pregnant group while the MUC1-CIC-lgG levels detected with SM3 did not show any significant differences. When the results were compared between lactating and non-lactating women, no significant differences were found. In conclusion, MUC1 and MUC1-CIC-lgM, detected with both MAbs, and MUC1-CIC-4gG levels detected with the MAb C595 are apparently induced by pregnancy.

Adult↗
PubMedDate not supplied

Analysis of the temporal compressibility of breast tumour marker assays: development of a "near patient" assay.

The aim of this study was to investigate whether immunoassays for circulating MUC1 antigen in breast cancer could be compressed in time so that serum level results would be made available during the time of the patient's visit to clinic. Two assays were used: -The EMCA (Euro DPC) is a liquid phase immunoassay and the ELSA CA15-3 (CIS) is a double determinant solid phase immunoradiometric assay. The effects of shortened incubation times were investigated by assaying standards and unknown samples and comparing the results with those using the standard kit protocols. The binding kinetics of the monoclonal antibodies employed in the assays were analysed separately. We conclude that the EMCA assay can be shortened to 35 min and we have attributed this to the fast binding kinetics inherent in a liquid phase assay. This shortened assay may produce the basis for a useful "near patient" assay. By comparison, the solid phase ELSA CA15-3 assay cannot be compressed without loss in assay performance.

Antibodies, Monoclonal↗
PubMedDate not supplied

The mucin antigens: what are we measuring?

Serum of breast cancer patients contains high molecular weight, mucin-like glycoproteins which are held to be differentiation markers for certain types of normal epithelia, in particular mammary epithelium. These components have primarily been identified using monoclonal antibodies raised against human milk fat globule membranes, tumour extracts or purified mucins. Even so, many of the antibodies produced react with a discrete region of the mucin protein core involving the hydrophilic turn domain APDTRPAP. The present investigation using the anti-urinary mucin antibody, C595, illustrates both the clinical potential of the mucin antigens in breast cancer studies as well as the exquisite specificity of immune recognition of a complex polymorphic glycoprotein at the level of the individual amino acids.

Amino Acid Sequence↗