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J Lunney

Publications and source records attributed to J Lunney.

9 recordsLinked to original sources
PubMed2001

Summary of workshop findings for porcine myelomonocytic markers.

About 65 monoclonal antibodies (mAb) including 17 internal controls were analyzed for their ability to recognize and bind to various cells of the myelomonocytic lineage. Flow cytometry (FCM) utilizing both single and double staining, and immunoprecipitation (IP) assays were used in the analysis. About 38 of the mAb were reactive with myelomonocytic cells, resulting in nine clusters of interest. Although the exact identity of many of the molecules on the cells bound by the mAb remains undetermined, information obtained about the mAb analyzed in this workshop should be helpful in further identifying various populations of myelomonocytic cells and their stages of differentiation. Out of 12 mAbs with potential CD11 specificity, seven were assigned to three different swine specific alpha chains of the CD11/CD18 integrin heterodimer, the assignment of the remaining four was tentative. One antibody had a binding specificity consistent with SWC3 and one with SWC8. CD14 expression on pig cells was characterized with a panel of CD14-positive antibodies, two of these antibodies were assigned to swine CD14. Two antibodies were assigned to CD163. Further work is required to determine the antigens recognized by many of the other mAb.

Animals↗
PubMed2000

A porcine cell surface receptor identified by monoclonal antibodies to SWC3 is a member of the signal regulatory protein family and associates with protein-tyrosine phosphatase SHP-1.

SWC3 was defined at the First International Swine CD Workshop as a specific myelomonocytic antigen of 230 kDa with mAbs 74-22-15, 6F3 and DH59B. In this report, we describe two new mAbs (BL1H7 and BA1C11) that react selectively with granulocytes, monocytes and macrophages. These monoclonal antibodies (mAbs) recognize a molecule in the range of 90-115 kDa in immunoprecipitation and/or Western blotting analyses. Two-colour FACS analyses showed that the distribution of BL1H7 and BA1C11 antigens was identical to that of SWC3. Moreover, in this assay, mAb 74-22-15 appeared to partially block the binding of mAbs BL1H7 and BA1C11, suggesting that all these mAbs reacted with the same or spatially close epitopes. Cross-blocking analyses indicated that it was the case with mAbs 74-22-15 and BL1H7. Immunoprecipitation experiments with mAbs 74-22-15, BL1H7 and BA1C11, followed by immunoblotting with mAb BL1H7 confirmed that all three mAbs recognize the same molecule. Analysis of the N-terminal sequence carried out on the affinity purified protein revealed homology with members of signal regulatory protein (SIRP) family. Like other members of this family, after treatment with sodium pervanadate, SWC3 became phosphorylated in tyrosines, and associated with the protein-tyrosine phosphatase SHP-1.

Animals↗
PubMed1988

An anti-human-T-cell monoclonal antibody with specificity for a novel determinant.

A new antihuman T cell monoclonal antibody, MAb 22, recognizes an antigen that is present on all mature T cells, but detected on only a subset of thymocytes. Dual color flow microfluorimetry (FMF) demonstrates that MAb 22 staining has concordant distribution with pan-T MAb specific for CD3 and CD5 and includes the CD4 and CD8 subsets; other FMF studies confirm T cell specificity of MAb 22 expression by cells of hematopoietic origin. The antigen recognized by MAb 22 is expressed on only a subset of thymocytes and by dual FMF is expressed at a mature thymocyte stage. Immunoprecipitation by MAb 22 demonstrates a series of molecules with a predominant 45 KD protein and associated 12 and 95 KD proteins under reducing conditions, while a 92 KD protein predominates under nonreducing conditions. Comparisons of expression on a variety of T cell lines, including a mutant line defective in the expression of the T cell receptor, by FMF analysis further distinguishes the determinant recognized by MAb 22 from those detected by MAb of defined T cell specificity.

Antigens, Differentiation↗
PubMed1976

A hepatic receptor of avian origin capable of binding specifically modified glycoproteins.

Evidence is reported to support the following conclusions: (i) The presence of a specific hepatic receptor capable of recognizing and binding galactose-terminated glycoproteins is responsible for maintaining near zero levels of circulating asialoglycoproteins in mammalian serum. (ii) The absence of this galactose-specific binding protein in avian, and presumably reptilian, liver is correlated with high levels of circulating asialoglycoproteins in the serum of these species. (iii) The evolutionary significance of these observations is reinforced by the recognition of an avian hepatic binding protein specific for terminal, N-acetyl-glucosamine residues on glycoproteins.

Acetylglucosamine↗
PubMedDate not supplied

Medicare beneficiaries' costs of care in the last year of life.

This paper profiles Medicare beneficiaries' costs for care in the last year of life. About one-quarter of Medicare outlays are for the last year of life, unchanged from twenty years ago. Costs reflect care for multiple severe illnesses typically present near death. Thirty-eight percent of beneficiaries have some nursing home stay in the year of their death; hospice is now used by half of Medicare cancer decedents and 19 percent of Medicare decedents overall. African Americans have much higher end-of-life costs than others have, an unexpected finding in light of their generally lower health care spending.

Aged↗