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Biomedical subjects

M L Mason

Publications and source records attributed to M L Mason.

12 recordsLinked to original sources
PubMed1992

Who is providing ambulatory care to Medicaid beneficiaries with acquired immunodeficiency syndrome in New York State?

This study examined the number of ambulatory care providers treating individuals with the acquired immunodeficiency syndrome who were Medicaid beneficiaries in New York State in 1988 and examined the distribution of this care across various practice settings. The study population was identified retrospectively in the New York State Medical HIV/AIDS Research Data Base and included a cohort of 5535 individuals with the acquired immunodeficiency syndrome who were enrolled in Medicaid in 1988 for at least 6 months after being diagnosed as having the disease and who had at least one ambulatory care encounter during the year. Ambulatory care for the study group was provided by more than 700 hospital or freestanding clinics and more than 3000 private physicians in 1988. Many sites had low caseloads; 47% of the clinics and 68% of the physicians treating this population saw only one or two patients with the acquired immunodeficiency syndrome who were enrolled in Medicaid. More than half the patients in the study group were seen most frequently in clinics for their ambulatory care during 1988. These data provide reassurance that a wide network of providers is involved in the care of patients with the acquired immunodeficiency syndrome who are Medicaid beneficiaries in New York.

Acquired Immunodeficiency Syndrome↗
PubMed1991

A methodology for building an AIDS research file using Medicaid claims and administrative data bases.

There is a current and continuing need for health services research on the epidemiology of AIDS and its impact on health care systems. However, large data bases designed for other purposes, such as hospital discharge abstract systems and medical claims systems, are the primary source of data for AIDS research. Thus, methodologies must be developed that enable researchers to investigate AIDS using data bases designed for other purposes. In this report, we describe a methodology for utilizing Medicaid Management Information Systems (MMIS) data to conduct health services research on AIDS. We developed an ICD-9-CM diagnosis-based algorithm that accurately identified the majority of AIDS cases, both before and after AIDS-specific ICD-9-CM codes became available in October 1986. Using diagnostic categories that we had developed previously to identify AIDS cases among disabled young men in California on Medicaid, we expanded the methodology to include children, men, and women of all ages in California and New York. The algorithm worked best with young disabled males, older males, and females between 18 and 50 years of age. The algorithm worked least well with nondisabled males, females over age 50 years, and children. We also developed methodologies for defining Medicaid AIDS onset, risk group, and date of death. Our research resulted in the identification of a study population representing the majority of Medicaid AIDS cases between 1983 and 1986 in California and New York. The AIDS study population data base was used in further research on eligibility patterns, the epidemiology of the AIDS epidemic, lifetime Medicaid utilization and expenditures, and the development of a survival-based severity index for Medicaid recipients with AIDS.

Acquired Immunodeficiency Syndrome↗
PubMed1989

Three-dimensional structure of a fluorescein-Fab complex crystallized in 2-methyl-2,4-pentanediol.

The crystal structure of a fluorescein-Fab (4-4-20) complex was determined at 2.7 A resolution by molecular replacement methods. The starting model was the refined 2.7 A structure of unliganded Fab from an autoantibody (BV04-01) with specificity for single-stranded DNA. In the 4-4-20 complex fluorescein fits tightly into a relatively deep slot formed by a network of tryptophan and tyrosine side chains. The planar xanthonyl ring of the hapten is accommodated at the bottom of the slot while the phenylcarboxyl group interfaces with solvent. Tyrosine 37 (light chain) and tryptophan 33 (heavy chain) flank the xanthonyl group and tryptophan 101 (light chain) provides the floor of the combining site. Tyrosine 103 (heavy chain) is situated near the phenyl ring of the hapten and tyrosine 102 (heavy chain) forms part of the boundary of the slot. Histidine 31 and arginine 39 of the light chain are located in positions adjacent to the two enolic groups at opposite ends of the xanthonyl ring, and thus account for neutralization of one of two negative charges in the haptenic dianion. Formation of an enol-arginine ion pair in a region of low dielectric constant may account for an incremental increase in affinity of 2-3 orders of magnitude in the 4-4-20 molecule relative to other members of an idiotypic family of monoclonal antifluorescyl antibodies. The phenyl carboxyl group of fluorescein appears to be hydrogen bonded to the phenolic hydroxyl group of tyrosine 37 of the light chain. A molecule of 2-methyl-2,4-pentanediol (MPD), trapped in the interface of the variable domains just below the fluorescein binding site, may be partly responsible for the decrease in affinity for the hapten in MPD.

Antibodies, Monoclonal↗
PubMed1988

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

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-methyl-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 x 10(10) 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 Fab during crystallization trials. In PEG, the ligand remained firmly bound to the protein. The liganded Fab crystallized in the monoclinic space group P2(1) in PEG, with a = 58.6, b = 97.2, c = 44.5 A and beta = 95.2 degrees. In MPD the space group was triclinic P1, with a = 58.3, b = 43.4, c = 42.3 A, alpha = 83.9 degrees, beta = 87.6 degrees, and gamma = 84.5 degrees. X-ray diffraction data were collected for both forms to 2.5-A resolution. Surprisingly, the triclinic form of the liganed antifluorescyl Fab 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.

Animals↗
PubMed1985

Longitudinal gradients of collagen and elastin gene expression in the porcine aorta.

The physical and chemical properties of the mammalian aorta are known to vary as a function of distance from the heart. These properties are highly dependent collagen and elastic fibers. In order to evaluate the mechanisms which regulate the accumulation of these two connective tissue proteins, gene expression was evaluated at both the biosynthetic and messenger RNA levels. Short-term (3 h) explant cultures of the medial portion of four segments of the descending aorta in newborn pigs were incubated in the presence of [3H] proline. Collagen production was quantified by collagenase digestion and elastin production was determined by immunoprecipitation. Between the conus arteriosus and the bifurcation of the iliac arteries, relative collagen synthesis increased 2-fold (from 5.8 to 12.0% of total protein synthesis), while relative elastin synthesis declined 10-fold (from 16.4 to 1.6% of total protein synthesis). Similarly, collagen production increased more than 7-fold (from 6.7 to 49.8 X 10(3) molecules/cell/h) while elastin production was reduced more than 3-fold (from 71.8 to 21.0 X 10(3) molecules/cell/h) along this developmental gradient. Elastin synthesis appeared to be controlled to a significant extent by the availability of elastin mRNA, since both cell-free translation and molecular hybridization to a cloned elastin gene probe showed gradients of elastin gene expression. Similarly, collagen synthesis was apparently regulated, at least in part, by an inverse gradient of collagen mRNA, as measured with a cloned cDNA for the pro-alpha 1(I) collagen gene. Marked changes in the amount of non-elastin protein synthesis accompanied differentiation and accounted for larger changes in relative synthesis. These results suggest that the phenotype of the cells of the porcine artery wall is distinct in different regions of this organ at this developmental stage.

Aging↗
PubMed1984

Elastin mRNA levels during foetal development of sheep nuchal ligament and lung. Hybridization to complementary and cloned DNA.

Elastin mRNA levels were quantified in sheep nuchal ligament and lung during the latter half of foetal development with elastin-specific cDNA (complementary DNA) probes using both hybridization in solution (saturation analysis) and hybridization on a fixed support (Northern analysis). For the solution-hybridization studies, cDNA prepared from nuchal-ligament mRNA was enriched to 65% for elastin sequences by hybridizing it to its template at a R0t (mol X s X litre-1) value that included only the abundant class of mRNA sequences. Hybridization of this probe to RNA extracted from nuchal ligament between 70 and 138 days after conception demonstrated elastin sequences increased about 10-fold (from 0.047 to 0.438% of total RNA). In contrast, lung elastin mRNA levels increased only 3-fold (from 0.009 to 0.022% of total RNA) during the same period. Over this development period these values correspond to increases in the average number of elastin mRNA molecules from 950 to 20 000 molecules/ligament cell and from 130 to 330 molecules/lung cell. For Northern analysis, elastin mRNA was purified from near-term-sheep nuchal ligament on sucrose density gradients. Analysis of the translation products of this elastin mRNA showed that relative elastin precursor synthesis was at least 80% of total [3H]valine incorporation. The Mr of this elastin mRNA, determined by methylmercury-agarose-gel electrophoresis, was approx. 1.25 X 10(6). Northern hybridization of nuchal ligament and lung RNA to a [32P]cDNA probe, transcribed from this sucrose-gradient-purified elastin mRNA, confirmed the developmental changes in elastin mRNA levels detected by solution-hybridization techniques. The specificity of this method was confirmed by using a cloned elastin gene fragment. These studies demonstrate that elastin mRNA levels in organs such as nuchal ligament and lung increase with foetal development, but that there are significant differences in the average cellular elastin mRNA content of these two organs.

Animals↗