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Biomedical subjects

M E Gilmartin

Publications and source records attributed to M E Gilmartin.

16 recordsLinked to original sources
PubMed1996

Body ventilators. Equipment and techniques.

Body ventilators have been used since the late 1800s and are still used today. This article reviews all of the body ventilators available today including tanks, cuirasses, wraps, rocking beds, and intermittent abdominal pressure ventilators. Diaphragm pacers and glossopharyngeal breathing also are reviewed. Clinical application of the ventilators, initiation, patient monitoring, and follow-up are reviewed.

Equipment Design↗
PubMed1990

Mechanical ventilation in the home.

Despite advances in the application of mechanical ventilation as a short-term, life-saving technique, intensive care units are increasingly faced with patients who cannot be weaned from ventilatory assistance and who require mechanical ventilation as a long-term, life-supporting necessity. Because of limited resources in health care facilities for the management of chronic ventilator-assisted individuals, home care has become an important option. With careful selection of appropriate candidates, home care for ventilator-assisted individuals can result in not only decreased respiratory symptoms, reduction in hospitalization, and improved physiologic measures, but also an improved quality of life with substantial survival and a reduction in the costs of medical care.

Home Care Services↗
PubMed1986

Rehabilitation and home care for ventilator-assisted individuals.

An increasing number of patients with chronic irreversible respiratory disorders are receiving mechanical ventilation in the home. Rehabilitation prior to hospital discharge allows improved independence and mobility in the home for these individuals.

Home Care Services↗
PubMed1986

Pulmonary rehabilitation. Patient and family education.

Patient and family education is essential in all settings, not only the rehabilitative setting. The patient may be in a variety of settings: the intensive care unit, a general medical or surgical unit, an outpatient clinic, or at home. The health care professional will need to determine what the patient has to learn. Teaching can be done by all members of the multidisciplinary team, and the education that has been completed should be communicated to other members through a good record keeping system. It can never be assumed that the patient already knows something. For example, many patients who have been taking medication for months or years do not really understand the expected beneficial effect or the side effects, and often patients are reluctant to ask questions concerning their treatment. The goal of patient education is to help patients take more responsibility for their self-care and to help them cope with changes that have taken place in their physical and functional status. It has been shown that when patients' involvement in the learning process is maximized, their ability to make decisions and take actions that increase their coping mechanisms is enhanced. Teaching is a never-ending process and may need repetition and reemphasis as the patient's condition changes and for the remainder of the relationship between the health professional and the patient and family. The learner's individuality must be respected and teaching must be adapted to meet individual patient needs. Patient and family education is a challenge to all health care professionals, but one that must be undertaken in an attempt to meet all of the individual's needs.

Family↗
PubMed1985

Three expressed sequences within the human beta-tubulin multigene family each define a distinct isotype.

This paper describes the isolation and complete sequence of a novel expressed human beta-tubulin gene (beta 2). The sequence is compared with that of two other expressed human beta-tubulin genes (M40 and 5 beta). All are encoded by four exons. Though the boundaries of each exon are absolutely conserved among the three genes, the intervening sequences differ considerably in size and sequence content. Two of the genes (M40 and 5 beta) contain one (M40) or ten (5 beta) members of the middle repetitive Alu family sequences within one of their intervening sequences. Comparison of the amino acid sequences encoded by each gene reveals a high level of homology overall, though there is significant divergence between the carboxy termini of two of the genes. The pattern of expression of each beta-tubulin gene has been studied in several different human cell lines using unique non-crosshybridizing probes derived from the 3' untranslated regions. Two of the genes, M40 and beta 2, are expressed at varying levels in all of the cell lines examined, though the level of expression of one of these genes parallels the other in most cases. The third gene, 5 beta, is detectably expressed only in cells of neural origin. Thus, distinct human beta-tubulin isotypes are encoded by genes whose exon size and number has been conserved evolutionarily, but whose pattern of expression may be regulated either co-ordinately or uniquely. Of the approximately 15 sequences contained in the human beta-tubulin multigene family, nine have now been sequenced fully. The overall composition of the multigene family and the evolutionary relationships among its various members are discussed.

Amino Acid Sequence↗
PubMed1984

Dual regulation of intermediate filament phosphorylation.

Intermediate filament proteins have been isolated from ME-180, cells of a human cervical carcinoma. Eight of these proteins have been identified as keratins by immunologic cross-reactivity to antibodies raised against authentic human epidermal keratins. The ME-180 keratin proteins consist of two major subunits designated MEK-1 and MEK-2 with approximate molecular weights of 58,000 and 53,000, respectively, and six minor subunits of 59, 57, 52.5, 50.5, 45, and 40 kilodaltons. When ME-180 cells were incubated for 2-24 h in the presence of [32P]orthophosphate, MEK-1 and MEK-2 as well as the 52.5- and 40-kilodalton keratins were phosphorylated at their serine residues. V8 protease digests revealed that phosphorylation of MEK-2 is restricted to one peptide representing approximately half the molecule. Regulation of MEK-1 and MEK-2 phosphorylation has been studied by prelabeling the cells for 2 h in 32P-labeled medium. This was followed by up to 2 h of continued incubation in the same medium after the addition of a variety of perturbing agents. The phosphorylation of MEK-2 increased in the presence of 10(-4) M dibutyryl cyclic AMP (twofold), 1 mM methylisobutylxanthine (2.5-fold), 10(-5) M isoproterenol (fivefold), and 10(-9) M cholera toxin (sevenfold). In contrast, MEK-1 phosphorylation was unaffected by these agents. Neither cyclic GMP, Ca++, hydrocortisone, nor epidermal growth factor had any effect on the phosphorylation of MEK-1 or MEK-2. The results indicate that the phosphorylation of these two keratins is independently controlled by cyclic AMP-dependent kinase for MEK-2 and by cyclic nucleotide-independent kinase for MEK-1. The observed differences in control suggest distinct functions for MEK-1 and MEK-2 within the cytoskeletal network.

Cells, Cultured↗
PubMed1980

Phosphorylation of epidermal keratins.

When human and rat epidermis are exposed to 32P-orthophosphoric acid, labeled phosphate is incorporated into several proteins. The pattern of phosphorylation is identical whether the isotope is delivered in vivo or in vitro. The predominant phosphorylated proteins are insoluble in Tris-HCl buffer but soluble in SDS-beta-mercaptoethanol. They migrate in SDS-polyacrylamide gels with apparent molecular weights between 45,000 and 65,000. When analyzed by two-dimensional gel electrophoresis, the labeled phosphoproteins co-migrate with keratins isolated from human callus. Serine is the phosphate acceptor in these proteins. The pattern of phosphorylation of these SDS-beta-mercaptoethanol soluble epidermal proteins is not changed in basal cell carcinoma, icthyosis vulgaris, Kyrle's disease or Netherton's syndrome. The pattern is altered in psoriasis. Others have demonstrated that a 63,000 molecular weight protein is absent from active psoriatic lesions. We have found that a 63,000 molecular weight phosphoprotein is present in uninvolved skin but absent in the psoriatic plaques.

Animals↗
PubMed1980

Control of epidermal and hair root protein synthesis.

Within the past several years, studies of protein synthesis in a variety of systems have focused upon translational control and post-translational modification. In parallel, the specific studies of keratin biosynthesis in tissues of epithelial origin have been directed at these same areas. Multiple proteins which effect positive and negative control over formation of the 80S initiation complex have been identified in mammalian epidermis. The current status of studies of these proteins is reviewed in this presentation. In addition, we discuss our studies of epidermal messenger RNA. The mRNA for keratin has been identified in tissue of avian origin and, more recently, mRNA has been isolated and partially purified from guinea pig epidermis. The messenger has a poly A-rich region and a sedimentation coefficient of approximately 18S. It codes for keratins in heterologous cell-free systems.

Cell-Free System↗
PubMed1977

Bleomycin: effects upon mammalian epidermal DNA synthesis.

The effects of bleomycin upon epithelial DNA synthesis have been evaluated in a keratinizing tissue culture line and following topical application on intact mouse epidermis. In both models, bleomycin inhibited epithelial DNA synthesis after prolonged exposure of the tissue to large doses of the polypeptide antibiotic. The effect is probably limited by the penetration of bleomycin through epithelial cell membranes. Inhibition of epidermal DNA synthesis was also observed in non-treated animals subjected to restraint and/or partial starvation. These conditions, which are commonly associated with studies of topical therapeutic agents, must, therefore, be carefully controlled.

Animals↗
PubMed1976

Mammalian epidermal protein synthesis: initiation factors.

There is a deficiency of initiation in protein-synthesizing systems prepared from mammalian epidermis. These systems do not respond to inhibitors of initiation although they remain sensitive to elongation inhibitors and exogenous ribonuclease. In spite of this deficiency of initiation, active protein factors which support initiation reactions are present in the potassium chloride extract of mammalian epidermal ribosomes. A factor corresponding to the reticulocyte factor IF-MP has been isolated. An inhibitor of initiation is also present in the epidermal KCl wash.

Animals↗
PubMed1975

Isolation and characterization of epidermal ribosomes.

The conditions required for isolation of ribosomal particles from guinea-pig epidermis and half-root cells have been studied. Density-gradient patterns of the ribosomes following isolation from either tissue under a wide variety of conditions are essentially the same. Monomeric ribosomes are the predominant species isolable although polymeric ribosomes and subunits can be identified. The density-gradient pattern is not related to runoff during preparation. Detergent extraction is required for maximal recovery of particles from epidermis or wax-epilated hair roots even without detergent. The yield of ribosomes from both epidermis and hair roots is greatest in buffers with potassium concentrations between 100 and 250mM. Yield is decreased in buffers with magnesium concentrations above 5mM. Activity in an in vitro amino acid-incorporating system is unaffected by potassium concentration and is highest at magnesium concentration of 3mM. Activity of epidermal ribosomes is inhibited by the wax-epilation method while hair root-cell ribosomes are equally active following preparation with either latex or wax. The isolated ribosomal particles are unstable at 4 degrees C.

Amino Acids↗
PubMed1975

Products of epidermal protein synthesis.

The products of epidermal protein synthesis in tissue slice and cell-free systems have been characterized by chromatographic, electrophoretic, and immunologic methods. Radiolabeled proteins of heterogeneous size are found in the supernatant and particulate fractions from both systems. The major labeled proteins in the supernatant fraction have molecular weights of approximately 43 000 and 65 000. The natively-insoluble proteins of the particulate fraction were solubilized either with desoxycholate or alkaline urea. Subsequent analysis of theses fractions yielded a labeled, high molecular weight, urea-soluble protein whose electrophoretic mobility was slower than that of the heavy chain of myosin. The immunologic reaction between the radiolabeled fraction and antibody raised against filamentous protein suggests that synthesis of proteins identical to epidermal filamentous protein occurs in the in vitro systems.

Animals↗