Biomedical subjects
Publications and source records attributed to D Gitlin.
85 of 217 clients who reported retrospectively that their intake therapist seemed confident of being helpful also reported cancelling and missing fewer follow-up sessions regardless of the length of treatment. Clients' reported confidence during the first session and clients' attendance at later sessions were also associated with three measures of satisfaction with individual therapy.
A Cell membrane fraction from term human placenta was prepared by homogenization and ultracentrifugation. The fraction was found to bind both human IgG and human serum albumin. Maximal specific binding occurred at pH 5.2, and the amount of binding was dependent upon incubation time, temperature, buffer, and ionic strength. The binding of human serum albumin was inhibited by preincubation with H-IgG but the reverse did not happen.
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Seven of 10 patients with visceral larva migrans (VLM) had serum precipitating antibodies specific for larval antigens of Toxocara canis as determined by double diffusion in agar. Such antibodies were absent in 114 normal adults and 25 patients with collagen disease. Precipitation of ascarid components by C-reactive protein resulted in false-positive reactions, but this precipitation was readily prevented by appropriate absorption of sera before testing. A more sensitive assay, the enzyme-linked immunosorbent assay, revealed high titers of antibodies to larvae of Toxocara in all patients with VLM; the log2 titer ranged from 9 to 14. Five of eight household relatives of these patients and four children who had had VLM two to four years before testing had titers of 6-12. Of the 114 normal adults, 105 had titers of 0-2; nine had titers of 3-8. Of the 25 patients with collagen disease, 23 had titers of 0, and two had titers of 4 and 6, respectively. Additional studies of those patients indicated that infection with Toxocara can be distinguished serologically from ascariasis, filariasis, and trichinellosis.
Specific plasma proteins were labeled with 131I, and their half-lives in lactating and nonlactating mice were determined. The proteins included mouse IgF and IgM, mouse, bovine, rabbit, and human IgG, human serum and salivary IgA, human transferrin and albumin, and mouse and human immunoglobin light chains. The rates at which these proteins are transferred across the mammary gland in mice suckling their young were calculated: transmammary protein transfer was found to be highly selective. The G-class immunoglobulins readily traversed the mammary gland, the rate being dependent on the IgG load presented to the transport system. Immunoglobulin lambda-chains and human serum IgA crossed the mammary gland even more rapidly than did the G immunoglobulins. Human IgA without secretory piece was transported into milk more rapidly than IgA with secretory piece attached. Protein transport across the mouse mammary gland was found to be similar to and yet different from protein transport across either the suckling mouse intestine or the mouse placenta as to which proteins crossed and at what relative rates.
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Human, rat, and mouse placentas and rat and mouse intestines were homogenized in buffered saline, and fraction consisting primarily of cell membranes was separated from each of the homogenates by differential centrifugation. Human, bovine, and guinea pig IgG, and human IgE, Bence-Jones protein, serum albumin, insulin, and growth hormone were labeled with (131)I or (125)I, and the binding of these proteins by the cell membrane fractions was investigated. Rat and mouse sucklings were given labeled proteins intragastrically, and the amount of each protein absorbed after a given interval of time was determined. It was found that the degree and specificity of protein binding by the cell membrane fractions from human and murine placentas strikingly paralleled the relative rate and specificity of protein transport from mother to fetus in the respective species at or near term. Similarly, the degree and specificity of protein binding by the cell membrane fractions from suckling rat and mouse intestines tended to parallel the rate and specificity of protein absorption from the gastrointestinal tract in these animals. However, some discordance between protein binding and protein transport was also observed. The data suggest that: (a) the binding of a protein by specific receptors on cell membranes may be a necessary first step in the transcellular transport of the protein; (b) specific protein binding by cell receptors does not ensure the transport of that protein across the tissue barrier; and (c) specific transport mechanisms other than or in addition to specific cell membrane receptors are involved in the active transport of proteins across the human or murine placenta or the suckling murine intestine.
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