Biomedical subjects
P C Anderson
Publications and source records attributed to P C Anderson.
Dermatology quiz (no.2). Loxosceles reclusa bite.
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Application of glacial acetic acid to penile skin.
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Loxoscelism threatening pregnancy: five cases.
Envenomation by the spider Loxosceles reclusa in five pregnant women proved to have no sustained adverse effects on mother or baby when managed conservatively only with low-dose prednisone. A striking toxic erythema of the skin, common with the bite of the spider, caused the greatest discomfort and concern for the patients but proved to be entirely tractable. No episodes of hemolysis, disorders of coagulation, or renal damage were discovered. There is no clinical evidence of any special risk during pregnancy in the event of loxoscelism.
Technology in dermatology: Meeting the challenge today and tomorrow. The Technology Congress Planning Committee.
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Morphology of peritoneal dialysis catheter tunnel: macroscopy and light microscopy.
There is scanty knowledge of the morphology of peritoneal dialysis catheter tunnels in humans, even though such knowledge may impact on peritoneal catheter design, implantation and postimplantation care. Past descriptions of catheter tunnels are based mainly on data from animal experiments. Based on these data, it has been assumed that epidermal spreading is inhibited by collagen fibers ingrown into the cuff. Our preliminary investigation indicated that this may not be the case in humans and led us to study catheter tunnel morphology in more detail. Eighteen catheter tunnels (2-5mm of tissue around the catheters) were removed in 17 peritoneal dialysis patients. The catheters were inserted 30 to 2013 days prior to removal (median 366 days). The catheters were removed electively or because of infectious or noninfectious complications. Contrary to the observations in animals, in only 1 case did epithelium extend to the cuff with only a minimal amount of granulation tissue present at the end of a 9 mm long sinus tract. In the remaining cases, the leading edge of the epithelium always met granulation tissue 1-14 mm from the exit, and the cuffs were found 8-33 mm from the exit. In tunnels older than 197 days, dense fibrous tissue was ingrown into the cuffs, and a dense fibrous capsule surrounded the cuff. The uninfected intercuff segment formed a pseudosheath, indistinguishable from a tendon sheath or synovial membrane. Infection in the catheter tunnel propagates through the part of the cuff adjacent to the tubing inside the capsule, suggesting that the cuff per se does not constitute a major barrier for spreading infection. This observation, by exclusion, infers that the beneficial role of an external cuff in decreasing exit infections is by providing firm anchorage of the catheter resulting in restriction of its piston like movement and thereby minimizing trauma and inward conveyance of outer sinus tract flora.
Personal computers: building better projects in medicine.
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Survey research, or debunking the Q-sort.
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Circinate plaques heralding juvenile chronic myelogenous leukemia.
Plaques of leukemia cutis were the first manifestation of juvenile chronic myelogenous leukemia in a 2-year-old. This is a rare and usually fatal form of childhood leukemia. Only three cases of leukemia cutis associated with juvenile chronic myelogenous leukemia have been published.
Loxoscelism and the history of the Missouri brown spider: a recollection of Dr. Joseph Flynn.
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Consensus sequences for early iodination and hormonogenesis in human thyroglobulin.
Thyroglobulin from a human goiter, containing four atoms of iodine/molecule (660,000 daltons), was iodinated with Na 125I and KI in vitro to achieve a net addition of either 2 or 7.8 atoms of iodine/molecule. After fractionation by high performance liquid chromatography, iodinated tryptic peptides from S-cyanoethylated 125I-thyroglobulin were purified, sequenced, characterized by [125I]iodoamino acid distribution, and localized within thyroglobulins primary structure based upon the published cDNA sequence, (Malthiery, Y., and Lissitsky, S. (1987) Eur. J. Biochem. 165, 491-498). The addition of 2 atoms of iodine/molecule of thyroglobulin produced iodotyrosyls at five principal sites, with no 125I-hormone formation. The addition of 7.8 atoms iodinated the same sites more heavily, produced iodotyrosyls at 10 additional sites, and formed iodothyronines at 5 sites. After addition of 2 atoms of iodine, tyrosyl 24 and 11% of thyroglobulins 125I, while tyrosyl 2572 had 24%, but with 7.8 added atoms of iodine, tyrosyl 24 had more of the thyroglobulins [125I]iodothyronine (36 versus 26%). Since tyrosyls 149, 866, and 1466 were iodinated early but did not form the inner rings of iodothyronines, they are attractive candidates for donors of outer iodothyronyl rings. The sequences around the iodotyrosyls fall into three consensus groups, as follows: 1) Glu/Asp-Tyr, associated with synthesis of thyroxine (residues 24, 2572, and 1309), or iodotyrosine (residues 2586 and 991); 2) Ser/Thr-Tyr-Ser, associated with synthesis of iodothyronine (residue 2765) and iodotyrosine (1466 and 883); and 3) Glu-X-Tyr, 7 of the remaining 8 iodotyrosyls occur in this sequence, and we found iodine incorporation at each place this sequence appears in the thyroglobulin molecule. Iodine has been found at homologues of most of these sites in thyroglobulins of other species. We conclude that the primary structure of thyroglobulin, and particularly these consensus sequences, have a major role in the formation of thyroid hormones and their iodinated precursors.
The hormonogenic sites of turtle thyroglobulin and their homology with those of mammals.
Thyroglobulin (Tg) from turtles previously injected with 125I was reduced, alkylated, and digested with trypsin. We purified the resultant peptides on HPLC columns, determined their amino acid sequences and the locations of [125I]T4 and [125I]T3 residues, and compared them with established sequences from humans, cows, rabbits, rats, and guinea pigs. We found five major T4 peptides, three of which were homologous with the major hormonogenic sites A, B, and D of mammalian Tg. Site A, the highly conserved major T4 site in mammals, had substitutions in three residues near the T4 residue and had much less of Tg's newly synthesized T4 than is found in mammalian Tg (25% in turtle vs. 44% in rabbit). Site B contained correspondingly more of Tg's new T4 (42% vs. 24% in rabbit). Turtle Tg contained little [125I]T3, and we did not find site C (Ser-T3/T4-Ser, the major T3 site in guinea pig and rabbit) in turtles, but did find Val-T4, a possible homolog. Site D was quantitatively less important than in mammals. The fifth turtle hormonogenic site, containing 12% of Tg's newly formed T4, had a tyrosyl residue substituted for the phenylalanine at residue 632 in the human sequence. We conclude that Tg's major hormonogenic sites are generally conserved across a considerable evolutionary distance, but that differences in primary structure occur and may contribute to changes in priority of hormone synthesis among these sites.
Thyrotropin alters the utilization of thyroglobulin's hormonogenic sites.
We injected rabbits and guinea pigs with bovine thyrotropin (TSH) daily for 3 days, while controls received saline. All animals received sodium [125I]iodide on the second day, and thyroglobulin was purified from the thyroids of each group by gel filtration. Hormonogenic tryptic peptides from each S-cyanoethylated thyroglobulin preparation were isolated by high performance liquid chromatography, and their amino acid sequences were determined, permitting their localization within the thyroglobulin polypeptide chain by comparison with cDNA-derived sequences from bovine and human thyroglobulins. Thyroglobulins from the saline-injected rabbits and guinea pigs contained the same four major hormonogenic sites, designated A-D, previously described (Dunn, J. T., Anderson, P. C., Fox, J. W., Fassler, C. A., Dunn, A. D., Hite, L. A., and Moore, R. C. (1987) J. Biol. Chem. 262, 16948-16952). In both species, sites A and C were the major loci for thyroxine and triiodothyronine, respectively. However, site D in the guinea pig had a greater ratio of [125I]thyroxine to [127I]thyroxine than did site A, whereas the reverse was true in the rabbit. TSH administration produced the following changes in thyroglobulins of both species, relative to controls: 1) an increase in the ratio of [125I]triiodothyronine to [125I] thyroxine (rabbit, 0.29 versus 0.17; guinea pig, 0.19 versus 0.08), with the increase in triiodothyronine principally at site C; 2) a marked increase in 125I/127I and in thyroxine formation at site D (14.1% of thyroglobulin's thyroxine versus 9.8% in rabbits, 24 versus 13% in guinea pigs); 3) a corresponding decrease in thyroxine formation at site A (33 versus 43% in rabbits, 30 versus 46% in guinea pigs); and 4) a sharp increase in conversion of thyroglobulin's N-terminal 125I-labeled approximately 20 kDa hormone-rich iodopeptide, which contains site A, to a 125I-labeled approximately 15-kDa (rabbit) or 125I-labeled approximately 13-kDa (guinea pig) form, reflecting probable peptide bond cleavage. Our results show that TSH alters both the structure of the thyroglobulin molecule and the priority of utilization of its hormonogenic sites. We conclude that these changes are important to TSH's enhancement of thyroid hormone synthesis.
Syphilis and AIDS.
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The sites of thyroid hormone formation in rabbit thyroglobulin.
Rabbit thyroglobulin (Tg) was labeled in vivo with 125I and purified by gel filtration. Separation by high performance liquid chromatography (HPLC) of tryptic digests of S-cyanoethylated Tg yielded four major iodothyronine-containing peaks, designated A, B, C, and D. These were further purified on HPLC and sequenced for identification of amino acid residues and for location of the iodothyronine by 125I counting. The published primary structure for bovine Tg, derived from cDNA sequencing of the Tg gene (Mercken, L., Simons, M.J., Swillens, S., Massaer, M., and Vassart, G. (1985) Nature 316, 647-651), permitted tentative location of the rabbit hormonogenic peptides within the Tg polypeptide chain. Site A, corresponding to bovine residue 5, contained 44% of Tgs [125I]T4 (thyroxine) and 25% of its [125I]T3 (triiodothyronine); its specific activity of iodine was higher than that for other sites, indicating priority of iodination. Site B, containing 24% of Tgs [125I]T4 and 18% of its [125I]T3, corresponded to bovine residue 2555. Site C, at the third residue from the C terminus (bovine residue 2748), was the major T3 site, accounting for over 50% of Tgs [125I]T3. The amino acid sequence around this site shows less homology among different animal species than do those flanking the other hormonogenic sites. Site D accounted for 17% of Tgs [125I]T4 and corresponded to bovine Tyr-1291, in the midportion of Tgs polypeptide chain. The three major T4-forming sites had the sequence Asp-Tyr (sites B and D) or Glu-Tyr (site A), while the sequence Ser-Tyr-Ser appeared to favor T3 synthesis (site C), suggesting an important influence of primary structure on hormonogenesis. We conclude that site A is the major T4-forming site and site C the major T3-forming one, but others are available and offer the opportunity for flexibility in meeting different demands for hormone formation.
Catheter infections during continuous peritoneal dialysis.
A typical tunnel infection is described in a patient receiving continuous ambulatory peritoneal dialysis. This complication of peritoneal dialysis is important to study and manage well because the infection leads to removal of the catheter and interruption of therapy. Most infections are due either to Staphylococcus aureus or to S. epidermidis.