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Biomedical subjects

L C Haynes

Publications and source records attributed to L C Haynes.

5 recordsLinked to original sources
PubMed2001

What every nurse needs to know about nocturnal sleep-related eating disorder.

This article provides information about a bizarre pattern of eating while asleep called nocturnal sleep-related eating disorder. People with this disorder, which has begun to be studied only recently, demonstrate features of both a sleep disorder and an eating disorder. Many clients are reluctant to initiate discussions regarding this condition because of feelings of powerlessness and shame. Other clients do not discuss their symptoms because nurses and other clinicians fail to gather accurate assessment data due to lack of knowledge within the professional community regarding the disorder. This review includes the historical background, definition of terms, and clinical manifestations of nocturnal sleep-related eating. In addition, emphasis on assessment and clinical management are included. Safety issues, the need to educate health care providers, and the role of the nurse in advocating for appropriate diagnosis, treatment, and referral are addressed.

Anticonvulsants↗
PubMed2000

Depression, delirium, and dementia in the elderly patient.

Perioperative nurses commonly care for patients with changes in mental status, especially elderly patients. Three common mental status disorders in the elderly are delirium, depression, and dementia. Each of the disorders can have similar clinical presentations. Despite similarities, the appropriate nursing interventions may vary significantly. Interventions discussed in this article focus on the etiology of the presenting problem and the nursing interventions that will promote the most positive outcome for the patient.

Aged↗
PubMed1986

Sequentially labile water-soluble prodrugs of alprazolam.

A 1,4-benzodiazepine analogue alprazolam (1) undergoes ring-opening hydrolysis under acidic conditions to form a triazolobenzophenone (2). At a neutral pH, 2 rapidly and quantitatively cyclizes back to 1. This facile reversible reaction was utilized in developing water-soluble prodrugs of 1 in which the "solubility anchoring" acyl moieties are formyl, acetyl, succinyl, glycyl, leucyl, and gamma-aminobutyryl groups. These compounds were prepared directly from 2 and corresponding acids through DCC coupling in a 1:1 mixture of H2O and THF. They should be stable in aqueous media at room temperature. Promoieties used should be nontoxic at an intended dose level. In vitro human serum hydrolysis study showed that only glycyl and leucyl amides were able to regenerate 1 within a reasonable period of time. Ex vivo competitive receptor binding assay in mice with [3H]flunitrazepam indicated that leucyl amide prodrug should be able to produce a rapid onset of the intrinsic central nervous system activity of 1 when parenterally administered. For all compounds studied, the final outcome of the biological response appears to be kinetically controlled, rather than by an unfavorable equilibrium, particularly by the first step in which the amide bond is hydrolyzed in vivo.

Alprazolam↗
PubMed1985

Serum-catalyzed hydrolysis of metronidazole amino acid esters.

Glycine (Gly), alanine (Ala), valine (Val), leucine (Leu), isoleucine (Ile), phenylalanine (Phe), and lysine (Lys) esters of metronidazole were synthesized using dicyclohexylcarbodiimide (DCC) coupling or a mixed-anhydride route, using tert-butyloxycarbonyl (tert-Boc) amino acids. Human serum-catalyzed hydrolysis of these esters at 37 degrees C give half-lives varying from 4.5 min for the Phe ester to 96 h for the Ile ester. Also determined was the pH-rate profile for hydrolysis in aqueous buffers at 25 degrees C. A linear relationship was observed between the logarithmic value of the hydrolysis rate constant in serum and that of the OH- -catalyzed hydrolysis of cationic esters. This finding may indicate that the esters studied are "equally" poor substrates for binding to the enzymes in serum and, thus, the difference observed in the serum-catalyzed hydrolysis rate is solely derived from the chemical lability of an ester bond. Interestingly, the extent of chemical activation observed in the buffer system appears to be amplified in the serum-catalyzed hydrolysis.

Amino Acids↗