Increased soluble VCAM-1 serum levels in preeclampsia are not correlated to urinary excretion or circadian blood pressure rhythm.

Objective: Soluble vascular cell adhesion molecule-1 (VCAM-1) is known to be elevated in serum of patients with preeclampsia, but there are no data available on the significance of urinary VCAM-1 excretion in preeclampsia. The aim of our study was to uncover possible circadian rhythms of VCAM-1 plasma levels and urinary VCAM-1 excretion in uncomplicated and hypertensive pregnancies and to ascertain their relation to blood pressure.

Study Design: A total of 10 normotensive and 10 preeclamptic pregnant women were included in this study.

Protegrin structure and activity against Neisseria gonorrhoeae.

Protegrin 1 (PG-1) is a broad-spectrum antimicrobial peptide that contains 18 amino acid residues (RG GRLCYCRRRFCVCVGR) and has two intramolecular cystine disulfide bonds. To determine the minimal structure responsible for protegrin-mediated activity against Neisseria gonorrhoeae, we synthesized 15 protegrin variants and tested them against two well-characterized gonococcal strains. The MICs of PG-1 were 0.

Clavanins, alpha-helical antimicrobial peptides from tunicate hemocytes.

Hemocytes from the invertebrate Styela clava, a solitary tunicate, contained a family of four alpha-helical antimicrobial peptides that were purified, sequenced and named clavanins A, B, C and D. Each clavanin contained 23 amino acid residues and was C-terminally amidated. The tunicate peptides resembled magainins in size, primary sequence and antibacterial activity.

Protegrins: structural requirements for inactivating elementary bodies of Chlamydia trachomatis.

We tested 20 protegrins against Chlamydia trachomatis serovar L2 (L2/434/Bu). Five of the protegrins had native structures; the others included nonamidated, enantiomeric, and truncated variants and peptides with <2 disulfide bonds. Antichlamydial activity resided principally in residues 5 to 15 of native protegrin PG-1, and optimal activity required both intramolecular disulfide bonds.