PubMed Health⌕ Search

PubMed · 8288946

Complement in human reproduction: activation and control.

Abstract

The behaviour of the complement system during human reproduction is now the focus of much scientific attention. The presence of antisperm antibodies in the reproductive tracts of some infertile individuals, and of complement in cervical and ovarian follicular fluid, suggests that complement-mediated damage of spermatozoa is involved in some cases of infertility. Further, deposition of maternal IgG and of complement in the extrafetal tissues indicates that complement activation occurs within the fetoplacental unit. Recently, three complement-regulatory proteins--decay-accelerating factor, membrane cofactor protein and CD59--have been detected on spermatozoa and in the extrafetal tissues. It is likely that these inhibitors are essential for normal reproductive function. This article reviews current understanding of the interaction of the complement system with cells and tissues involved in reproduction, with emphasis on the nature and function of the controlling proteins.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

I A Rooney, T J Oglesby, J P Atkinson. 1993. Complement in human reproduction: activation and control.. https://doi.org/10.1007/bf02918258

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

C3 activation is inhibited by analogs of compstatin but not by serine protease inhibitors or peptidyl alpha-ketoheterocycles.

C3 convertase is a key enzyme in the complement cascade and is an attractive therapeutic target for drug design. Recent studies have demonstrated that this enzyme is inhibited by compstatin (Morikis, D. , Assa-Munt, N., Sahu, A., Lambris, J.D., 1998. Solution structure of Compstatin, a potent complement inhibitor. Protein Sci. (7) 619-627; Sahu, A., Kay, B.K., Lambris, J.D., 1996. Inhibition of human complement by a C3-binding peptide isolated from a phage-displayed random peptide library. J. Immunol. (157) 884-891), a 13 amino acid cyclic peptide that binds to C3. Since the enzyme exhibits some homology to serine proteases, substrate-based design could be another avenue for drug design. In this study, we confirm the activity of compstatin using different sources of enzyme and different assay systems. We also tested the activity of substituted compstatin analogs and compared the selectivity and toxicity of these compounds to peptidyl alpha-ketoheterocyclic compounds. Our work confirms the activity of compstatin in both alternative and classical complement pathways, describes 11 new active analogs of this cyclic peptide, and provides evidence for key segments of the peptide for activity. Compstatin and related active analogs showed little or no inhibition of clotting or key enzymes in the clotting cascade nor did they appear to have significant cytotoxicity. The characteristics of compstatin suggest that this peptide and its analogs could be attractive candidates for further clinical development. By contrast, known serine protease inhibitors, including peptidyl alpha-ketoheterocycles, did not inhibit C3 convertase illustrating the atypical nature of this enzyme.

Complement Activation↗

An ethnopharmacological study on common privet (Ligustrum vulgare) and phillyrea (Phillyrea latifolia).

Ligustrum vulgare and Phillyrea latifolia leaves were well known in the Mediterranean historical medicine for their oropharyngeal anti-inflammatory effects. At the present time a popular phytotheraputical use of these species remains only in a few isolated southern European areas. Phytochemical and phytopharmacological studies of the methanolic extractives of their leaves were carried out. Flavonoidic fractions as well as different isolates, apigenin and luteolin derivatives showed significant in vitro complement inhibiting effects on the classical pathway of the complement system. A possible phytoceutical utilisation of the aerial parts of these species could represent (especially regarding the genus Phillyrea) an interesting perspective for many semi-arid Mediterranean regions.

Complement Activation↗