PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 7131931

Complement levels in human tears.

J Imanishi·F Takahashi·A Inatomi·H Tagami·T Yoshikawa·M Kondo
View original source ↗Export metadata ↓

Abstract

The single radial immunodiffusion technique was modified to determine tear complement component C3 with small sample volume. The C3 levels in the tears from 18 normal subjects and 42 patients with ocular diseases were determined using this method. In the normal subjects, the mean level of tear C3 was 5.12 mg per 100 ml. The physiological level of tear C3 was estimated to be less than 10 mg per 100 ml from the results in normal subjects and patients with noninflammatory ocular diseases. The cases of severe inflammatory diseases such as antiviral keratoconjunctivitis, herpetic keratitis and acute catarrhal conjunctivitis showed a high level of C3 in the tears. The C3 level was relatively low in the cases of mild inflammatory diseases such as allergic conjunctivitis. These results indicated that protein concentration of C3 in the tear was proportional to the severity of inflammation of the anterior ocular segment.

Explore related subjects

Complement C3ConjunctivitisEye DiseasesHumansHypersensitivityInflammationKeratitis, DendriticKeratoconjunctivitisProteinsTearsJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

J Imanishi, F Takahashi, A Inatomi, H Tagami, T Yoshikawa, M Kondo. 1982. Complement levels in human tears.. https://pubmed.ncbi.nlm.nih.gov/7131931/

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

KEEP EXPLORING

Related citations

PubMed1992

Spontaneous thioester bond formation in alpha 2-macroglobulin, C3 and C4.

Purified alpha 2-macroglobulin and complement proteins C3 and C4 were treated with ammonia to break their intramolecular thioester bonds and reform the original free cysteinyl and glutamyl side chains. When this reaction was performed at low temperature a conformational intermediate was trapped which lacked a thioester, but which could refold to the native structure and spontaneously reform the thioester and full biological function. The findings suggest that these proteins may undergo spontaneous post-translational self-modification forming the thioesters without involvement of enzymes or high energy metabolites such as ATP.

Complement C3↗
PubMed1992

Expression of complement components of the alternative pathway by glioma cell lines.

Glioma cell lines express proteins of the complement alternative pathway, namely C3, factor B, factor H, and factor I. Secretion of these proteins was shown by a sensitive and specific ELISA. C3 and factor H were rapidly secreted by glioma cell line CB193 and reached a concentration of 140 ng/ml/10(6) cells after 72 h of culture. Factor B and factor I were secreted at a lower rate and reached concentrations of 25 and 15 ng/ml/10(6) cells, respectively. Western blot and immunoprecipitation experiments showed that secreted proteins were identical to the corresponding plasma proteins. For factor H, besides the well known 150-kDa species, an additional polypeptide of 45 kDa with factor H immunoreactivity was observed. This species corresponded to the N-terminal truncated form found in plasma. In preliminary experiments, we observed control of these syntheses by cytokines. IL-1 beta significantly increased C3 secretion, with no effect on factor H. Secretion of factor H was enhanced by IFN-gamma. These results show that a glioma cell line could be a useful tool to study complement biosynthesis by glial cells in humans.

Complement C3↗