Monoclonal antibodies directed against extracellular matrix proteins reduce the adherence of Candida albicans to HEp-2 cells

The presence of the extracellular matrix (ECM) proteins collagen types I and IV, laminin and fibronectin on the surface of HEp-2 cells was confirmed by flow cytometry using monoclonal antibodies. Monoclonal antibodies directed against these ECM proteins reduced the adherence of C. albicans ATCC 44990 to HEp-2 cells, the greatest reductions being evident in assays which incorporated anti-collagen type IV monoclonal antibody. The ability of sugaramines to inhibit the adherence of C. albicans to a variety of cell types has been demonstrated previously and the most significant reduction in C. albicans – HEp-2 adherence was in assays which incorporated 0.2M galactosamine. The combination of anti-collagen IV monoclonal antibody and galactosamine reduced the adherence of C. albicans to HEp-2 cells by approximately 70% (p < 0.05). This revised version was published online in June 2006 with corrections to the Cover Date.     

Production of autostimulatory growth factors by the human carcinoma line,RPMI 2650

Summary The human carcinoma line RPMI 2650 produces autocrine factors; they are detected by the ability of RPMI 2650 conditioned medium (CM) to stimulate growth in soft agar of RPMI 2650 cells plated at low density. The autocrine activity in crude CM can be fractionated by ultrafiltration into a lower molecular weight (MW) fraction (R1–30), which concentrates molecules in the 1000–30 000 Da range; and a higher MW fraction (R30) with molecules greater than 30 000 Da in a more concentrated form. R1–30 is labile to acid, base, and heat treatment, whereas R30 is stable to (and sometimes activated by) these treatments. Boiling of R30, however, renders it labile to acid, base, and trypsin treatments. CM can be separated into a weakly heparin-binding fraction (with stability properties similar, but not identical, to R1–30), and a non-heparin binding fraction (with stability properties similar to R30). RPMI 2650 cells secrete transforming growth factor (TGF)α- and TGFβ-like molecules, but the R1–30 fraction can be distinguished from these TGFs, and from most other known growth factors, by its unusual combination of acid lability and weak affinity for heparin. Since the R30/non-heparin binding fraction is rendered labile by boiling or acid treatment, it may represent a bound or conformationally stable form of a growth factor.