Identification of different molecular forms of human airway lysozyme

Jacquot, Jacky; Benali, Rachid; Zahm, Jean‐Marie; Puchelle, Édith

doi:10.1016/0003-2697(87)90634-8

Cited by 3 publications

(2 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…4), an elution position required for the elucells. Evidence now indicates a strong connection bettion of human airway lysozyme [19]. The lysozyme ween cytoskeletal structures and protein synthesis and content in the 0.35 M NaCl fraction (3.0 pg/106 cells delivery in epithelial cells [25,26].…”

Section: Resultsmentioning

confidence: 99%

Modulation of albumin‐like protein and lysozyme production by bovine tracheal gland serous cells

et al. 1990

Self Cite

View full text Add to dashboard Cite

Bovine tracheal submucosal gland serous cells were cultured in medium supplemented with either 10% fetal calf serum or 2% Ultroser G, a commercial serum substitute for cell culture. The proteins synthesized and secreted into the culture medium during PsS]methionine pulse, chase and isoproterenol-stimulated periods were analyzed. Marked differences in the patterns of secretory radiolabeled proteins with M, values ranging from 15080 to 95000 were observed between pulse and chase media of cells cultured in fetal calf serum and Ultroser G. In the presence of Ultroser G, albumin-like protein production was inhibited 9596 as compared to cultures incubated with fetal calf serum. A bovine lysoxyme-type enzymatic activity was detected only in medium from stimulated cells cultured in Ultroser G. The results suggest that bovine tracheal serous cells synthesize different proteins according to the composition of culture medium and release certain proteins when adrenergically stimulated.

show abstract

Section: Resultsmentioning

confidence: 99%

Modulation of albumin‐like protein and lysozyme production by bovine tracheal gland serous cells

et al. 1990

Self Cite

View full text Add to dashboard Cite

show abstract

“…Lysozyme can also originate from leucocytes, present in high concentration when airways are infected by pathogenic bacteria (74]. Four enzymatically active lysozyme forms have been isolated and purified depending on whether lysozyme was purified from purulent secretions, non-purulent secretions from chronic bronchitic patients, or from normal tracheobronchial explants in organotypic culture [83]. Additional studies are needed to characterize .…”

Section: Antibacterial Componentsmentioning

confidence: 99%

Functions of proteins and lipids in airway secretions

Jacquot¹,

Hayem²,

Galabert³

1992

Eur Respir J

View full text Add to dashboard Cite

Proteins and lipids synthesized by airway secretory cells or transudated are active components in the protection of respiratory epithelium. Proteins and ions are involved in the control of mucus hydration. Secretory proteins, such as secretory immunoglobulin A (IgA), transferrin and lysozyme, participate in the airway antibacterial defence. Other biochemical components found in secretions, such as anti-inflammatory and antioxidant agents as well as antiproteases, contribute significantly to the protection of the underlying epithelium.

show abstract