Identification of the lysosomal membrane glycoprotein Lamp-1 as a receptor for type-1-fimbriated (mannose-specific) Escherichia coli.

• The presence of several glycosylated sites with high-mannose oligosaccharides on the lysosome-associated membrane glycoproteins (Lamps)_ combined with the fact that neutrophil Lamps are present in mobilizable organelles inspired us to investigate their ability to bind type-1 fimbriated (mannose-binding) Escherichia coli and subsequently define a potential function for the Lamps in human neutrophils. Bacterial binding to Lamps purified from chronic myeloic leukemia cells was investigated by separation of the proteins by sodium dodecyl sulfate polyacrylamide gel electrophoresis, transfer to a blotting membrane and overlay with type-1-fimbriated bacteria. The overlays were developed by growth. The bacteria bound readily to Lamp-1 while there was almost no binding to Lamp-2. Hence, we state that a possible function for neutrophil Lamp-1 is bacterial binding.

Ämnesord

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Immunologi inom det medicinska området (hsv//swe)

MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Immunology in the medical area (hsv//eng)

Nyckelord

Antigens

CD

isolation & purification

physiology

Bacterial Adhesion

Cell Membrane

metabolism

Electrophoresis

Polyacrylamide Gel

Escherichia coli

physiology

Fimbriae

Bacterial

physiology

Humans

Immunoblotting

Leukemia

Myelogenous

Chronic

BCR-ABL Positive

blood

Lysosome-Associated Membrane Glycoproteins

Lysosomes

metabolism

Mannose

Membrane Glycoproteins

isolation & purification

physiology

Molecular Weight

Neutrophils

physiology

Publikations- och innehållstyp

ref (ämneskategori)

art (ämneskategori)