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Identification of neutrophil gelatinase-associated lipocalin as a novel
matrix protein of specific granules in human neutrophils
L Kjeldsen, DF Bainton, H Sengelov and N Borregaard
Department of Hematology, State University Hospital, Rigshospitalet,
Kobenhavn, Denmark.
Neutrophil gelatinase-associated lipocalin (NGAL) is a novel 25-kD protein
of human neutrophils, that is in part covalently complexed with neutrophil
gelatinase. However, both NGAL and gelatinase exist mainly in forms not
associated with each other. An explanation for this phenomenon might be
that the unassociated proteins reside in different subcellular
compartments. The aim of the present study was to determine the subcellular
localization of NGAL. An enzyme-linked immunosorbent assay (ELISA) for NGAL
was developed using specific anti-NGAL antibodies. The assay was applied on
subcellular fractions of neutrophils obtained after centrifugation of a
postnuclear supernatant on a two-layer Percoll gradient. The distribution
profile of NGAL was found to colocalize strictly with the distribution
profile of lactoferrin. This was confirmed by immunogold double-labeling of
frozen thin sections of neutrophils that showed a high degree of
colocalization of NGAL and lactoferrin, and by exocytosis experiments,
which showed lactoferrin, vitamin B12-binding protein, and NGAL to be
similarly released upon stimulation. Therefore, NGAL is a novel matrix
protein of specific granules and thus partly segregated from gelatinase,
the major part of which is located in a separate compartment, the
gelatinase granules. An ELISA specific for the NGAL/gelatinase complex was
developed and the subcellular distribution and release of this complex was
determined. The distribution and mobilization of the complex allowed us to
confirm the existence of differentially mobilized granule subpopulations
among peroxidase negative granules.
Volume 83,
Issue 3,
pp. 799-807,
02/01/1994
Copyright © 1994 by The American Society of Hematology
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