Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.1.4.3 (
phospholipase C
)
18,461
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The subcellular localization of
GPI-80
, a novel, adhesion-regulating protein, was investigated in human neutrophils. Surface expression of
GPI-80
was determined by FACS analysis as well as by the ability for
phospholipase C
to cleave the protein from the cell surface. Increasing amounts of
GPI-80
were exposed on the cell surface after weak stimulation with the chemoattractant fMLF, suggesting that the protein can be translocated to the plasma membrane from intracellular stores. By subcellular fractionation of the neutrophils,
GPI-80
was defined as a component of a light membrane fraction, containing secretory vesicles and plasma membranes, and it was absent from the neutrophil granule fractions. Separation of the plasma membranes from the secretory vesicles by flotation gradient fractionation confirmed that the
GPI-80
was localized in the mobilizable secretory vesicles by approximately 50%, and the rest was plasma membrane-bound. Thus, we identify secretory vesicles as the reservoir of
GPI-80
from which it may translocate to the plasma membrane after weak stimulation of the cells.
...
PMID:Neutrophil secretory vesicles are the intracellular reservoir for GPI-80, a protein with adhesion-regulating potential. 1120 68
We have previously cloned a glycosylphosphatidyl inositol (GPI)-anchored protein, designated
GPI-80
that associated with integrin and may modulate leukocyte adherence and migration. Recent studies have shown that
GPI-80
belongs to a Vanin family that is related to pantetheinase, but the regulatory function of
GPI-80
in cell adherence is still unclear. To clarify the possible functions of
GPI-80
, we transfected
GPI-80
cDNA into Chinese hamster ovary (CHO) cells and observed adherence and morphological changes. Adherence of
GPI-80
transfectants was significantly decreased when signal strength for the cell adhesion is weak, and the cell spreading of the transfectants was strongly inhibited. This inhibitory effect of
GPI-80
expression was largely canceled by
GPI-80
shedding with phosphatidy-linositol-specific
phospholipase C
. Interestingly, spreading of
GPI-80
transfectants was temporarily recovered from the round shape but not maintained by stimulation with known activators of beta1 integrins, phorbol myristate acetate and manganese ions. Taken together, these results suggest that the expression of
GPI-80
on CHO cells can influence cell spreading in weak adhesive signal conditions via extracellular matrix molecules.
...
PMID:Inhibition of cell spreading in CHO cells transfected with cDNA of a glycosylphosphatidyl inositol-anchored protein, GPI-80. 1607 29
