Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: O95498 and P05107 Pubmed SVM Score :0.0
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Interacting proteins: O95498 and P05107 Pubmed SVM Score :0.0
GPI 80 cross linking induced up regulation of CD11b / CD18 ( Mac 1 ) expression on neutrophil surfaces and shedding of L selectin , which depends on tyrosine phosphorylation and cytoskeleton remodeling . ^^^
Interacting proteins: O95498 and P05107 Pubmed SVM Score :0.0
To clarify the mechanisms by which GPI 80 functions on leukocytes , we explored the possibility of its physical association with beta 2 integrin which is important for leukocyte adherence , locomotion , and extravasation . beta 2 integrin , detected by anti CD 18 mAb , was coprecipitated with GPI 80 from human neutrophil lysates by a mAb to GPI 80 . ^^^ In addition , GPI 80 was immunoprecipitated from human neutrophil lysates by anti human CD 18 mAb . ^^^
Interacting proteins: O95498 and P05107 Pubmed SVM Score :0.0
In addition , TNF alpha induced GPI 80 release was inhibited by blocking monoclonal antibodies specific to components of Mac 1 ( CD11b and CD 18 ) . 4 Antioxidants ( pyrrolidine dithiocarbamate and N acetyl L cysteine ) inhibited GPI 80 release by TNF alpha stimulation , but superoxide dismutase did not . ^^^
Interacting proteins: O95498 and P05107 Pubmed SVM Score :0.0
To investigate the physiological role ( s ) of GPI 80 , we examined the topological relationship of GPI 80 and the beta 2 integrin subunit ( CD 18 ) on resting and migrating human neutrophils by confocal laser microscopy . ^^^ On resting neutrophils , GPI 80 was evenly distributed on the cell surface and was associated with CD 18 . ^^^ On the other hand , during the early phase of migration ( 5 30 minutes ) , GPI 80 was detected on cell bodies and also on pseudopodia , but CD 18 was detected only on cell bodies , where it was associated with GPI 80 . ^^^ In the late phase of migration ( 60 minutes ) , GPI 80 was detected only on pseudopodia and its association with CD 18 was hardly observed . ^^^