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the synaptic localization of APP (show APP Proteins), ADAM10, and BACE1 (show BACE Proteins) in the mouse cerebral cortex, was examined.
Pharmacological inhibition of ADAM10 reduces sEphrin-B2 levels in bronchoalveolar lavage and prevents lung fibrosis in mice. Consistent with the mouse data, ADAM10-sEphrin-B2 signaling is upregulated in fibroblasts from human subjects with idiopathic pulmonary fibrosis.
Xenoestrogens biphenol-A and nonylphenol stimulate the release of EGFR (show EGFR Proteins)-ligands by differentially activating ADAM17 (show ADAM17 Proteins) or ADAM10.
study confirms the importance of ICOSL (show ICOSLG Proteins) shedding in ICOS (show ICOS Proteins)/ICOSL (show ICOSLG Proteins) function and expression and it identifies ADAM10 as the most important sheddase for controlling ICOSL (show ICOSLG Proteins) levels
Tspan3 (show TSPAN3 Proteins) is a central endocytic membrane component regulating the expression of ADAM10, presenilin and the amyloid precursor protein (show APP Proteins).
these results show that ADAM10-Notch (show NOTCH1 Proteins) signaling in ovarian somatic cells governs the primordial follicle formation by controlling the development of ovarian pregranulosa cells.
Findings provide evidence that ADAM10, and not ADAM17 (show ADAM17 Proteins), is indispensable for proper retinal development as a regulator of NOTCH (show NOTCH1 Proteins) signaling.
this study shows that during positive selection in the spleen, B-cell receptor signaling causes immature type 1 transitional B cells to become receptive to Notch (show NOTCH1 Proteins) ligands via Taok3 (show TAOK3 Proteins)-mediated surface expression of ADAM10
Thus, Leda-1/Pianp (show C12orf53 Proteins) is constitutively processed by proprotein convertases, sheddases including MMPs and ADAM10/17 and intramembrane protease gamma-secretase.
ADAM10 was dispensable for alpha-toxin (show PLC Proteins)-dependent xenophagic targeting of S. aureus, whereas a role for alpha-toxin (show PLC Proteins) attack on the plasma membrane was confirmed.
therapies against ADAM10 and ADAM17 (show ADAM17 Proteins) may promote cancer stem cell migration away from the tumourigenic niche resulting in a differentiated phenotype that is more susceptible to treatment.
Presence of anti-ADAM10 auto-Antibodies seems to reflect the increased tumor expression of the immunogenic immature-ADAM10 in a group of Colorectal cancer patients, and is associated with a favourable prognosis in patients at stage III of the disease.
ADAM10 and ADAM17 (show ADAM17 Proteins) are the best characterized members of the ADAM (A Disintegrin and Metalloproteinase) - family of transmembrane proteases. Both are involved diverse physiological and pathophysiological processes.For ADAM17 (show ADAM17 Proteins) phosphatidylserine exposure is required to then induce its shedding function.
A better understanding of the regulatory mechanisms controlling the expression, subcellular localization and activity of ADAM10 will likely uncover suitable drug targets which will allow a more specific and fine-tuned modulation of its proteolytic activity
In the present study, the authors show that deletion of a triple serine (3S) motif (Ser (show SIGLEC1 Proteins)-359 to Ser (show SIGLEC1 Proteins)-361) adjacent to the cleavage site is sufficient to prevent IL-6R cleavage by ADAM17 (show ADAM17 Proteins), but not ADAM10. We find that the impaired shedding is caused by the reduced distance between the cleavage site and the plasma membrane.
Here, I review some of the proposed functions of ADAM10 associated with intestinal crypt homeostasis and tumorigenesis within the gastrointestinal tract in vivo.
Study reports the structure of the ADAM10 ectodomain, providing fundamental insights into how substrate selectivity and regulation of catalytic activity is achieved in this important representative of the ADAM family of metalloproteases.
Data suggest that ADAM10 associates directly with all members of a subgroup of tetraspanins having eight cysteines in the large extracellular domain ('TspanC8'): Tspan5 (show TSPAN5 Proteins), Tspan10, Tspan14, Tspan15 (show TSPAN15 Proteins), Tspan17, and Tspan33 (show TSPAN33 Proteins). [REVIEW]
Results found ADAM10 expression under the regulation of MIR (show MLXIP Proteins)-655 which binds the 3'-UTR of ADAM10 mediating the progression of hepatocellular carcinoma.
Data suggest that activation of the metalloproteinase ADAM10 by signal peptide peptidase-like 3 (SPPL3) triggered by mutant BRAF(V600E) was a critical transformation event.
A dramatic decline in ephrinB2 (show EFNB2 Proteins) protein levels on the absence of flotillin-1 (show FLOT1 Proteins) expression is specific, and is partly the result of an increased susceptibility to cleavage by the metalloprotease ADAM10.
significantly increased expression of ADAM10 in the ISR versus non-ISR segment in diabetic minipigs
Data show that ADAM10 and APLP2 (show APLP2 Proteins) are expressed in proximal tubule cells, and that ADAM10 activity has a pronounced effect on expression of specific brush-border proteins.
Intracellular trafficking of ADAM10 critically requires a novel sorting signal within its cytoplasmic domain.
N-glycosylation is crucial for ADAM10 processing and resistance to proteolysis, and results suggest that it is required for full-enzyme activity.
Members of the ADAM family are cell surface proteins with a unique structure possessing both potential adhesion and protease domains. This gene encodes and ADAM family member that cleaves many proteins including TNF-alpha and E-cadherin.
a disintegrin and metalloprotease domain 10a
, ADAM metallopeptidase domain 10
, disintegrin and metalloproteinase domain-containing protein 10
, ADAM10 metallopeptidase
, disintegrin and metalloproteinase domain-containing protein 10-like
, ADAM 10
, a disintegrin and metalloprotease domain (ADAM) 10
, a disintegrin and metalloprotease domain 10
, kuzbanian protein homolog
, mammalian disintegrin-metalloprotease
, a disintegrin and metalloproteinase domain 10
, a disintegrin and metallopeptidase domain 10
, myelin-associated metalloproteinase