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Study provides accurate validation of functional CGRP receptor expression throughout the brainstem and the spinal cord of non-human primates: several areas in the brainstem were shown to express CLR and RAMP1 mRNA and protein
RAMP1-deficient mice with concanavalin A (ConA)-mediated hepatitis, characterized by severe liver injury accompanied by infiltration of immune cells and increased secretion of pro-inflammatory cytokines by Kupffer cells and splenic T cells, showed poor survival.
the cardiovascular response of Ramp1(-/-), Ramp2(+/-), Ramp3(-/-), Ramp1(-/-)/Ramp3(-/-) double-knockout (dKO), and Calcrl(+/-) mice to AM and CGRP were compared to wildtype mice.These results suggest that the hypotensive effect of AM is primarily mediated through the CLR/RAMP1 heterodimer, but that AM signaling via CLR/RAMP2 and CLR/RAMP3 also contributes to some hypotensive action.
RAMP1 signaling improves lymphedema and accelerates lymphangiogenesis associated with reduced recruitment of pro-inflammatory macrophages.
RAMP1 exerted mucosal protection in DSS-induced colitis via attenuation of recruitment of inflammatory cells and of pro-inflammatory cytokines.
Together, these data indicate that signaling through RAMP1 and CLR plays a role in mediating asthma pathology
multiple NKX3.1 binding sites were found in the RAMP1 locus in human prostate cancer cells and in the normal mouse prostate.
Data indicate that IL-17 production is suppressed in RAMP1-deficient mice in the experimental autoimmune encephalomyelitis (EAE) model and RAMP1-deficient mice are completely resistant to EAE.
Data indicate that the lack of an intact CGRP receptor component RAMP1 resulted in an increased recruitment and activation of neutrophils.
Data show that mechanical ventilation reduced the expression of receptor activity-modifying protein RAMP3, but not of intermedin (IMD), calcitonin receptor-like receptor (CRLR), and RAMP1 and RAMP2.
significantly diminished intestinal peristalsis was observed by the allergy induction in RAMP1-deficient mice compared with WT mice.
These findings suggest that RAMP1 may be a new therapeutic target to regulate CGRP-mediated effects during disease including pathophysiological states in which Ang II plays a major role.
Co-expression of RAMP1 and CRLR reconstituted a CGRP receptor that was able to activate the pheromone-signaling pathway with pharmacological properties similar to those observed previously in mammalian cells.
role in cell surface expression of CRLR/RAMP heterodimeric receptors
The mouse cDNA for RAMP1 was cloned and we examined the signal transduction mechanism through the CGRP receptor. mRAMP1 is a 148-amino acid single membrane-spanning protein with a short cytoplasmic portion.
These findings suggest that tissue specificity of RAMP-1 gene expression is mediated by a negative acting transcription factor that represses RAMP-1 gene expression in non-RAMP-1 expressing tissues.
These results indicate that CGRP signaling through CLR/RAMP1 receptors plays a crucial role in the regulation of both blood pressure by vascular relaxation and proinflammatory cytokine production from dendritic cells.
CTR is not only down regulated by signaling through the CTR but also by the peptides signaling through calcitonin receptor-like receptor, and receptor activity modifying proteins
These data suggest that hypersensitivity to CGRP could be a potential mechanism underlying central sensitization in migraine and point to CGRP-receptor antagonists as a possible therapy for other pain disorders.
structure of the human CGRP receptor in complex with CGRP and the Gs-protein heterotrimer at 3.3 A global resolution, determined by Volta phase-plate cryo-electron microscopy
T-A-T RAMP1 gene haplotype might have utility as a genetic marker for Essential Hypertension and that the RAMP1 gene may be associated with increased susceptibility to Essential Hypertension in a Japanese population.
Data suggest CGRP receptor (CGRPR) ECL2 (extracellular loop 2 domain) enables interaction with N-terminal residues of CGRP; this provides evidence for dual involvement of ECL2 in two-domain binding model of CGRP/CGRPR interaction; CGRPR is obligate heterodimer of CLR/RAMP1. (CGRP = calcitonin gene-related peptide; CLR = calcitonin receptor-like receptor; RAMP1 = receptor [calcitonin] activity modifying protein 1)
Evidence that DNA methylation at RAMP1 gene promoter plays a role in migraine was described.
RAMP1 rs7590387 has a role in the transformation of episodic migraine into medication overuse headache.
Data suggest that ligand binding of a G protein-coupled receptor (GPCR) may inform drug development targeting calcitonin receptor-like receptor (CLR):receptor activity-modifying proteins RAMP1/2 complexes.
A novel functional role for RAMP1 in regulation of CaSR signalling in addition to its known role in receptor trafficking, is reported.
RAMP1 overexpression enhances the promoting effect that exogenous CGRP has on osteogenic differentiation
No significant association of the tested SNPs of the RAMP1 gene were found with migraine susceptibility.
CLR and RAMP1 co-localize in the enteric nervous system of human stomach, ileum, and colon, and are in close proximity to their ligands CGRP and IMD
The present finding demonstrated that RAMP1 immunoreactivity was localized in many neurons and phenopalatine ganglion.
lower expression in bronchial biopsies from subjects with asthma
The T-A-C haplotype is a genetic marker for cerebral infarction, and RAMP1 is associated with increased susceptibility to cerebral infarction.
These data for the first time pinpoint a specific RAMP1 residue important for both antagonist and agonist potency and are consistent with the N-terminal domain of RAMP1 forming the binding pocket interface with calcitonin receptor-like receptor.
RAMP1 overexpression attenuates Ang-II-induced hypertension and induces a protective change in cardiovascular autonomic regulation
Receptor activity modifying proteins interaction with human and porcine calcitonin receptor-like receptor (CRLR) in HEK-293 cells
Receptor activity-modifying protein 1 determines the species selectivity of non-peptide CGRP receptor antagonists.
The CGRP receptor components, RAMP1 and CRLR, are down-regulated during myeloid differentiation of CD34+ cells, and CGRP receptor selectively promotes the development of CFU-GM.
The protein encoded by this gene is a member of the RAMP family of single-transmembrane-domain proteins, called receptor (calcitonin) activity modifying proteins (RAMPs). RAMPs are type I transmembrane proteins with an extracellular N terminus and a cytoplasmic C terminus. RAMPs are required to transport calcitonin-receptor-like receptor (CRLR) to the plasma membrane. CRLR, a receptor with seven transmembrane domains, can function as either a calcitonin-gene-related peptide (CGRP) receptor or an adrenomedullin receptor, depending on which members of the RAMP family are expressed. In the presence of this (RAMP1) protein, CRLR functions as a CGRP receptor. The RAMP1 protein is involved in the terminal glycosylation, maturation, and presentation of the CGRP receptor to the cell surface.
receptor (calcitonin) activity modifying protein 1
, receptor activity-modifying protein 1
, receptor activity modifying protein 1
, receptor (G protein-coupled) activity modifying protein 1
, CRLR activity-modifying protein 1
, calcitonin receptor-like receptor activity modifying protein 1
, calcitonin-receptor-like receptor activity-modifying protein 1