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The AM-RAMP2 system exerts crucial vasoprotective effects after vascular injury and could be a therapeutic target for the treatment of vascular diseases.
Results provide in vivo evidence of a role for RAMP2 in placental development distinct from the RAMP2-calcitonin receptor-like receptor (show CALCRL Proteins)/adrenomedullin (show ADM Proteins) signaling paradigm; decreases Pthr1 (show PTH1R Proteins) expression and causes a blunted response to systemic parathyroid hormone (show PTH Proteins); and identify additional pathways underlying the endocrine and fertility defects of the previously characterized Ramp2 heterozygous adult females.
the Adrenomedullin (show ADM Proteins)-RAMP2 system regulates vascular integrity, whereas RAMP2 deletion promotes vascular permeability
RAMP2 is essential for early vascular development and knockout-mice die in utero.
These results indicate the AM-RAMP2 system works to protect nerve cells from both acute and chronic cerebral ischemia by maintaining cerebral blood flow suppressing oxidative stress, and in the case of chronic ischemia, enhancing capillary growth.
The AM-RAMP2 system is a key determinant of vascular integrity and homeostasis from prenatal stages through adulthood.
These data demonstrate that the adrenomedullin (show ADM Proteins)-RAMP2 system is essential for cardiac metabolism and homeostasis.
Data show that mechanical ventilation reduced the expression of receptor activity-modifying protein RAMP3 (show RAMP3 Proteins), but not of intermedin (IMD (show ADM2 Proteins)), calcitonin receptor-like receptor (CRLR (show CALCRL Proteins)), and RAMP1 (show RAMP1 Proteins) and RAMP2.
Adrenomedullin (show ADM Proteins)-RAMP2 system is the potential target for the induction of liver sinusoidal endothelial cells.
this work reveals an essential role for RAMP2 in endocrine physiology and provides the first in vivo evidence for a physiological role of RAMP2 beyond that of AM/CLR (show CALCR Proteins) signaling
This work suggests that RAMP2 may modify the agonist activity and trafficking of the GCGR (show GCGR Proteins), with potential relevance to production of new peptide analogs with selective agonist activities.
Data suggest that a single GlcNAc residue at CTR (show CALCR Proteins) N130 (asparagine 130) is responsible for enhanced affinity of calcitonin (show CALCA Proteins) for CTR (show CALCR Proteins) ECD (show SHFM1 Proteins); the same appears to apply for enhanced affinity of amylin (show IAPP Proteins) for RAMP2-CTR (show CALCR Proteins) ECD (show SHFM1 Proteins). [GlcNAc = N-acetylglucosamine; CTR (show CALCR Proteins) = calcitonin receptor (show CALCR Proteins); ECD (show SHFM1 Proteins) = extracellular domain; RAMP2 = receptor (calcitonin) activity modifying protein 2].
interaction of RAMP2 or RAMP3 (show RAMP3 Proteins) with CLR (show DCLK3 Proteins) induces conformational variation in the juxtamembrane region, yielding distinct binding pockets, probably via an allosteric mechanism.
This study reveals the glucagon receptor (show GCGR Proteins) as a previously unidentified target for GLP-1 receptor (show GLP1R Proteins) agonists and highlights a role for RAMP2 in regulating its pharmacology.
Data suggest that ligand binding of a G protein-coupled receptor (GPCR (show TAS1R3 Proteins)) may inform drug development targeting calcitonin receptor-like receptor (CLR (show CALCRL Proteins)):receptor activity-modifying proteins RAMP1 (show RAMP1 Proteins)/2 complexes.
the AM system is widely expressed in human thymus from newborns; both AM1 receptor components CLR (show DCLK3 Proteins) and RAMP2, but not RAMP3 (show RAMP3 Proteins), are not associated with the plasma membrane of TECs and thymocytes but are located intracellularly, notably in the nucleus
Adrenomedullin (show ADM Proteins)-RAMP2 system suppresses ER stress-induced tubule cell death and is involved in kidney protection.
Data suggest isoforms of RAMP modulate accessibility of peptides to residues situated on CALCRL (calcitonin receptor-like receptor (show CALCRL Proteins)) N-terminal domain; RAMP3 (show RAMP3 Proteins)/RAMP2/RAMP1 (show RAMP1 Proteins) appear to alter accessibility of specific residues at CALCRL (show CALCRL Proteins)-RAMP interface.
RAMP2 gene expression increases with gestational age development in the fetal lung.
The CRLR (show CALCRL Proteins)-RAMP2 interactions were confirmed for the full-length proteins on the cell surface by site-specific photo-crosslinking.
Data indicate that adrenomedullin (show ADM Proteins) mRNA and protein signal were only found in trophoblast binucleate cells (BNCs), whereas those of CRLR (show CALCRL Proteins), RAMP2 and RAMP3 (show RAMP3 Proteins) were detected in cotyledonary villous and caruncular epithelial cells.
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 (RAMP2) protein, CRLR functions as an adrenomedullin receptor. The RAMP2 protein is involved in core glycosylation and transportation of adrenomedullin receptor to the cell surface.
receptor (calcitonin) activity modifying protein 2
, receptor activity modifying protein 2
, receptor activity-modifying protein 2
, receptor (G protein-coupled) activity modifying protein 2
, receptor activity modifying protein 2 isoform
, CRLR activity-modifying protein 2
, calcitonin receptor-like receptor activity modifying protein 2
, calcitonin-receptor-like receptor activity-modifying protein 2
, receptor-activity-modifying protein 2