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the cardiovascular response of Ramp1 (show RAMP1 Proteins)(-/-), Ramp2 (show RAMP2 Proteins)(+/-), Ramp3(-/-), Ramp1 (show RAMP1 Proteins)(-/-)/Ramp3(-/-) double-knockout (dKO), and Calcrl (show CALCRL Proteins)(+/-) mice to AM and CGRP (show CALCA Proteins) were compared to wildtype mice.These results suggest that the hypotensive effect of AM is primarily mediated through the CLR (show CALCR Proteins)/RAMP1 (show RAMP1 Proteins) heterodimer, but that AM signaling via CLR (show CALCR Proteins)/RAMP2 (show RAMP2 Proteins) and CLR (show CALCR Proteins)/RAMP3 also contributes to some hypotensive action.
RAMP3 regulates drainage through lymphatic vessels.
G-protein-coupled receptor 30 interacts with receptor activity-modifying protein 3 and confers sex-dependent cardioprotection.
Data show that mechanical ventilation reduced the expression of receptor activity-modifying protein RAMP3, but not of intermedin (IMD (show ADM2 Proteins)), calcitonin receptor-like receptor (CRLR (show CALCRL Proteins)), and RAMP1 (show RAMP1 Proteins) and RAMP2 (show RAMP2 Proteins).
these data demonstrate a sex-dependant, cardioprotective role of RAMP3 in the setting of chronic hypertension.
role in cell surface expression of CRLR (show CALCRL Proteins)/RAMP heterodimeric receptors
RAMP2 (show RAMP2 Proteins) and RAMP3 have distinct physiological functions throughout embryogenesis, adulthood, and old age
tight regulation of WAP (show Wap Proteins) gene expression parallels variations in the chromatin structure and DNA methylation (show HELLS Proteins) profile throughout the Ramp3-WAP (show Wap Proteins)-Tbrg4 (show TBRG4 Proteins) locus.
interaction of RAMP2 (show RAMP2 Proteins) or RAMP3 with CLR (show DCLK3 Proteins) induces conformational variation in the juxtamembrane region, yielding distinct binding pockets, probably via an allosteric mechanism.
the AM system is widely expressed in human thymus from newborns; both AM1 receptor components CLR (show DCLK3 Proteins) and RAMP2 (show RAMP2 Proteins), but not RAMP3, are not associated with the plasma membrane of TECs and thymocytes but are located intracellularly, notably in the nucleus
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/RAMP2 (show RAMP2 Proteins)/RAMP1 (show RAMP1 Proteins) appear to alter accessibility of specific residues at CALCRL (show CALCRL Proteins)-RAMP interface.
The expression of RAMP3 is downregulated in the fetal lung with increasing gestational age.
the RAMP3 TMD (show TTN Proteins) participates in the negative regulation of CLR (show DCLK3 Proteins)/RAMP3 internalization.
Data show that LOXL2 (show LOXL2 Proteins) and RAMP3 are strongly coexpressed in human colon, breast, and gastric carcinomas but not in normal colon or gastric epithelial cells.
This study provides insight into the role of three amino acid changes in human RAMP3.
Morphological fluorescence techniques, bioluminescence resonance energy transfer, and bimolecular fluorescence complementation analysis demonstrate that the secretin receptor (show SCTR Proteins) associates specifically with RAMP3, but not with RAMP1 (show RAMP1 Proteins) or RAMP2 (show RAMP2 Proteins).
Receptor activity modifying proteins interaction with human and porcine calcitonin receptor-like receptor (CRLR (show CALCRL Proteins)) in HEK (show EPHA3 Proteins)-293 cells
results show the presence of calcitonin receptor-like receptor (show CALCRL Proteins) and receptor activity-modifying proteins in middle meningeal, middle cerebral, pial, and superficial temporal vessels
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 (show RAMP2 Proteins) and RAMP3 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 (RAMP3) protein, CRLR functions as an adrenomedullin receptor.
receptor (calcitonin) activity modifying protein 3
, receptor activity modifying protein 3
, receptor activity-modifying protein 3
, receptor (G protein-coupled) activity modifying protein 3
, Receptor activity-modifying protein 3
, CRLR activity-modifying protein 3
, calcitonin receptor-like receptor activity modifying protein 3
, calcitonin-receptor-like receptor activity-modifying protein 3
, receptor-activity-modifying protein 3