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anti-Mouse (Murine) RAMP3 Anticorps:
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Human Polyclonal RAMP3 Primary Antibody pour IF (p), IHC (p) - ABIN1386642
Qiao, Wang, Wang, Zhao, Zhang, Han, Peng: Intermedin is upregulated and attenuates renal fibrosis by inhibition of oxidative stress in rats with unilateral ureteral obstruction. dans Nephrology (Carlton, Vic.) 2015
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.
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), calcitonin receptor-like receptor (CRLR), and RAMP1 and RAMP2.
these data demonstrate a sex-dependant, cardioprotective role of RAMP3 in the setting of chronic hypertension.
role in cell surface expression of CRLR/RAMP heterodimeric receptors
RAMP2 and RAMP3 have distinct physiological functions throughout embryogenesis, adulthood, and old age
tight regulation of WAP gene expression parallels variations in the chromatin structure and DNA methylation profile throughout the Ramp3-WAP-Tbrg4 locus.
high RAMP3 expression is an independent prognostic factor of favorable overall survival and recurrence-free survival in patients with HCC and its expression might reduce the negative effect of TP53 mutation on survival.
interaction of RAMP2 or RAMP3 with CLR 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 and RAMP2, 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) N-terminal domain; RAMP3/RAMP2/RAMP1 appear to alter accessibility of specific residues at CALCRL-RAMP interface.
The expression of RAMP3 is downregulated in the fetal lung with increasing gestational age.
the RAMP3 TMD participates in the negative regulation of CLR/RAMP3 internalization.
Data show that LOXL2 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 associates specifically with RAMP3, but not with RAMP1 or RAMP2.
Receptor activity modifying proteins interaction with human and porcine calcitonin receptor-like receptor (CRLR) in HEK-293 cells
results show the presence of calcitonin receptor-like receptor and receptor activity-modifying proteins in middle meningeal, middle cerebral, pial, and superficial temporal vessels
Co-expression of calcitonin receptors (CT) lacking a portion of domain 1 with receptor activity-modifying protein (RAMP) 1, 2, or 3 appears to produce functional CT-(8-32)-sensitive adrenomedullin receptors.
Data found that expressions of RAMP1, RAMP2 and RAMP3 mRNAs increased with the worsening of heart function, but the expressions of RAMP1 and RAMP2 mRNA decreased at level IV of heart failure.
RAMP3 interacts with N-ethylmaleimide-sensitive factor to cause the change in trafficking
results, using both endogenous and overexpressed cellular models, indicate a novel function for NHERF-1 and RAMP3 in the internalization of the adrenomedullin receptor and suggest additional regulatory mechanisms for receptor trafficking
the respective C-tails of hRAMP2 and -3 differentially affect hCRLR surface delivery and internalization
This study reveals important functionality of the RAMP C-terminal domain and identifies key differences in the role of the RAMP C terminus for calcitonin receptor versus calcitonin receptor-like receptor-based receptors.
Identification of RAMP3 residues for adrenomedjullin receptors are reported.
The His residues of hRAMP2 and -3 differentially govern adrenomedullin receptor function.
Data indicate that adrenomedullin mRNA and protein signal were only found in trophoblast binucleate cells (BNCs), whereas those of CRLR, RAMP2 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