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MRC2 encodes a member of the mannose receptor family of proteins that contain a fibronectin type II domain and multiple C-type lectin-like domains. Additionally we are shipping MRC2 Antibodies (77) and MRC2 Kits (31) and many more products for this protein.
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A second loss-of-function mutation in the bovine mannose receptor C (MRC2) gene causes illegitimate receptor oligomerization, which is predicted to impair function of the MRC2 encoded protein, Endo180.
The positional identification of a 2-bp deletion in the open reading frame of the MRC2 receptor causing the recessive Crooked (show LRP6 Proteins) Tail Syndrome in cattle, isdescribed.
Endo180 knockdown in pancreatic stellate cells (PSCs) attenuated the invasive abilities of PSCs and co-cultured pancreatic cancer cells, and decreased the expression level of phosphorylated myosin light chain 2 (MLC2 (show MYL12B Proteins)).
results provide a molecular mechanism to support the structural flexibility of uPARAP, and shed light on the structural flexibility of other members of the MR family
A model of the ligand-binding region of uPARAP was obtained by molecular replacement.
The positive correlation between suPLAUR expression and body mass index, suggests that leukocyte recruitment in obese tissue may be regulated, at least in part, through the splicing of the PLAUR (show PLAUR Proteins) transcript.
Our findings identify sarcoma cell-resident uPARAP/Endo180 as a central player in the bone degeneration of advanced osteosarcoma
Study identifies the interaction between lectin domain in Endo180 and CD147 as an Epithelial-to-mesenchymal transition suppressor and indicates that stabilization of this molecular complex improves prostate cancer survival rates.
AGE-dependent modification of the basal lamina induces invasive behaviour in non-transformed prostate epithelial cells via Endo180 pathway linked to cancer progression.
MRC2 is downregulated by UVA irradiation and reduces collagen internalization; this can be recovered by all-trans retinoic acid
Our findings correlate for the first time impaired collagen uptake via Endo180 with the pericellular accumulation of collagen fragments during photoaging.
TGFbeta1 (show TGFB1 Proteins)-Endo180-dependent collagen deposition is dysregulated at the tumour-stromal interface in bone metastasis.
Findings show that under in vivo conditions, uPARAP does not play a role in the phagocytic uptake of collagen fibrils by fibroblasts.
uPARAP function in cutaneous wound repair
Both uPARAP and MMP-2 (show MMP2 Proteins) take part in matrix turnover processes important for bone growth.
Genetic ablation of the Mrc2 impaired the intracellular collagen degradation pathway.
This function of uPARAP/Endo180 defines a novel role of intracellular collagen turnover in fibrosis protection.
uPARAP is highly expressed in the murine lung, and loss of uPARAP leads to differences in lung mechanics, lung permeability, and collagen content after injury
data establish an important fibrosis-attenuating role for Mrc2-expressing renal interstitial cells and suggest the involvement of a lysosomal collagen turnover pathway
A novel functional role of collagen glycosylation: interaction with the endocytic collagen receptor (show ITGA2 Proteins) uparap/ENDO180.
This gene encodes a member of the mannose receptor family of proteins that contain a fibronectin type II domain and multiple C-type lectin-like domains. The encoded protein plays a role in extracellular matrix remodeling by mediating the internalization and lysosomal degradation of collagen ligands. Expression of this gene may play a role in the tumorigenesis and metastasis of several malignancies including breast cancer, gliomas and metastatic bone disease.
mannose receptor, C type 2
, C-type mannose receptor 2
, C-type mannose receptor 2-like
, collagen-binding factor Endo180
, endocytic receptor 180
, macrophage mannose receptor 2
, C-type lectin domain family 13 member E
, UPAR-associated protein
, endocytic receptor (macrophage mannose receptor family)
, urokinase-type plasminogen activator receptor-associated protein
, lectin lambda
, novel lectin