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MFAP5 encodes a 25-kD microfibril-associated glycoprotein which is rich in serine and threonine residues.
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MFAP5 was up-regulated in breast cancers compared with that in normal breast tissues, and further increased in breast cancer bone metastasis. Functionally, MFAP5 overexpression accelerated breast cancer cell proliferation and migration, while an opposite effect was observed when MFAP5 was knocked down.
Study shows that over-expression of MFAP5 and TNNC1 (show TNNC1 Proteins) is correlated with cervical lymph node metastasis (CLNM), metastasis relapse-free survival and overall survival. These results propose that MFAP5 and TNNC1 (show TNNC1 Proteins) may be potential markers for predicting occult cervical lymphatic metastasis and prognosis of oral tongue carcinoma.
Likely pathogenic variants included a TGFB2 (show TGFB2 Proteins) variant in one patient and a SMAD3 (show SMAD3 Proteins) variant in another. These variants have been reported previously in individuals with similar phenotypes. Variants of uncertain significance of particular interest included novel variants in MYLK (show MYLK Proteins) and MFAP5, which were identified in a third patient
The results answer the question of how MAGP2 controls cell type dependent Notch (show NOTCH1 Proteins) signaling, but more importantly uncover a new mechanism to understand how extracellular matrices and cellular environments impact Notch (show NOTCH1 Proteins) signaling.
Our results demonstrate that factors involving low-grade inflammation modulate MFAP5 expression and that the modified expression of MFAP5 may further regulate adipose tissue inflammation.
FAK (show PTK2 Proteins)/CREB (show CREB1 Proteins)/TNNC1 (show TNNC1 Proteins) has a role in mediating the effect of stromal MFAP5 on ovarian cancer metastatic potential
Alteration of MAGP-2, a component of microfibrils and elastic fibers, appears as an initiating mechanism of inherited Thoracic aortic aneurysm and dissection (TAAD).
EPS led to the discovery of two novel immunomodulatory proteins, MFAP5 and PENK (show PENK Proteins) that when administered to mice subjected to endotoxemic shock, reversed the cytokine storm and provided a significant survival benefit
Decreased MFAP5 gene expression in the endometrium of patients with implantation failure after in vitro ertilization treatment
The MAGP2-based assay provided superior performance for the purpose of cell culture identification compared to assays using standard reference genes.
Binding of MAGP2 to microfibrils is regulated by proprotein convertase cleavage.
Loss of MAGP2 expression in vivo has pleiotropic effects.
interaction with fibrillin-1 (show FBN1 Proteins) and fibrillin-2 (show FBN2 Proteins) suggesting role in elastic fiber assembly
Tight skin fibrillin 1 (show FBN1 Proteins) altered extracellular matrix organization and caused fibrosis by affecting deposition of MAGP-2 or other fibrillin-1 (show FBN1 Proteins)-associated proteins.
microfibril-associated MAGP-2 may stimulate elastic fiber macroassembly by targeting the release of elastin (show ELN Proteins) globules from the cell membrane onto developing elastic fibers
MAGP-2 is identified as a novel regulator of angiogenesis.
results show MAGP-2 is covalently and periodically located along the fibrillin-containing microfibrils of the developing nuchal ligament, suggesting that it is an integral component of most if not all of the microfibrils in this elastic fiber-rich tissue
This gene encodes a 25-kD microfibril-associated glycoprotein which is rich in serine and threonine residues. It lacks a hydrophobic carboxyl terminus and proline-, glutamine-, and tyrosine-rich regions, which are characteristics of a related 31-kDa microfibril-associated glycoprotein (MFAP2). The close similarity between these two proteins is confined to a central region of 60 aa where precise alignment of 7 cysteine residues occurs. The structural differences suggest that this encoded protein has some functions that are distinct from those of MFAP2.
microfibrillar associated protein 5
, microfibril-associated glycoprotein 2
, microfibril-associated glycoprotein-2
, microfibrillar-associated protein 5