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anti-Mouse (Murine) PRELP Antikörper:
anti-Human PRELP Antikörper:
anti-Rat (Rattus) PRELP Antikörper:
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Therefore, this study established a new role of PRELP in modulating beta-catenin (zeige CTNNB1 Antikörper)/connexin43 (zeige GJA1 Antikörper) pathway and osteoblast differentiation.
when delivered via an AAV vector to the retina of mice, PRELP inhibited laser-induced choroidal neovascularization by 60%. PRELP reduced deposition of membrane attack complex in vivo by 25.5%.
PRELP has a role in skeletal remodeling.
Up regulation of prolargin in RA suggests the likelihood of an adaptive mechanism to control the increased osteoclastogenesis in RA and may have therapeutic value in controlling the disease.
PRELP was more expressed in peritoneal lesions. Considering that the genes studied participate either directly or indirectly in cellular processes that can lead to cell migration, angiogenesis, and inappropriate invasion, it is possible that the deregulation of these genes caused the development and maintenance of ectopic tissue.
this study shows that PRELP enhances host innate immunity against Moraxella catarrhalis through increasing complement-mediated attack, improving phagocytic killing activity of neutrophils, and preventing bacterial adherence to lung epithelial cells
These findings provide support for a role of the N-terminal region of PRELP as an important regulator of cell adhesion and behaviour, which may be of importance in pathological conditions.
The unique expression of a 38 kDa PRELP in chronic lymphocytic leukemia (CLL) cells may suggest involvement in the pathobiology of CLL
PRELP expression governs stem cells to differentiate into ligament tissue in a mouse model.
PRELP may down-regulate complement attack at basement membranes and on damaged cartilage and therefore limit pathological complement activation in inflammatory disease such as RA.
Relative abundance of PRELP mRNA and protein inhuman sclera, and observed age-related variation in scleral PRELP expression suggests that PRELP may play critical role in regulating biomechanical properties of scleral extracellular matrix.
PRELP overexpression leads to a connective tissue phenotype in the skin, where the organization of collagen fibrils in the dermis was perturbed and the thickness of the hypodermal fat layer was diminished.
The protein encoded by this gene is a leucine-rich repeat protein present in connective tissue extracellular matrix. This protein functions as a molecule anchoring basement membranes to the underlying connective tissue. This protein has been shown to bind type I collagen to basement membranes and type II collagen to cartilage. It also binds the basement membrane heparan sulfate proteoglycan perlecan. This protein is suggested to be involved in the pathogenesis of Hutchinson-Gilford progeria (HGP), which is reported to lack the binding of collagen in basement membranes and cartilage. Alternatively spliced transcript variants encoding the same protein have been observed.
, proline-arginine-rich end leucine-rich repeat protein
, 55 kDa leucine-rich repeat protein of articular cartilage
, prolargin proteoglycan
, proline arginine-rich end leucine-rich repeat protein