ASPN
ASPN (asporin, also known as PLAP-1, SLRR1C and FLJ20129) is a secreted class I small leucine-rich proteoglycan of the extracellular matrix. It restrains TGF-beta and BMP signalling and influences collagen mineralisation in cartilage and the periodontal ligament. Browse Assay Genie's current range of ASPN research reagents below, or read on for the biology behind the target.
ASPN is a secreted extracellular matrix protein that acts as a negative regulator of growth factor signalling in skeletal and tooth-supporting tissues. In articular cartilage it is a critical regulator of TGF-beta: it blocks the interaction between TGF-beta and its receptor at the cell surface and so inhibits canonical TGF-beta/Smad signalling, thereby restraining chondrogenesis. In the periodontal ligament (PDL) it prevents BMP2 from binding to the BMPR1B receptor, which blocks BMP-dependent activation of SMAD proteins and inhibits PDL cell differentiation and mineralisation. This helps keep the PDL from ossifying and maintains homeostasis of the tooth-supporting system.
Asporin also binds collagen and calcium, and it is reported to play a role in osteoblast-driven collagen biomineralisation. The protein belongs to the small leucine-rich proteoglycan (SLRP) family, class I subfamily, and the HGNC places the gene in the group of small leucine rich repeat proteoglycans. The ASPN gene is annotated with multiple transcript variants produced by alternative splicing, and the mouse ortholog is Aspn.
The protein is also known as PLAP-1 (periodontal ligament-associated protein 1), SLRR1C and FLJ20129, and was previously listed as asporin (LRR class 1). Polymorphisms in the aspartic acid repeat region of the ASPN gene are associated with susceptibility to osteoarthritis and with intervertebral disc disease, which makes asporin a frequent subject in studies of cartilage homeostasis and osteoarthritis pathogenesis.
Asporin is an essential regulator of cartilage homeostasis, and variants in its aspartic acid repeat are linked to osteoarthritis susceptibility.
Asporin blocks the TGF-beta/receptor interaction on the cell surface and inhibits canonical TGF-beta/Smad signalling in articular cartilage.
By limiting BMP2 binding to BMPR1B, asporin keeps the periodontal ligament from mineralising and maintains the tooth-supporting system.
Asporin binds collagen and calcium and contributes to osteoblast-driven collagen biomineralisation, relevant to matrix and bone studies.
ASPN encodes asporin, an extracellular matrix proteoglycan that negatively regulates TGF-beta and BMP signalling. It limits chondrogenesis in articular cartilage, prevents ossification of the periodontal ligament, and binds collagen and calcium to influence collagen biomineralisation.
ASPN is also called PLAP-1, SLRR1C and FLJ20129, and was previously named asporin (LRR class 1). The gene produces multiple transcript variants through alternative splicing. Its HGNC gene group is small leucine rich repeat proteoglycans.
Polymorphisms in the aspartic acid repeat region of the ASPN gene are associated with susceptibility to osteoarthritis and intervertebral disc disease. A mouse ortholog, Aspn, exists; check the datasheet of any product for its validated reactivity.
Other small leucine-rich proteoglycans, TGF-beta and BMP pathway components and cartilage matrix markers with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9BXN1; product specifications from Assay Genie datasheets.