- EGFR Signaling Pathway
- TGF-beta Signaling
- Canonical Wnt Signaling
- non-Canonical Wnt Signaling
- Notch Signaling
- p53 Pathway
- NF-kB Pathway
- Cytokine Signaling
SPARC-like protein 1 (SPARCL1; also known as SC1, high endothelial venule protein, or hevin) is an extracellular matrix-associated, secreted glycoprotein belonging to the secreted protein acidic and rich in cysteine (SPARC) family of matricellular proteins. It contains three conserved structural domains that are implicated in the regulation of cell adhesion, migration, and proliferation. SPARCL1 is expressed during embryogenesis and tissue remodeling and is especially prominent in brain and vasculature. Its down-regulation in a number of cancers and the possibility of its functional compensation by SPARC has led to recent interest in hevin as a tumor suppressor and regulator of angiogenesis. SPARCL1 has antiadhesive properties, and loss of SPARCL1 expression is associated with increased proliferative activity and cell cycle progression. It is suggested that it may influence multiple cellular processes during distinct stages of brain development and function. In addition, SPARCL1 can influence the function of astroglial cells in the developing and mature central nervous system (CNS).
- Mouse Monoclonal Antibody, Cat No:10046-MM06
- SPARCL1 Antibody, Rabbit MAb, Cat No:10046-R204
- Rabbit Polyclonal Antibody (Antigen Affinity Purified), Cat No:10046-RP01
SPARCL1 ELISA Pair sets
SPARCL1 cDNA Clones
- Homo sapiens SPARCL1 transcript variant 2 cDNA Clone(NM_004684.4), Cat No:HG10046-M
- Mus musculus SPARCL1 cDNA Clone, Cat No:MG50544-M
SPARCL1, mast9, hevin, SC1, PIG33, SPARC-like 1 (mast9, hevin), proliferation-inducing protein 33 [Homo sapiens]
Sparcl1, mast9, hevin, Sc1, Ecm2, SPARC-like 1 (mast9, hevin), extracellular matrix protein 2 [Mus musculus]
Entrez Gene summary for SPARCL1 :
OMIM - description for SPARCL1 :
The cells in high endothelial venules (HEVs) in lymphoid tissues have a plump, almost cuboidal, appearance and support high levels of lymphocyte extravasation from blood, possibly due to the presence of desmosome-like junctions rather than tight junctions in the HEVs. Lymphocytes stick to HEVs through a process of rolling, activation, and strong adhesion, followed by transendothelial migration and the passage of lymphocytes through the HEV basement membrane. In chronic inflammation, the activated endothelium of nonlymphoid tissues acquires an HEV-like morphology and function. Hevin is highly expressed in HEV and is thought to contribute to the induction or maintenance of features of the HEV endothelium that facilitate lymphocyte migration
Wikipedia summary for SPARCL1 :
SPARC-like protein 1 is a protein that in humans is encoded by the SPARCL1 gene
Recommended name: SPARC-like protein 1
Belongs to the SPARC family. Contains 1 EF-hand domain. Contains 1 follistatin-like domain. Contains 1 Kazal-like domain.
N- and O-glycosylated. O-glycosylated with a core 1 or possibly core 8 glycan. Thr-398 is the preferred site to Thr-399.
|Subcellular location:||Secreted › extracellular space › extracellular matrix|
Highly expressed in lymph node, brain, heart, lung, skeletal muscle, ovary, small intestine, and colon, with lower levels in placenta, pancreas, testis, spleen, and thymus, and no expression in kidney, liver, and peripheral blood leukocytes.
General information above from UniProt
By differential hybridization of a tonsillar high endothelial cell cDNA library, Girard and Springer (1995) obtained a cDNA encoding SPARCL1, which they termed Hevin. Sequence analysis predicted that Hevin is an evolutionarily conserved, 664-amino acid secreted protein. Hevin contains 7 potential N-linked glycosylation sites, an N-terminal signal peptide, a long acidic region rich in glu and asp, a cysteine-rich domain, and a C-terminal region with a 12-residue segment homologous to the calcium-binding loops of EF-hand structures in the calmodulin family of proteins (see CALM1; 114180). The 232 C-terminal amino acids of Hevin are 62% identical to the homologous portion of SPARC (182120). In situ hybridization analysis showed selective expression of Hevin in the cytoplasmic region of high endothelial cells. Northern blot analysis revealed high expression of a 2.7-kb Hevin transcript in lymph node, brain, heart, lung, skeletal muscle, ovary, small intestine, and colon, with lower levels in placenta, pancreas, testis, spleen, and thymus, and no expression in kidney, liver, and peripheral blood leukocytes. Unlike SPARC, Hevin is absent from flat umbilical vein endothelial cells. Girard and Springer (1995) proposed that Hevin may have antiadhesive properties similar to those of SPARC.
- SPARCL1 is a lymphocyte adhesion receptor for high endothelium
- SPARCL1 regulates the terminal phase of radial glia-guided migration in the cerebral cortex
- SPARCL1 has important functions in extracellular matrix synthesis and cellular adhesion to extracellular matrix
- SPARCL1 regulates dermal extracellular matrix and collagen fibril formation
- SPARCL1 has the capacity to modulate the structure of dermal extracellular matrix, specifically by its regulation of decorin levels and collagen fibril assembly
- SPARCL1 can influence the function of astroglial cells in the developing and mature central nervous system
- SPARCL1 may be a component of the 'matrix response' involved in remodeling events associated with neuronal degeneration following neural injury
- SPARCL1 has anti-invasive effects and reduced expression in metastasis of pancreatic cancer
- homolog to SPARC
Phenotype Information for SPARCL1 from OMIM (Online Mendelian Inheritance in Man)