Disease relevance of COLEC12

• Ligand-binding studies of CHO-K1 cells expressing hSRCL type I and type II demonstrated their specific binding capacity in Escherichia coli and Staphylococcus aureus [1].
• SRCL /CL-P1 was recently identified as a scavenger receptor with a C-type lectin domain, which was expressed in vascular endothelial cells and could bind to Gram-positive and Gram-negative bacteria, yeast and oxidized LDL [2].

High impact information on COLEC12

• SRCL shares with the asialoglycoprotein receptor the ability to mediate endocytosis and degradation of glycoprotein ligands [3].
• Thus, SRCL shares with the dendritic cell receptor DC-SIGN the ability to bind the Lewis(x) epitope [3].
• The amino acid sequence of the CRD is very similar to the CRD of the asialoglycoprotein receptor and other galactose-specific receptors, but SRCL binds selectively to asialo-orosomucoid rather than generally to asialoglycoproteins [3].
• These studies suggest that SRCL might be involved in selective clearance of specific desialylated glycoproteins from circulation and/or interaction of cells bearing Lewis(x)-type structures with the vascular endothelium [3].
• The clp1 gene of the mushroom Coprinus cinereus is essential for A-regulated sexual development [4].

Biological context of COLEC12

• Haplotype analysis of the human collectin placenta 1 (hCL-P1) gene [5].
• By sequencing the CL-P1 gene in ten Japanese volunteers, we identified five single-nucleotide polymorphisms (SNPs) with a minor allele frequency of at least 29% [5].
• The clp1 transcript was normally detected only in the presence of the A protein heterodimer formed when homokaryons with compatible A genes were mated [4].
• Structure of a nucleotide-bound Clp1-Pcf11 polyadenylation factor [6].
• Moreover, we suggest that this complex represents a stabilized ATP bound form of Clp1 that requires the participation of other non-CFIA processing factors in order to initiate timely ATP hydrolysis during 3' end processing [6].

Anatomical context of COLEC12

• When hSRCL type I and type II were expressed in CHO-K1 cells, they were localized in the plasma membrane forming clusters on the surface [1].
• We show that scavenger receptor with C-type lectin (SRCL), a member of the scavenger receptor family containing coiled-coil, collagen-like, and C-type lectin/carbohydrate recognition domains, is expressed in cultured astrocytes and microglia [7].
• Thus, Gfi1 selectively specifies IL7-dependent development of B cells from CLP1 progenitors, providing clues to the transcriptional networks integrating cytokine signals and lymphoid differentiation [8].

Associations of COLEC12 with chemical compounds

• After PSP bolus injection, CLR and CLP were 252.8 +/- 57.9 and 350.0 +/- 41.3 mL/min/1.73 m2, respectively [9].
• Therefore, we conclude that CLP is a trypsin-like serine protease [10].
• The crystal structures of gamma-carboxyglutamic acid domains of coagulation factors X and IX have recently been clarified in structural studies of complexes between the gamma-carboxyglutamic acid domain of factors X and X-bp (a venom CLP) and between the gamma-carboxyglutamic acid domain of factors IX and IX-bp (a venom CLP) [11].

Analytical, diagnostic and therapeutic context of COLEC12

• Northern blot analysis revealed that hSRCL type I and type II mRNAs are abundantly expressed in adult human tissues [1].
• Molecular cloning and functional characterization of a human scavenger receptor with C-type lectin (SRCL), a novel member of a scavenger receptor family [1].
• An approximately 2.1-fold increase in immunofluorescence intensity was observed for the SRCL transfectants compared to control vector transfectants [2].
• 293/EBNA-1 cells stably expressing SRCL were found to take up GalNAc but not mannose-conjugated particles on confocal microscopy [2].

References