Disease relevance of Csrp1

• These findings suggest that a major function of CRP during the acute-phase response is to limit tissue damage and modulate acute inflammation [1].
• In C57BL/6 mice, injection of CRP either before or after induction of NTN suppressed proteinuria and glomerular pathology [1].
• Extended survival was caused by the persistence of reduced bacteremia in mice treated with any CRP [2].
• Human C-reactive protein (CRP) protects mice from lethality after infection with virulent Streptococcus pneumoniae type 3 [2].
• CRP treatment of NZB/NZW mice during acute disease rapidly decreased proteinuria, and the treated mice remained aproteinuric for at least 10 weeks [1].

High impact information on Csrp1

• Ltk resembles a receptor tyrosine kinase; it has a short, glycosylated, and cysteine-rich N-terminal domain [3].
• Laminin and fragments (1, 1-4) containing the inner rod-like segments from its short arms, which consist of cysteine-rich, "EGF-like" repeats, stimulated thymidine incorporation in cultured cells possessing EGF receptors but had no effect on a cell line lacking this receptor [4].
• At the amino terminus of this domain is a cysteine-rich sequence that has been proposed as a novel type of zinc finger [5].
• Metallothioneins are small cysteine-rich proteins that bind heavy metals such as zinc, cadmium, copper and mercury [6].
• We show that MLP, CRP, and betaCRP define a subclass of LIM-only proteins with unique dual subcellular localization in the nucleus and along actin-based filaments in the cytosol [7].

Chemical compound and disease context of Csrp1

• Insertion mutations were isolated in cya and crp of Yersinia enterocolitica, which encode adenylate cyclase and the cyclic AMP (cAMP) receptor protein (CRP) [8].
• Although the level of SAP mRNAs in the unstimulated mouse was about one-tenth of that of CRP mRNAs, it increased up to 60-fold during the first 20 hr, and returned gradually to the original level at 69 hr after the administration of Escherichia coli lipopolysaccharide [9].

Biological context of Csrp1

• Members of the cysteine-rich protein (CRP) family display two LIM domains and are implicated in muscle development [10].
• Linkage mapping of Csrp to proximal mouse chromosome 3 [11].
• Conclusions: The Muc3 mucin cysteine-rich domain plays an active role in epithelial restitution, and represents a potential novel therapeutic agent for intestinal wound healing [12].
• Analysis of the deduced amino acid sequence predicts that the molecule consists of two globular domains of 70 and 36 kD separated by a cysteine-rich domain of 28 kD [13].
• Our studies provide biochemical evidence of the role of the cysteine-rich domains of p185c-neu in assembly and transactivation of erbB complexes and also indicate that these subdomains might be useful clinical targets [14].

Anatomical context of Csrp1

• Cysteine-rich protein (CRP)2 is a member of the LIM-only CRP family that is expressed in vascular smooth muscle cells (VSMC) [15].
• The LIM protein cysteine-rich protein (CRP) 2 associates with the actin cytoskeleton and may maintain the cytoarchitecture [16].
• We have ectopically expressed CRP2, the predominant CRP in macrophages, in P388 lymphoblasts [17].
• Interestingly, although several markers of mature smooth muscle are already expressed, CRP1 expression in the bladder is not upregulated until the onset of bladder expansion at embryonic day 16.5, at which time its expression becomes very prominent [10].
• As development proceeds, CRP1 transcripts are observed throughout the SMC lineage, with minimal, transient expression detected in skeletal and cardiac muscle [10].

Associations of Csrp1 with chemical compounds

• MTF-1 is also involved in the cadmium response of cysteine- and glycine-rich protein 1 gene (Csrp1), which is implicated in cytoskeletal organization [18].
• SPARC is a Mr 43,000 secreted, acidic, cysteine-rich glycoprotein homologous to 43K bovine endothelial 'culture shock' protein [19].
• To investigate the significance of C1 and C2 domains of gamma-PKC in translocation, we expressed mutant gamma-PKC-GFP fusion protein in which the two cysteine rich regions in the C1 region were disrupted (designated as BS 238) or the C2 region was deleted (BS 239) [20].
• This is followed by a second domain, rich in cysteine, that shows sequence homology with cysteine-rich domains in turkey ovomucoid and other serine proteinase inhibitors [21].
• Functional analysis of agouti mutations in transgenic mice indicate that the cysteine-rich C terminus, signal peptide, and glycosylation site are required for agouti activity in vivo [22].

Other interactions of Csrp1

• The deduced CRS1C and CRS4C polypeptides are apparent precursors of secreted, cationic, proline- and cysteine-rich peptides that contain Cys-Pro-X repeats [23].
• Metallothionein (MT), a low molecular-weight, cysteine-rich, metal-binding protein, is induced by many environmental factors and a variety of stimuli [24].
• Fertilin alpha and beta are the first identified members of a new family of membrane proteins that each has the following domains: pro-, metalloprotease, disintegrin, cysteine-rich, EGF-like, transmembrane, and cytoplasmic domain [25].
• PKD contains membrane localization signals and a cysteine-rich repeat sequence homologous to that seen in the regulatory domain of protein kinase C (PKC) [26].
• Sca-2 is a member of the Ly-6 family, a group of small cysteine-rich cell surface proteins that are anchored in the membrane by a glycosyl-phosphatidylinositol moiety [27].

Analytical, diagnostic and therapeutic context of Csrp1

• We have determined by Northern analysis and in situ hybridization that CRP1 expression is developmentally regulated in the embryonic mouse and displays organ specific regulation in adults [10].
• We describe the molecular cloning and characterization of a secreted, acidic, cysteine-rich glycoprotein (SPARC) of apparent Mr 43,000 which is a major product of mouse embryo parietal endoderm [28].
• cDNA sequence analysis of a 29-kDa cysteine-rich surface antigen of pathogenic Entamoeba histolytica [29].
• Based on protein sequence alignment, TLP is most closely related to the cysteine-rich proteins, a subclass of the family of LIM-only proteins [30].
• The positions of the antigenic determinants for the Class II monoclonal antibodies were found by Western blotting analysis to reside in the N-proximal region of CRP [31].

References