Disease relevance of Csrp1

• Myocardial infarction in humans provokes an acute phase response, and C-reactive protein (CRP), the classical acute phase plasma protein, is deposited together with complement within the infarct [1].
• These observations demonstrate that human CRP and complement activation are major mediators of ischemic myocardial injury and identify them as therapeutic targets in coronary heart disease [1].
• Levels of CRP reporter gene expression were increased 2-fold despite severe hyperinsulinemia compared with non-diabetic non-obese transgenic mice [2].
• Although the role of CRP has been implicated in atherogenesis, its direct effects on vascular cells are poorly defined [3].
• The basic mechanisms responsible for this association are not clear; CRP may merely be a marker of inflammation with no specific role in the pathogenesis of cardiac disease or may directly modulate the disease process [4].

High impact information on Csrp1

• The proteins have several features common to the family of tyrosine kinase growth-factor receptors, including cysteine-rich external domains, a hydrophobic transmembrane region and a cytoplasmic tyrosine kinase domain [5].
• The amino acid sequence deduced from the nucleotide sequences of the cDNAs indicated the presence of a cysteine-rich DNA-binding domain that is highly conserved in all steroid receptors [6].
• The product of the Wnt-1 proto-oncogene is a cysteine-rich glycoprotein that plays a crucial role in the development of the vertebrate central nervous system [7].
• Here we show that injection of human CRP into rats after ligation of the coronary artery reproducibly enhanced infarct size by approximately 40% [1].
• Results of this study suggested that the ability of H. influenzae to vary expression of this unusual bacterial structure may correlate with its ability both to persist on the mucosal surface (ChoP+ phenotype) and to cause invasive infection by evading innate immunity mediated by CRP (ChoP- phenotype) [8].

Chemical compound and disease context of Csrp1

• In both age groups, ischemia resulted in a depletion of glucose, OAA, ATP AND CRP, a diminution of Pyr, Citr and alpha-Keto and an accumulation of FDP, Lact, Succ, ADP and AMP in brain cortex [9].
• The second cysteine-rich (Cys-2) domain of rat brain PKC-gamma regulatory region C1 (92-173) was expressed in Escherichia coli cells and purified [10].
• BACKGROUND: The aim of the present study was to evaluate the effects of systemic administration of low-dose doxycycline and a bisphosphonate, alendronate, on serum levels of interleukin-1beta (IL-1beta), osteocalcin (OC), and C-reactive protein (CRP) in experimental periodontitis in rats [11].
• Cadmium injection (less than 3 mg/kg body weight) in white rat was found to be associated with the appearance of CRP in liver cytosol after 8 hr and in serum after 18 hr of injection [12].
• Interleukin-1 (IL-1) activity and the acute phase response, as measured by plasma CRP and iron, were used to determine if the standard disease modifying antirheumatic drugs (DMARDs), gold, chloroquine and D-penicillamine had a common profile of activity in the adjuvant arthritic (AA) rat [13].

Biological context of Csrp1

• Isolation and developmental expression of a rat cDNA encoding a cysteine-rich zinc finger protein [14].
• In situ hybridization of 3H-labeled CRP cDNA to human metaphase chromosomes confirms this assignment and permits regional localization to bands 1q24-1q32 [15].
• Although all members of the protein kinase C family so far identified have a tandem repeat of the characteristic cysteine-rich zinc-finger-like sequence in the regulatory domain, the zeta subspecies contains only one set of this sequence [16].
• EF-hand motifs, cysteine-rich zinc-finger-like sequences, and putative ATP-binding sites were all conserved between the two kinase species [17].
• The precursor has seven N-linked glycosylation sites and an unusual structure containing 18 epidermal growth factor-like domains and four cysteine-rich internal repeats [18].

Anatomical context of Csrp1

• Furthermore, by using an osteoblastic cell line (CRP 10/30) which is a powerful promoter of osteoclastic resorption in vitro, we obtained evidence that the inhibitory effect of bisphosphonates was the result of an action on osteoblasts rather than on osteoclasts [19].
• CTGF is a 38 kDa cysteine-rich peptide whose synthesis and secretion are selectively induced by transforming growth factor beta (TGF-beta) in connective tissue cells [20].
• We therefore conclude that CRP occurs as a membrane-associated protein constitutively expressed on liver macrophages functioning as a receptor mediating galactose-specific binding of particulate ligands [21].
• The non-glycosylated rat CRP, however, was still able to bind to phosphorylcholine-Sepharose and to be secreted by hepatocytes [22].
• This result was further confirmed by immunohistochemical staining of lung sections that showed the localization of CRP in alveolar macrophages [23].

Associations of Csrp1 with chemical compounds

• The deduced extracellular parts of the AMIGOs contain six leucine-rich repeats (LRRs) flanked by cysteine-rich LRR NH2- and COOH-terminal domains and by one immunoglobulin domain close to the transmembrane region [24].
• This domain comprises leucine and cysteine rich motifs, followed by two immunoglobulin like (Ig-like) domains [25].
• Protein kinase C normally has a tandem repeat of a characteristic cysteine-rich sequence in C1, the conserved region of the regulatory domain [26].
• These cationic arginine- and cysteine-rich peptides inhibit corticotropin (ACTH)-stimulated rat adrenal cell corticosterone production [27].
• Studies using tunicamycin revealed that the N-linked oligosaccharide present in rat CRP was not required for formation of its dimeric component, oligomerization, ability to bind to phosphorylcholine, or secretion [22].

Other interactions of Csrp1

• The predicted Elk protein contains all the hallmarks of a receptor tyrosine kinase, including an N-terminal signal sequence, a cysteine-rich extracellular domain, a membrane-spanning segment, a cytoplasmic tyrosine kinase domain, and a C-terminal tail [28].
• Three cysteine-rich cationic peptides, designated RatNP-1, RatNP-3, and RatNP-4, were purified from an acid extract of rat polymorphonuclear neutrophils, sequenced, and tested for antimicrobial activity [29].
• The effect of the stress-induced, cysteine-rich protein, metallothionein I (MT), on oxygen consumption by rat liver mitochondria was studied [30].
• The discontinuity of cysteine-rich and S,T,P-rich areas near the C-terminus has not been observed in other mammalian mucin structures reported to date [31].

Analytical, diagnostic and therapeutic context of Csrp1

• However, in acute phase serum or heparinized plasma from hypercholesterolemic rabbits part or all of the CRP was found by gel filtration and immunoelectrophoretic techniques to be complexed with beta-VLDL, an abnormal apoB-containing plasma lipoprotein present in these animals [32].
• Tissue TNF-alpha expression measured by Northern blot analysis and serum C-reactive protein (CRP) levels, a marker of inflammation, were significantly reduced in animals pretreated with rIL-6 [33].
• A mAb specific for rat neo-CRP labels liver macrophages but not hepatocytes and reacts with the isolated protein in a Western blot assay [21].
• Western blot analysis showed that CRP was present in the lung tissue, lung lavage, and alveolar macrophages [23].
• In this study, the nature of the oligosaccharide chain of rat CRP was investigated by fast atom bombardment-mass spectrometry (FAB-MS), and general features of its biosynthetic pathway were also analyzed [22].

References