Disease relevance of SCPEP1

• The abundance of mRNA coding for hscp 36 was found to be similar in both normal and simian virus 40 (SV40) transformed human fibroblasts [1].
• RESULTS: Only 1 of 7 cases of chronic lymphocytic leukemia expressed a CT gene (HOM-TES-14/SCP-1), and 10 follicular lymphomas were negative for all of the CT genes tested [2].
• Furthermore, an analysis of toxic and nontoxic duplexes identifies a strong correlation between the toxicity and the presence of a 4-base-pair motif (UGGC) in the RISC-entering strand of toxic siRNA [3].
• Very early risk stratification by electrocardiogram at rest in men with suspected unstable coronary heart disease. The RISC Study Group [4].
• Belactins A and B, new inhibitors of serine carboxypeptidase were discovered in the fermentation broth of Saccharopolyspora sp. MK19-42F6 [5].

Psychiatry related information on SCPEP1

• We studied the relationships between structure and schizotypal features (assessed using RISC and SIS) and verbal learning and memory (measured using RAVLT) in relatives at high risk of developing schizophrenia and normal controls [6].
• The CD-RISC has sound psychometric properties and distinguishes between those with greater and lesser resilience [7].

High impact information on SCPEP1

• We recently showed that Scp1 is an evolutionarily conserved regulator of neuronal gene silencing [8].
• Moreover, these results provide a template for the design of specific inhibitors of Scp1 for the study of neuronal stem cell development [8].
• Fcp1 and Scp1 belong to a family of Mg(2+)-dependent phosphoserine (P.Ser)/phosphothreonine (P.Thr)-specific phosphatases [8].
• The fundamental engines of RNA silencing are RISC and RITS complexes, whose common components are 21-25 nt RNA and an Argonaute protein containing a PIWI domain of unknown function [9].
• Endothelin-1 is a peptidic substrate in vitro of lysosomal protective protein/cathepsin A (PPCA) with serine carboxypeptidase activity [10].

Biological context of SCPEP1

• Radiation hybrid mapping studies placed the rat RISC locus on chromosome 10q [11].
• A near full-length rat RISC cDNA was cloned and found to have a 452-amino acid open reading frame containing an amino-terminal signal sequence, followed by several conserved domains comprising the catalytic triad common to members of the serine carboxypeptidase family [11].
• Overexpression of SCP 1, 2, or 3 decreased linker phosphorylation of Smads 1, 2 and 3 [12].
• Chemical modifications impairing the cleavage of the passenger strand also impair the cleavage of a target RNA in vitro as well as the silencing of a reporter gene in vivo, suggesting that passenger strand removal is facilitated by its cleavage during RISC assembly [13].
• The RISC (Relationship between Insulin Sensitivity and Cardiovascular disease) Study is using the infrastructure of an extended European collaborative research group to study insulin resistance and CVD risk in 1500 healthy people aged 30 to 60 years from 20 centres in 13 countries [14].

Anatomical context of SCPEP1

• Western blotting studies using conditioned medium from transfected COS-7 cells suggest that RISC is a secreted protein [11].
• One of these, hscp 36 (heat-stable cytoskeletal protein having an apparent molecular weight of 36,000), cross-reacted efficiently with an antiserum to chicken skeletal muscle tropomyosin [1].
• In proteins such as the eponymous calponin, IQGAP1, and Scp1, a single CH-domain exists, but there has been some controversy over whether this domain binds to actin filaments [15].
• Cloning and characterization of CPVL, a novel serine carboxypeptidase, from human macrophages [16].
• Intracellular cathepsin A (acid serine carboxypeptidase) activity increased four-fold compared with in those of the parent and mock-transfected cell lines [17].

Associations of SCPEP1 with chemical compounds

• Expression of RISC is low in cultured SMC but progressively increases over a 5-day time-course treatment with all-trans-retinoic acid [11].
• Structure of wheat serine carboxypeptidase II at 3.5-A resolution. A new class of serine proteinase [18].
• Prolylcarboxypeptidase, a lysosomal serine carboxypeptidase, cleaves COOH-terminal amino acids linked to proline, as in angiotensin II and III and [des-Arg9] bradykinin [19].
• Peptide aldehyde complexes with wheat serine carboxypeptidase II: implications for the catalytic mechanism and substrate specificity [20].
• Structure of the complex of L-benzylsuccinate with wheat serine carboxypeptidase II at 2.0-A resolution [21].

Other interactions of SCPEP1

• Lysosomal protective protein/cathepsin A is a serine carboxypeptidase that forms a complex with beta-galactosidase and neuraminidase [22].
• Carboxypeptidase Z is a serine carboxypeptidase secreted by Absidia zychae NRIC 1199 [23].
• Amidation of growth hormone releasing factor (1-29) by serine carboxypeptidase catalysed transpeptidation [24].
• Members in this family include acetylcholinesterase, dienelactone hydrolase, lipase, thioesterase, serine carboxypeptidase, proline iminopeptidase, proline oligopeptidase, haloalkane dehalogenase, haloperoxidase, epoxide hydrolase, hydroxynitrile lyase and others [25].

Analytical, diagnostic and therapeutic context of SCPEP1

• In situ hybridization verified the localization of RISC to medial SMC of the adult rat aorta [11].
• Tissue Northern blotting studies demonstrated robust expression of RISC in rat aorta, bladder, and kidney with much lower levels in all other tissues analyzed; high level RISC expression was also observed in human kidney [11].
• The structures of two ternary complexes of wheat serine carboxypeptidase II (CPD-WII), with a tetrapeptide aldehyde and a reaction product arginine, have been determined by X-ray crystallography at room temperature and -170 degrees [20].
• The transition probabilities and risk factor trends used in the RISC model were based on data from 3501 subjects (the study cohort) [26].
• Molecular cloning and sequence analysis of the scpZ gene encoding the serine carboxypeptidase of Absidia zychae [23].

References