P14; Procollagen COOH-terminal proteinase enhancer 1;PCPE-1Procollagen C-proteinase enhancer 1 Type 1 procollagen C-proteinase enhancer protein; Type I procollagen COOH-terminal proteinase enhancer;Flags: Precursor
Organism
Mus musculus (Mouse)
NCBI Taxonomy ID
10090
Chromosome Location
chr:5;138046331-138055012;-1
View in Ensembl genome browser
Function in Stage
Uncertain
Function in Cell Type
Uncertain
Probability (GAS) of Function in Spermatogenesis
0.145775341 The probability was calculated by GAS algorithm, ranging from 0 to 1. The closer it is to 1, the more possibly it functions in spermatogenesis.
Description
Temporarily unavailable
Abstract of related literatures
1. Type I procollagen COOH-terminal proteinase (C-proteinase) enhancer, a glycoprotein that binds to the COOH-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity, was purified from mouse fibroblast culture media. Partial amino acid sequences obtained from proteolytic fragments were found to have identity with the deduced amino acid sequence of a cDNA clone of unknown function, previously isolated from a mouse astrocyte library. Sequences of mouse enhancer cDNA, obtained in the present study, predict a approximately 50-kDa, 468-amino acid protein that differs from the 43-kDa, 402-amino acid protein predicted by the previously reported astrocyte-derived clone. Human cDNAs encode an enhancer of 449 amino acids. Previous biochemical studies have found the mouse enhancer as a 55-kDa form, which is readily processed to 36- and 34-kDa forms, retaining full C-proteinase enhancing activity and the ability to bind the COOH-terminal propeptide. Data presented here show the 36-kDa form to correspond to the amino-terminal portion of the 55-kDa protein. This is the most conserved region between mouse and human enhancers, comprising two domains with homology to domains found in a number of proteases and proteins with developmental functions. Such domains are thought to mediate interactions between proteins. Mouse enhancer RNA is shown to be at highest levels in collagen-rich tissues, especially tendon. The human enhancer gene, PCOLCE, is localized to 7q21.3-->q22, the same chromosomal region containing the type I collagen alpha 2 chain gene, COL1A2. PMID: [7523404]
2. The CNS is composed of neurons and glial cells (i.e., astrocytes, oligodendrocytes, and microglia). The brain communicates with the blood circulation through choroid plexus and meninges as well as through the blood-brain barrier. To identify transcripts specifically expressed in a distinct brain cell type, we have previously constructed a subtracted cDNA library from the poly(A)+ RNAs of a velate protoplasmic-like astrocytic cell line, designated D19. This library was screened in order to isolate transcripts over-expressed in this astroglial cell line versus another astroglial cell line. Of the six recombinants which have been isolated, three sequences have not been described. Their sizes ranged from 100 to 200 bp and they hybridized to mRNAs expressed in vivo inside and outside the CNS. We have constructed a size-selected D19 cDNA library in order to obtain the full length cDNAs corresponding to the three undescribed sequences. We report here the isolation of a 1.6 kb cDNA corresponding to one of these recombinants, named p14. Its sequence has not yet been described and its deduced amino acid sequence codes for a 43 kDa protein with a putative signal peptide. In situ hybridization shows that this transcript is expressed at a high level in choroid plexus and leptomeninges and also in perivascular cells in the adult mouse brain. It is also expressed in cell subsets of kidney and gonads as well as in perivascular cells in skeletal and cardiac muscles. These localizations suggest that the encoded protein might be involved in transport processes and hormonally controlled. PMID: [2027019]
3. The enzyme procollagen C-proteinase removes the carboxy-terminal propeptide from procollagen. In the present study we describe an improved procedure for the purification of this enzyme. From the medium of cultured mouse fibroblasts, consisting of ammonium sulfate precipitation, gel filtration and affinity chromatography on a lysyl-Sepharose column, followed by chromatography on a column of Sepharose coupled to the carboxy-terminal propeptide of type I procollagen (PP-Sepharose). This procedure yielded a practically homogeneous, 18,500-fold-purified enzyme preparation and the molecular mass of the purified C-proteinase as determined by sodium dodecyl sulfate/polyacrylamide gel electrophoresis was 80 kDa. The lysyl-Sepharose step separated the enzyme from the majority of the contaminating proteins, including a 55-kDa protein which was further purified by PP-Sepharose chromatography and identified as an additional form of the 36-kDa and 34-kDa procollagen C-proteinase enhancer proteins described before [Adar et al. (1986) Collagen Relat. Res. 6,267-277]. It enhanced the C-proteinase activity, bound to the carboxyl propeptide of type I procollagen, cross-reacted immunologically with the 36-kDa as well as the 34-kDa enhancer proteins, and in common with the latter proteins, it was glycosylated. In the course of PP-Sepharose chromatography, a large proportion of the 55-kDa protein disappeared with the concomitant appearance of the smaller enhancer proteins. All these findings suggest that the 55-kDa protein is a precursor of the low molecular mass enhancer proteins. Also suggested from this study is that lysyl-Sepharose chromatography is a highly beneficial purification step which may find use in the purification of the C-proteinase from other sources as well. PMID: [2689170]
4. Using antibodies to the procollagen C-proteinase enhancer of mouse fibroblast culture medium, we have screened by immunoblotting extracts of several post natal mouse and rat tissues for the presence of the enhancer antigen. All rodent connective tissues were relatively rich in enhancer; lower amounts were found in skeletal muscle and heart and essentially no enhancer was detected in kidney, liver or brain. The amounts of enhancer in mouse tendon and calvaria extracts were age related, with highest amounts in 11 and 19 d tendons and in 1 d calvaria-the times of rapid growth of these organs. The results suggest that procollagen C-proteinase enhancer is a specific connective tissue glycoprotein that is likely to regulate procollagen processing in vivo. PMID: [2256940]