Last update 01 Nov 2024

PCOLCE

Last update 01 Nov 2024

Basic Info

Synonyms

PCOLCE, PCPE, PCPE-1

+ [7]

Introduction

Binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity. C-terminal processed part of PCPE (CT-PCPE) may have an metalloproteinase inhibitory activity.

Drugs associated with PCOLCE

CN114903974

Patent Mining

Target

PCOLCE

Mechanism-

Active Org.

Mudanjiang Medical University

Originator Org.

Mudanjiang Medical University

Active Indication

Connective and Soft Tissue Neoplasms

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with PCOLCE

100 Translational Medicine associated with PCOLCE

0 Patents (Medical) associated with PCOLCE

125

Literatures (Medical) associated with PCOLCE

01 Dec 2024·Matrix Biology

PCPE-2 (procollagen C-proteinase enhancer-2): The non-identical twin of PCPE-1

Review

Author: Moali, Catherine ; Bauer, Julien ; Bonod, Christelle ; Napoli, Manon ; Goff, Sandrine Vadon-Le

PCPE-2 was discovered at the beginning of this century, and was soon identified as a close homolog of PCPE-1 (procollagen C-proteinase enhancer 1). After the demonstration that it could also stimulate the proteolytic maturation of fibrillar procollagens by BMP-1/tolloid-like proteinases (BTPs), PCPE-2 did not attract much attention as it was thought to fulfill the same functions as PCPE-1 which was already well-described. However, the tissue distribution of PCPE-2 shows both common points and significant differences with PCPE-1, suggesting that their activities are not fully overlapping. Also, the recently established connections between PCPE-2 (gene name PCOLCE2) and several important diseases such as atherosclerosis, inflammatory diseases and cancer have highlighted the need for a thorough reappraisal of the in vivo roles of this regulatory protein. In this context, the recent finding that, while retaining the ability to bind fibrillar procollagens and to activate their C-terminal maturation, PCPE-2 can also bind BTPs and inhibit their activity has substantially extended its potential functions. In this review, we describe the current knowledge about PCPE-2 with a focus on collagen fibrillogenesis, lipid metabolism and inflammation, and discuss how we could further advance our understanding of PCPE-2-dependent biological processes.

01 Oct 2024·Journal of Lipid Research

PCPE2: Expression of Multifunctional Extracellular Glycoprotein Associates With Diverse Cellular Functions

Review

Author: Sorci-Thomas, Mary G ; Thomas, Michael J. ; Xu, Hao ; Thomas, Michael J ; Wang, Angela ; Sorci-Thomas, Mary G.

Procollagen C-endopeptidase enhancer 2, known as PCPE2 or PCOC2 (gene name, PCOLCE2) is a glycoprotein that resides in the extracellular matrix, and is similar in domain organization to PCPE1 / PCPE, PCOC1 (PCOLCE1 /PCOLCE). Due to the many similarities between the two related proteins, PCPE2 has been assumed to have biological functions similar to PCPE. PCPE is a well-established enhancer of procollagen processing activating the enzyme, BMP-1. However, reports show that PCPE2 has a strikingly different tissue expression profile compared to PCPE. With that in mind and given the paucity of published studies on PCPE2, this review examines the current literature citing PCPE2 and its association with specific cell types and signaling pathways. Additionally, this review will present a brief history of PCPE2's discovery, highlighting structural and functional similarities and differences compared to PCPE. Considering the widespread use of RNA sequencing techniques to examine associations between cell-specific gene expression and disease states, we will show that PCPE2 is repeatedly found as a differentially regulated gene (DEG) significantly associated with a number of cellular processes, well beyond the scope of procollagen fibril processing.

01 Oct 2024·Molecular Neurobiology

SOX9 Promotes Collagen VI Secretion by Upregulating PCOLCE in Neurofibroma

Article

Author: Bing, Zhitong ; Wang, Jianying ; Yuan, Guoqiang ; Wang, Bo ; Yao, Xuan ; Yin, Hang ; Su, Yuanping ; Pan, Yawen ; Li, Qiao ; Dong, Qiang

Neurofibromatosis type 1 (NF1) is caused by NF1 gene mutations. Patients with NF1 often have complications with tumors, such as neurofibroma. In order to investigate the pathogenesis of human neurofibroma, a systematic comparison of protein expression levels between Schwann cell-like sNF96.2 cells, which originated from malignant peripheral nerve sheath tumors (MPNST), and normal Schwann cells was performed using 4-D label-free proteomic analysis. In addition, the expression levels and localization of dysregulated proteins were confirmed using a Gene Expression Omnibus (GEO) transcriptomic dataset, Western blot analysis, and immunofluorescence labeling. The effects of SRY-box transcription factor 9 (SOX9) in the neurofibroma and surrounding microenvironment were evaluated in vivo using a tumor transplantation model. The present study observed that SOX9 and procollagen C-endopeptidase enhancer (PCOLCE) were significantly altered. NF1 mutation promoted the nuclear translocation and transcriptional activity of SOX9 in neurofibromas. SOX9 increased collagen VI secretions by enhancing the activation of PCOLCE in neurofibroma cells. These findings might provide new perspectives on the pathophysiological significance of SOX9 in neurofibromas and elucidate a novel molecular mechanism underlying neurofibromas.

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PCOLCE

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