RETRACTED ARTICLE:Type IV collagen α1-chain noncollagenous domain blocks MMP-2
activation both in-vitro and in-vivo

Sudhakar, Yakkanti Akul; Verma, Raj Kumar; Pawar, Sunil

doi:10.1038/srep04136

Cited by 14 publications

(9 citation statements)

References 48 publications

(76 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It was first reported that metalloproteinase 9 (MMP‐9) might cleave collagen α3(IV) chain to release NC1 (non‐collagenous 1) domain, a 28‐kDa peptide, from its C‐terminus in the rat testis via proteolysis . This NC1‐peptide has also been shown to be a biologically active peptide, capable of modulating a number of cellular functions including MMP activation, cell adhesion, angiogenesis, tumorigenesis, and others based on studies in multiple endothelia and/or epithelia . Studies have shown that NC1‐peptide was also generated in the testis, capable of modulating Sertoli cell tight junction (TJ)‐permeability barrier function, and its cloning into the mammalian expression vector pCI‐neo to be used for its overexpression in Sertoli cells in vitro as well as in the testis in vivo was shown to perturb the Sertoli cell BTB function both in vitro and in vivo .…”

Section: Introductionmentioning

confidence: 99%

“…9 This NC1-peptide has also been shown to be a biologically active peptide, capable of modulating a number of cellular functions including MMP activation, cell adhesion, angiogenesis, tumorigenesis, and others based on studies in multiple endothelia and/or epithelia. [10][11][12][13] Studies have shown that NC1-peptide was also generated in the testis, capable of modulating Sertoli cell tight junction (TJ)-permeability barrier function, 14 and its cloning into the mammalian expression vector pCI-neo to be used for its overexpression in Sertoli cells in vitro as well as in the testis in vivo was shown to perturb the Sertoli cell BTB function both in vitro and in vivo. 15 These studies thus illustrate that the NC1-peptide exerts its modulating effects to support spermatogenesis are mediated through changes in the cytoskeletal organization of both actin-and MT-cytoskeletons, in particular the organization of actin filament bundles and MTs across the Sertoli cell at the ultrastructures known as the basal ectoplasmic specialization (ES) or apical ES at the Sertoli cell-cell or Sertoli-spermatid interface, respectively.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

NC1‐peptide regulates spermatogenesis through changes in cytoskeletal organization mediated by EB1

Liu

et al. 2020

FASEB j.

View full text Add to dashboard Cite

are contributed equally to the completion of this work.Abbreviations: +TIP, microtubule plus (+)-end tracking protein; AJ, adherens junction; aPKC, atypical protein kinase C; Arp3, actin-related protein 3; BM, basement membrane; BTB, blood-testis barrier; Crb3, Crumbs homolog-3; DAPI, 4', 6-diamidino-2-phenylindole; Dia1, Diaphanous-related formin-1; Dlg1, Discs large 1; Dvl3, Disheveled 3; EB1, end-binding protein 1; Eps8, epidermal growth factor receptor pathway substrate 8; ES, ectoplasmic specialization; Fzd3, Frizzled 3; F12/DMEM, Ham's F12 nutrient mixture/Dulbecco's modified Eagle's medium (1:1, vol/vol); GAPDH, glyceraldehyde 3-phosphate dehydrogenase; GJ, gap junction; H&E, hematoxylin and eosin staining; IF, immunofluorescence microscopy; IgG, immunoglobulin; IP, immunoprecipitation; MAP1a, microtubule-associated protein 1a; MARK, microtubule affinity-regulatory kinase 4; MT, microtubule; mTOR, mammalian target of rapamycin; NC1 domain, non-collagenous domain 1; Pals1, protein associated with Lin-7 1; PatJ, Pals1-associated tight junction protein; Par6, partitioning-defective (Par) protein 6; rpS6, ribosomal protein S6; TJ, tight junction; ZO-1, zonula occludens-1. AbstractDuring the epithelial cycle of spermatogenesis, different sets of cellular events take place across the seminiferous epithelium in the testis. For instance, remodeling of the blood-testis barrier (BTB) that facilitates the transport of preleptotene spermatocytes across the immunological barrier and the release of sperms at spermiation take place at the opposite ends of the epithelium simultaneously at stage VIII of the epithelial cycle. These cellular events are tightly coordinated via locally produced regulatory biomolecules. Studies have shown that collagen α3 (IV) chains, a major constituent component of the basement membrane, release the non-collagenous (NC) 1 domain, a 28-kDa peptide, designated NC1-peptide, from the C-terminal region, via the action of MMP-9 (matrix metalloproteinase 9). NC1-peptide was found to be capable of inducing BTB remodeling and spermatid release across the epithelium. As such, the NC1-peptide is an endogenously produced biologically active peptide which coordinates these cellular events across the epithelium in stage VIII tubules. Herein, we used an animal model, wherein NC1-peptide cloned into the pCI-neo mammalian expression vector was overexpressed in the testis, to better understanding the molecular mechanism by which NC1-peptide regulated spermatogenic function. It was shown that NC1-peptide induced considerable downregulation on a number of cell polarity and planar cell polarity (PCP) proteins, and studies have shown these polarity and PCP proteins modulate spermatid polarity and adhesion via their effects on microtubule (MT) and F-actin cytoskeletal organization across the epithelium. More important, NC1-peptide exerted its effects by downregulating the expression of microtubule (MT) plus-end tracking protein (+TIP) called EB1 (end-binding protein 1). We cloned the full-length EB1 cDNA for its ov...

show abstract

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

NC1‐peptide regulates spermatogenesis through changes in cytoskeletal organization mediated by EB1

Liu

et al. 2020

FASEB j.

View full text Add to dashboard Cite

show abstract

“…MMP´s can be activated by removal of the N-terminal pro-domain. They are inactivated via interaction with Tissue Inhibitors Of Matrix Metalloproteinases (TIMP`s) [10] [11] [3] [12]. …”

Section: Introductionmentioning

confidence: 99%

“…The proportion of pro-MMP-2, TIMP-2 and MT1-MMP is an important factor for the regulation of pro-MMP-2 activation and the expression of MMP-2 and TIMP-2 is connected to each other. [13] [14] [15] [10]. …”

Section: Introductionmentioning

confidence: 99%

MMP-2 Isoforms in Aortic Tissue and Serum of Patients with Ascending Aortic Aneurysms and Aortic Root Aneurysms

Tscheuschler¹,

Meffert²,

Beyersdorf³

et al. 2016

PLoS ONE

View full text Add to dashboard Cite

ObjectiveThe need for biological markers of aortic wall stress and risk of rupture or dissection of ascending aortic aneurysms is obvious. To date, wall stress cannot be related to a certain biological marker. We analyzed aortic tissue and serum for the presence of different MMP-2 isoforms to find a connection between serum and tissue MMP-2 and to evaluate the potential of different MMP-2 isoforms as markers of high wall stress.MethodsSerum and aortic tissue from n = 24 patients and serum from n = 19 healthy controls was analyzed by ELISA and gelatin zymography. 24 patients had ascending aortic aneurysms, 10 of them also had aortic root aneurysms. Three patients had normally functioning valves, 12 had regurgitation alone, eight had regurgitation and stenosis and one had only stenosis. Patients had bicuspid and tricuspid aortic valves (9/15). Serum samples were taken preoperatively, and the aortic wall specimen collected during surgical aortic repair.ResultsPro-MMP-2 was identified in all serum and tissue samples. Pro-MMP-2 was detected in all tissue and serum samples from patients with ascending aortic/aortic root aneurysms, irrespective of valve morphology or other clinical parameters and in serum from healthy controls. We also identified active MMP-2 in all tissue samples from patients with ascending aortic/aortic root aneurysms. None of the analyzed serum samples revealed signals relatable to active MMP-2. No correlation between aortic tissue total MMP-2 or tissue pro-MMP-2 or tissue active MMP-2 and serum MMP-2 was found and tissue MMP-2/pro-MMP-2/active MMP-2 did not correlate with aortic diameter. This evidence shows that pro-MMP-2 is the predominant MMP-2 species in serum of patients and healthy individuals and in aneurysmatic aortic tissue, irrespective of aortic valve configuration. Active MMP-2 species are either not released into systemic circulation or not detectable in serum. There is no reliable connection between aortic tissue—and serum MMP-2 isoforms, nor any indication that pro-MMP-2 functions as a common marker of high aortic wall stress.

show abstract

“…Matrix metalloproteinases (MMPs) are known to play a critical role in tumour progression, invasiveness, and metastasis 27 and are promising tumour biomarkers overexpressed in most cancers 28 . MMPs degrade collagen type IV and further enable the escape of cancer cells to other organs 29 . Additionally, MMP probes have been shown to decrease the incidence of positive margins and increase tumour-free survival after dissections.…”

mentioning

confidence: 99%

Increased precision of orthotopic and metastatic breast cancer surgery guided by matrix metalloproteinase-activatable near-infrared fluorescence probes

Chi

Zhang

Mao

et al. 2015

Sci Rep

View full text Add to dashboard Cite

Advanced medical imaging technology has allowed the use of fluorescence molecular imaging-guided breast cancer surgery (FMI-guided BCS) to specifically label tumour cells and to precisely distinguish tumour margins from normal tissues intra-operatively, a major challenge in the medical field. Here, we developed a surgical navigation system for real-time FMI-guided BCS. Tumours derived from highly metastatic 4T1-luc breast cancer cells, which exhibit high expression of matrix metalloproteinase (MMP) and human epidermal growth factor receptor 2 (HER2), were established in nude mice; these mice were injected with smart MMP-targeting and “always-on” HER2-targeting near-infrared (NIR) fluorescent probes. The fluorescence signal was imaged to assess in vivo binding of the probes to the tumour and metastatic sites. Then, orthotopic and metastatic breast tumours were precisely removed under the guidance of our system. The post-operative survival rate of mice was improved by 50% with the new method. Hematoxylin and eosin staining and immunohistochemical staining for MMP2 and CD11b further confirmed the precision of tumour dissection. Our method facilitated the accurate detection and complete removal of breast cancer tumours and provided a method for defining the molecular classification of breast cancer during surgery, thereby improving prognoses and survival rates.

show abstract

RETRACTED ARTICLE:Type IV collagen α1-chain noncollagenous domain blocks MMP-2 activation both in-vitro and in-vivo

Cited by 14 publications

References 48 publications

NC1‐peptide regulates spermatogenesis through changes in cytoskeletal organization mediated by EB1

NC1‐peptide regulates spermatogenesis through changes in cytoskeletal organization mediated by EB1

MMP-2 Isoforms in Aortic Tissue and Serum of Patients with Ascending Aortic Aneurysms and Aortic Root Aneurysms

Increased precision of orthotopic and metastatic breast cancer surgery guided by matrix metalloproteinase-activatable near-infrared fluorescence probes

Contact Info

Product

Resources

About