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Last update 23 Jan 2025

Collagen x FN1 x laminin

Last update 23 Jan 2025

Basic Info

Related Targets

CollagenFN1laminin

Drugs associated with Collagen x FN1 x laminin

Ocriplasmin

Target

Collagen x FN1 x laminin

Mechanism

Collagen inhibitors [+2]

Active Org.

Thrombogenics, Inc. [+2]

Originator Org.

Thrombogenics, Inc.

Active Indication

Vitreomacular traction [+1]

Inactive Indication

Acute Ischemic Stroke [+11]

Drug Highest PhaseApproved

First Approval Ctry. / Loc.

First Approval Date17 Oct 2012

Clinical Trials associated with Collagen x FN1 x laminin

EUCTR2015-005473-20-BE

/ Not yet recruitingPhase 2

Pilot study on robot assisted retinal vein cannulation with ocriplasmin infusion for central retinal vein occlusion.

Start Date23 Nov 2016

Sponsor / Collaborator

UZ Leuven

NCT02681809

/ TerminatedPhase 2

A Phase 2, Randomised, Double Masked, Sham Controlled, Multicentre Study to Evaluate the Efficacy and Safety of Ocriplasmin in Inducing Total Posterior Vitreous Detachment (PVD) in Subjects With Non-proliferative Diabetic Retinopathy (NPDR)

The purpose of this study is to assess the efficacy and safety of up to 3 intravitreal injections of ocriplasmin (0.0625mg or 0.125mg), in subjects with moderate to very severe non-proliferative diabetic retinopathy (NPDR), to induce total posterior vitreous detachment (PVD) in order to reduce the risk of disease progression to proliferative diabetic retinopathy (PDR).

Start Date01 Dec 2015

Sponsor / Collaborator

Thrombogenics, Inc.

NCT02035748

/ CompletedPhase 4

Assessment of Anatomical and Functional Outcomes in Patients Treated With Ocriplasmin for Vitreomacular Traction/Symptomatic Vitreomacular Adhesion (VMT/sVMA)

The purpose of this study is to observe the anatomical and functional outcomes of ocriplasmin (JETREA®) over a 6-month follow-up period.

Start Date01 Apr 2014

Sponsor / Collaborator

Alcon Research Ltd.

100 Clinical Results associated with Collagen x FN1 x laminin

100 Translational Medicine associated with Collagen x FN1 x laminin

0 Patents (Medical) associated with Collagen x FN1 x laminin

2,022

Literatures (Medical) associated with Collagen x FN1 x laminin

01 Dec 2025·Molecular Biology Reports

Enhanced post-thaw functional characteristics of cryopreserved caprine dermal fibroblasts through adhesion to extracellular matrix proteins

Article

Author: Singh, Manoj Kumar ; Pathak, Manisha ; Soni, Yogesh Kumar ; Goel, Anjana ; Pathak, Juhi ; Singh, Shiva Pratap

BACKGROUNDExtracellular matrix (ECM) proteins play a crucial role in regulating the biological properties of adherent cells. For cryopreserved fibroblasts, a favourable ECM environment can help restore their natural morphology and function more rapidly, minimizing post-thaw stress responses.METHODS AND RESULTSThis study explored the functional responses of cryopreserved enriched caprine adult dermal fibroblast (cadFibroblast) cells to structural [collagen-IV and rat tail collagen (RTC)] and adhesion ECM proteins (laminin, fibronectin, and vitronectin) under in vitro culture conditions. The cryopreserved cadFibroblasts were evaluated for cell morphology, confluence, viability, cell adhesion, colony-forming units, proliferation, population doubling time migration (scratch wound healing assay), and quantitative real-time PCR for gene expression analyses when cultivated on surfaces coated with ECM proteins. A significantly (p < 0.05) higher cellular responses regarding cell adhesion ability, proliferation, CFUs, migration rate and differential gene expression of cell adhesion (β integrin, β tubulin, and E-cadherin) associated marker genes were observed with adhesion ECM proteins (laminin, fibronectin, and vitronectin) than with structural ECM proteins (collagen-IV and RTC). RT-PCR analyses revealed ECM-dependent differential template expression in cultured post-thawed cadFibroblasts.CONCLUSIONSOverall, while comparing different types of ECM proteins, adhesion ECM proteins (laminin, fibronectin, and vitronectin) provide a relatively better niche that supports adhesion, growth, proliferation, and migration of post-thawed cadFibroblasts compared with structural ECM proteins (collagen-IV and RTC) and the culture without ECM. The outcomes of the present study are crucial for replicating physiological conditions in experimental models for future research involving cryopreserved dermal fibroblasts or any other cell type, which can lead to future developments in tissue engineering and regenerative medicine.

01 Jan 2025·Theriogenology

Characterization of decellularized porcine oviduct- and uterine-derived scaffolds evaluated by spermatozoa-based biocompatibility and biotoxicity

Article

Author: Navarro, María Cortina ; Izquierdo-Rico, Mª José ; Izquierdo-Rico, Ma José ; García-Vázquez, Francisco Alberto ; Martínez-Cáceres, Carlos Manuel ; Cortina-Navarro, María ; Martínez-López, Cristina

Decellularized extracellular matrix (dECM) are widely utilized in regenerative medicine and tissue engineering due to their ability to promote cell growth, proliferation, and differentiation. In reproduction, research is focused on the utilization of these scaffolds to treat pathologies causing reproductive dysfunction or to improve assisted reproduction technologies (ARTs). We developed an efficient protocol employing the immersion-agitation technique to decellularize porcine oviductal and uterine sections, comparing the efficacy of fresh versus frozen treatments. Both methods successfully generated acellular matrices with less than 3 % residual DNA, effectively preserving structural and protein integrity. Scanning and transmission electron microscopy confirmed the ultrastructural integrity, whereas Masson's Trichrome staining highlighted better collagen preservation in frozen treatments. Proteomic analysis of decellularized scaffolds revealed collagen and key macromolecules such as laminin, filamin, dermatopontin, and fibronectin, which are essential for extracellular matrix structure and cell functions such as adhesion and migration. Innovatively, we assessed the biocompatibility and cytotoxicity of the scaffolds using spermatozoa, demonstrating that thorough washing ensures the scaffold biocompatibility without compromising sperm viability or motility. Our findings not only contribute to the standardization of decellularization protocols for female reproductive organs but also emphasize the importance of evaluating sperm biocompatibility to ensure the safety of dECM scaffolds.

08 Nov 2024·Biological and Pharmaceutical Bulletin

Downregulation of Genes for Skeletal Muscle Extracellular Matrix Components by Cisplatin

Article

Author: Nanri, Hayato ; Sakai, Hiroyasu ; Ikarashi, Nobutomo ; Kiyama, Miho ; Ogiwara, Takayuki ; Chiba, Yoshihiko ; Hosoe, Tomoo ; Kon, Risako ; Miyauchi, Yu ; Soga, Shinki ; Yonamine, Shiori

The extracellular matrix (ECM) in skeletal muscle is involved in a variety of physiological functions beyond the mechanical support of muscle tissue, nerves, and blood vessels; however, the role of the ECM in skeletal muscle remains unclear. There is little information regarding changes in the expression of factors comprising the ECM during cisplatin-induced muscle atrophy. In the present study, we examined the changes in gene expressions for skeletal muscle extracellular matrix components in skeletal muscle during cisplatin-induced muscle atrophy. Intraperitoneal administration of cisplatin caused muscle atrophy in mice and during this cisplatin-induced muscle atrophy, the expression of many procollagen genes (Col1a1, Col1a2, Col3a1, Col4a1, Col5a1, and Col5a2), elastin (Eln), fibronectin (Fn1), Laminin (Lama1, Lama2, and Lamb1) decorin (Dcn), heparan sulphate proteoglycans (Hspg2) and integrin (Itgb1) constituting the ECM was suppressed. Additional studies are needed to elucidate the pathological significance and mechanisms of reduced gene expression of ECM components associated with cisplatin-induced muscle atrophy.

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