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Related Concept Videos

Role of Matrix Metalloproteases in Degradation of ECM01:23

Role of Matrix Metalloproteases in Degradation of ECM

Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult body.
A...
The Extracellular Matrix01:29

The Extracellular Matrix

Overview
In order to maintain tissue organization, many animal cells are surrounded by structural molecules that make up the extracellular matrix (ECM). Together, the molecules in the ECM maintain the structural integrity of tissue as well as the remarkable specific properties of certain tissues.
Composition of the Extracellular Matrix
The extracellular matrix (ECM) is commonly composed of ground substance, a gel-like fluid, fibrous components, and many structurally and functionally diverse...
The Extracellular Matrix01:42

The Extracellular Matrix

In order to maintain tissue organization, many animal cells are surrounded by structural molecules that make up the extracellular matrix (ECM). Together, the molecules in the ECM maintain the structural integrity of tissue as well as the remarkable specific properties of certain tissues.Composition of the Extracellular MatrixThe extracellular matrix (ECM) is commonly composed of ground substance, a gel-like fluid, fibrous components, and many structurally and functionally diverse molecules.
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
Extracellular Matrix01:26

Extracellular Matrix

Unlike epithelial tissue, which is composed of cells closely packed with little or no extracellular space in between, connective tissue cells are dispersed in a matrix. This extracellular matrix (ECM) is composed of fibrous proteins like collagen, elastin, and fibronectin in a ground substance consisting of interstitial fluid, cell adhesion proteins, and proteoglycans. The proteoglycans form a gel-like material in the spaces between cells and provide hydration, buffering, binding, and force...
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...

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Related Experiment Video

Updated: Jul 5, 2026

Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography
07:32

Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography

Published on: March 30, 2022

RECK, a novel matrix metalloproteinase regulator.

N Meng1, Y Li, H Zhang

  • 1Department of Surgery, The Forth Hospital of Hebei Medical University, Shijiazhuang, Hebei Province, China.

Histology and Histopathology
|May 24, 2008
PubMed
Summary

The reversion-inducing-cysteine-rich protein with kazal motifs (RECK) regulates matrix metalloproteinases (MMPs). This review explores RECK

Area of Science:

  • Biochemistry
  • Cell Biology
  • Oncology

Background:

  • Extracellular matrix (ECM) macromolecules are crucial for tissue development and morphogenesis.
  • Matrix metalloproteinases (MMPs), Zn-dependent endopeptidases, degrade ECM and are implicated in physiological and pathological processes.
  • RECK (reversion-inducing-cysteine-rich protein with kazal motifs) is a newly identified membrane-anchored regulator of MMPs.

Purpose of the Study:

  • To review the structure, function, and regulation of RECK.
  • To highlight RECK's role in malignant transformation and its potential as a therapeutic target.
  • To provide insights into future research directions for RECK.

Main Methods:

  • Literature review focusing on RECK's molecular characteristics.

More Related Videos

Detection of Functional Matrix Metalloproteinases by Zymography
09:30

Detection of Functional Matrix Metalloproteinases by Zymography

Published on: November 8, 2010

Related Experiment Videos

Last Updated: Jul 5, 2026

Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography
07:32

Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography

Published on: March 30, 2022

Detection of Functional Matrix Metalloproteinases by Zymography
09:30

Detection of Functional Matrix Metalloproteinases by Zymography

Published on: November 8, 2010

  • Analysis of RECK's involvement in cellular processes, particularly cancer.
  • Synthesis of current knowledge on RECK's regulatory mechanisms.

    • Main Results:

    • RECK exhibits a unique structure with kazal motifs, enabling its function as an MMP inhibitor.
    • RECK expression is downregulated during malignant transformation, suggesting a tumor-suppressive role.
    • RECK's activity is modulated by various signaling pathways.

    Conclusions:

    • RECK is a significant regulator of MMPs with a critical role in maintaining tissue homeostasis.
    • The downregulation of RECK in cancer presents it as a promising target for anti-tumor therapies.
    • Further research into RECK's structure-function relationship and regulatory networks is warranted for therapeutic development.