Applying Proteomics to Investigate Extracellular Matrix in Health and Disease

Randles, Michael J.; Lennon, Rachel

doi:10.1016/bs.ctm.2015.06.001

Cited by 16 publications

(9 citation statements)

References 43 publications

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“…The basement membranes that line cerebral blood vessels consist of collagen IV, laminins and heparan sulfate proteoglycans (HSPGs) perlecan and agrin (39,40). In the brain, neural interstitial matrix separates cells and consists of networks of chondroitin sulfate proteoglycans (CSPGs), tenascins, hyaluronan, and link proteins.…”

Section: Proteomics Glycomics and Glycoproteomics Of Matrisome Molementioning

confidence: 99%

Proteomics, Glycomics, and Glycoproteomics of Matrisome Molecules

Raghunathan¹,

Sethi²,

Klein³

et al. 2019

Molecular & Cellular Proteomics

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In Brief Extracellular networks of matrisome proteins and their binding partners give rise to dynamic cell and tissue-specific microenvironments. The extreme complexity of matrisome molecule glycosylation and other post-translational modifications belies the need for specialized omics methods. It is necessary to map the modifications of matrisome molecules in detail in order to understand their roles in normal and pathological physiology. We review proteomics, glycomics and glycoproteomics methods for matrisome molecules toward the goal of achieving detailed matrisome maps. Highlights • Highly glycosylated matrisome proteins and their binding partners comprise extracellular networks that mediate tissue-specific cellular microenvironments. • Elucidation of roles of matrisome molecules in disease mechanisms requires detailed mapping of matrisome glycosylation and other post-translational modifications. • We review tissue workup methods for matrisome proteomics, glycomics and glycoproteomics. • The combination of proteomics, glycomics and glycoproteomics profiles matrisome protein modifications distinct from those studied by immunohistochemistry.

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Section: Proteomics Glycomics and Glycoproteomics Of Matrisome Molementioning

confidence: 99%

Proteomics, Glycomics, and Glycoproteomics of Matrisome Molecules

Raghunathan¹,

Sethi²,

Klein³

et al. 2019

Molecular & Cellular Proteomics

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“…Several mass-spectrometry(MS)-based proteomic studies have found predominant ECM components in connective tissues and basal membranes, including collagen I, III, IV, VIII, XII, XIV, and XXI types, laminins, nidogens, fibronectin, vimentin, perlecan, prolargin, versican, matriline, tenascins, thrombospondin, decorin, and fibromodulin. 36 , 37 The maintenance of homeostasis and ECM turnover is involved in several factors and mechanisms. This comprises complex interactions between matrix metalloproteinases (MMP) and tissue inhibitors of matrix metalloproteinases (TIMP).…”

Section: Introductionmentioning

confidence: 99%

New insights into the pathogenesis of Peyronie's disease: A narrative review

Krakhotkin¹,

Chernylovskyi²,

Mottrie

et al. 2020

Chronic Diseases and Translational Medicine

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Peyronie’s disease (PD) is a benign, progressive fibrotic disorder characterized by scar or plaques within the tunica albuginea (TA) of the penis. This study provides new insights into the pathogenesis of PD based on data from different studies regarding the roles of cytokines, cell signaling pathways, biochemical mechanisms, genetic factors responsible for fibrogenesis. A growing body of literature has shown that PD is a chronically impaired, localized, wound healing process within the TA and the Smith space. It is caused by the influence of different pathological stimuli, most often the effects of mechanical stress during sexual intercourse in genetically sensitive individuals with unusual anatomical TA features, imbalanced matrix metalloproteinase/tissue inhibitor of metalloproteinase (MMP/TIMP), and suppressed antioxidant systems during chronic inflammation. Other intracellular signal cascades are activated during fibrosis along with low expression levels of their negative regulators and transforming growth factor-β1 signaling. The development of multikinase agents with minimal side effects that can block several signal cell pathways would significantly improve fibrosis in PD tissues by acting on common downstream mediators.

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“…Identification and quantification of the components of distinct extracellular matrix (ECM) proteins and comprehension of their underpinning network interactions represent key steps towards elucidating the role of the ECM in health and pathological conditions [1,2]. Proteomics offers an opportunity to address these challenges in a global and unbiased manner, without the need for hypothesis-driven molecular candidates.…”

Section: Introductionmentioning

confidence: 99%

Divide-and-Conquer Matrisome Protein (DC-MaP) Strategy: An MS-Friendly Approach to Proteomic Matrisome Characterization

Ouni

Ruys

Dolmans

et al. 2020

IJMS

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Currently, the extracellular matrix (ECM) is considered a pivotal complex meshwork of macromolecules playing a plethora of biomolecular functions in health and disease beyond its commonly known mechanical role. Only by unraveling its composition can we leverage related tissue engineering and pharmacological efforts. Nevertheless, its unbiased proteomic identification still encounters some limitations mainly due to partial ECM enrichment by precipitation, sequential fractionation using unfriendly-mass spectrometry (MS) detergents, and resuspension with harsh reagents that need to be entirely removed prior to analysis. These methods can be technically challenging and labor-intensive, which affects the reproducibility of ECM identification and induces protein loss. Here, we present a simple new method applicable to tissue fragments of 10 mg and more. The technique has been validated on human ovarian tissue and involves a standardized procedure for sample processing with an MS-compatible detergent and combined centrifugation. This two-step protocol eliminates the need for laborious sample clarification and divides our samples into 2 fractions, soluble and insoluble, successively enriched with matrisome-associated (ECM-interacting) and core matrisome (structural ECM) proteins.

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Applying Proteomics to Investigate Extracellular Matrix in Health and Disease

Cited by 16 publications

References 43 publications

Proteomics, Glycomics, and Glycoproteomics of Matrisome Molecules

Proteomics, Glycomics, and Glycoproteomics of Matrisome Molecules

New insights into the pathogenesis of Peyronie's disease: A narrative review

Divide-and-Conquer Matrisome Protein (DC-MaP) Strategy: An MS-Friendly Approach to Proteomic Matrisome Characterization

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