Spasmolytic Polypeptide Metaplasia

Spasmolytic Polypeptide Metaplasia (SPEM) is a gastric epithelial response in which mature chief cells acquire mucous neck cell-like characteristics after injury, and it matters because it is associated with chronic atrophy and gastric cancer development. Parietal-cell loss, inflammation, and tissue damage can alter the glandular environment, promoting cellular reprogramming and expression of mucous-lineage markers such as trefoil factor 2 and MUC6. In cancer research, SPEM provides a model for studying metaplasia, tissue repair, and progression toward dysplasia in the stomach. Characterizing its cellular origins and signaling pathways may clarify how persistent inflammation reshapes gastric epithelium and help identify biomarkers or intervention points for cancer prevention.

Spasmolytic Polypeptide Metaplasia - Related Videos

Research

JoVE Journal - Biology
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Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli

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Cited by 48 •

2014

Elastin-like polypeptides are stimulus-responsive biopolymers with applications ranging from recombinant protein purification to drug delivery. This protocol describes the purification and characterization of elastin-like polypeptides and their peptide or protein fusions from Escherichia coli using their lower critical solution temperature phase transition behavior as a simple alternative to chromatography.

Education

JoVE Core - Pharmacology

Spasmolytic Agents: Chemical Classification

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2023

Spasmolytic agents are drugs used to alleviate muscle spasms and spasticity. They can be categorized into different chemical groups based on their mechanisms of action. Centrally acting spasmolytics primarily affect the spinal cord, while others directly target skeletal muscle cells. A major class of centrally acting spasmolytics is the α2-agonist, such as tizanidine. These drugs bind to α2-adrenoceptors, inhibiting the release of the excitatory neurotransmitter glutamate. They also promote...

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides

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Cited by 6 •

2012

We describe here a technique that is now routinely used to isolate stably bound ribosome nascent chain complexes (RNCs). This technique takes advantage of the discovery that a 17 amino acid long SecM "arrest sequence" can halt translation elongation in a prokaryotic (E. coli) system, when inserted into (or fused to the C-terminus) of virtually any protein.

Acinar-to-Ductal Metaplasia Induction: A Method to Study Acinar Cell to Ductal Cell Differentiation in 3D Ex Vivo Culture

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2023

This video describes the technique of differentiating pancreatic acinar cells to ductal cells in ex vivo 3D culture. This helps to understand the mechanisms regulating the acinar-to-ductal metaplasia (ADM), a key process in the early development of pancreatic cancer.

Isolation of Ribosome Bound Nascent Polypeptides in vitro to Identify Translational Pause Sites Along mRNA

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Cited by 2 •

2012

A technique to identify translational pause sites on mRNA is described. This procedure is based on isolation of nascent polypeptides accumulating on ribosomes during in vitro translation of a target mRNA, followed by the size analysis of the nascent chains using a denaturing gel electrophoresis.

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